text:
Life in Pieces
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Life in Pieces
Genre
Sitcom
Created by
Justin Adler
Starring
Colin Hanks
Betsy Brandt
Thomas Sadoski
Zoe Lister-Jones
Dan Bakkedahl
Angelique Cabral
Niall Cunningham
Holly Barrett
Giselle Eisenberg
James Brolin
Dianne Wiest
Hunter King
Ana Sophia Heger
Composer(s)
Rob Simonsen
Country of origin
United States
Original language(s)
English
No. of seasons
3
No. of episodes
53 (list of episodes)
Production
Executive producer(s)
Justin Adler
Aaron Kaplan
Jeff Morton
Jason Winer
Camera setup
Single-camera
Running time
21 minutes
Production company(s)
Kapital Entertainment
40 or 50 Years, Inc.
20th Century Fox Television
Distributor
20th Television
Release
Original network
CBS
Picture format
HDTV 1080i
Original release
September 21, 2015 (2015-09-21) – present
External links
Website
www.cbs.com/shows/life-in-pieces/
Life in Pieces is an American sitcom television series created by Justin Adler and airs on CBS.[1] The series debuted on September 21, 2015. The first season was picked up for a full 22-episode order on October 27, 2015.[2] On May 11, 2016, CBS renewed the show for a second season,[3] which premiered on October 27, 2016.[4]
On March 23, 2017, CBS renewed the series for a third season, which premiered on November 2, 2017.[5][6]
Contents
[hide]
1 Premise
2 Cast
2.1 Main cast
2.2 Recurring cast
3 Episodes
4 Broadcast
5 Reception
5.1 Ratings
6 References
7 External links
Premise[edit]
The series chronicles the lives of three generations of the Short family as they go about their daily lives in Los Angeles County. Each episode is told as four short stories, one for each branch of the Short family.[7]
Cast[edit]
Main cast[edit]
Colin Hanks as Greg Short:[8]
Husband of Jen Short; youngest child and younger son of John and Joan Short; younger brother of Matt Short and Heather (Short) Hughes; father of daughter Lark Short; worked for a crowd funding website until he quit his job in "Crytunes Divorce Tablet Ring".
Betsy Brandt as Heather (Short) Hughes:[8]
Wife of Dr. Tim Hughes; oldest child and only daughter of John and Joan Short; older sister of Matt and Greg Short; mother of Tyler, Samantha, and Sophia Hughes; a stay at home mom
Thomas Sadoski as Matthew "Matt" Short:[8]
Recently divorced; middle child and oldest son of John and Joan Short; brother of Heather and Greg Short; dated Colleen Brandon Ortega until the end of "Hair Recital Rainbow Mom". He and Colleen got back together in "Cinderella Fantasy Prom Dougie". They got engaged in the second half of the two-part season 1 finale, "Crytunes Divorce Tablet Ring".
Zoe Lister-Jones as Jennifer "Jen" Collins Short:[8]
A lawyer; mother of daughter Lark; wife of Greg Short. She announced that she is pregnant with their second child in season 1 finale, "Crytunes Divorce Tablet Ring"; however, it was later revealed that she had a miscarriage in the season 2 premiere, "Annulled Roommate Pill Shower".
Dan Bakkedahl as Dr. Timothy "Tim" Hughes, M.D.:[8]
An ENT doctor; husband of Heather (Short) Hughes; father of Tyler, Samantha, and Sophia Hughes
Angelique Cabral as Colleen Brandon Ortega:[8]
Granddaughter of Tonita; owns a male puppy named "Princess"; dated Matt Short until the end of "Hair Recital Rainbow Mom". She and Matt got back together in "Cinderella Fantasy Prom Dougie". They got engaged in "Crytunes Divorce Tablet Ring".
Niall Cunningham as Tyler Hughes:[8]
Oldest child and only son of Tim and Heather Hughes; brother of Samantha and Sophia Hughes; dated Clementine from "Babe Secret Phone Germs" until they married before "Crytunes Divorce Tablet Ring". Beginning of season 3, they are getting divorced. It was mutual and decided to become friends.
Holly Barrett as Samantha "Sam" Hughes:[8]
Middle child and older daughter of Tim and Heather Hughes; sister of Tyler and Sophia Hughes
Giselle Eisenberg as Sophia Hughes:[8]
Youngest child and younger daughter of Tim and Heather Hughes; sister of Tyler and Samantha Hughes
James Brolin as John Bertram Short:[8]
Retired airline pilot; partner of Joan (Pirkle) Short; father of Heather (Short) Hughes, Matt Short, and Greg Short; owns a female Yorkie named Tank since "Sexting Mall Lemonade Heartbreak".
Dianne Wiest as Dr. Joan (Pirkle) Short:[8]
Partner of John Short; therapist; daughter of GiGi Pirkle; mother of Heather (Short) Hughes, Matt Short, and Greg Short. She and John are still together but, in "Crytunes Divorce Tablet Ring", they confessed to their kids that they got divorced in 1980 in protest when their best friends, a lesbian couple, couldn't get married.
Hunter King as Clementine Hughes: (recurring season 1, main seasons 2–)[9]
Daughter of Mary-Lynn; niece of Spencer (her "uncle-dad"); dated Tyler Hughes from "Babe Secret Phone Germs" until they married before "Crytunes Divorce Tablet Ring". Beginning of season 3, they decided to get a divorce, it was mutual and decided to still become friends.
Ana Sophia Heger as Lark Short: (main seasons 3–)
Daughter of Greg and Jen Short
Recurring cast[edit]
Ann Guilbert as Shirley "GiGi" Pirkle: Mother of Dr. Joan (Pirkle) Short; widow (husband was Winston); lived at Hidden Harbor (Retirement Community), then lived at Rocking Hill Nursing Home. Following Guilbert's death in June 2016, the GiGi character's death was written into "Eyebrow Anonymous Trapped Gem" as a tribute, and all four stories of the episode revolved around GiGi.
Jordan Peele as Chad: Ex-fiancé of Colleen. Chad had some legal troubles and hired Jen's law firm to represent him. He rented his share in Colleen's apartment to Dougie, who was part of his legal team (she's currently Colleen's roommate).
Fortune Feimster as Dougie: A coworker of Jen; daughter of Jen's boss; member of legal team hired by Chad; Colleen's roommate since the season 1 finale, "Crytunes Divorce Tablet Ring". Dougie is loud, boisterous, uncouth and abrasive physically and emotionally. Despite that, she showed a more vulnerable side when she came out of the closet to Colleen and Matt. She had her very first lesbian kiss with Heather, Tim's wife. When Matt moved in with Colleen and Dougie, it was discovered that Matt wrestled in high school and both he and Dougie went undefeated in their high school careers. In the season 2 premiere, "Annulled Roommate Pill Shower", Dougie challenged Matt to a wrestling match to determine whether or not she has to move out of the apartment. Dougie won the match using her patented "hook, line, and sinker" move to keep her spot in the apartment.
Martin Mull as Gary Timpkins: neighbor and patient of Joan; a recent widower
Susan Park as Dr. Sally Hong: Jen's OB/GYN
Tonita Castro as Tonita: Colleen's grandmother. Tonita was very close to Colleen's ex-fiancée, Chad, and she also is the nanny of Lark, the daughter of Greg and Jen.
Mercedes Ruehl as Mia: Colleen's mother. Married four times. Colleen fears she is turning into her mother.
Bella Shepard as Lexie: one of Samantha's friends
Ashley Wolff as Jenna: one of Samantha's friends
Andrew McKeough as Jayden
Martin Starr as Oscar: an exterminator; a field worker for "Scram! Trappers" animal control & pest removal
Stephnie Weir as Bernadette
Rhys Darby as Teddy
Megan Mullally as Mary-Lynn: mother of Clementine; sister and partner of Spencer
Nick Offerman as Spencer: brother and partner of Mary-Lynn; parent ("uncle-dad") of Clementine
Josh Groban as Ian: an Irish salesman of guitars at a music store who often flirts with his female customers
Russell Peters as Dr. Tak Oh, M.D.: coworker of Tim; widower (wife was Jackie)
Wayne Federman as Dr. Saul Antro
Angela Malhotra as Nurse Silvie: coworker of Tim
Cary Elwes as Professor Sinclair Wilde: Joan's creative writing teacher since "Dinner Professor Steps Lesbian"
Anne Stedman as Sangria: Colleen's stepmom
Episodes[edit]
Main article: List of Life in Pieces episodes
Season
Episodes
Originally aired
First aired
Last aired
1 22 September 21, 2015 (2015-09-21) March 31, 2016 (2016-03-31)
2 22 October 27, 2016 (2016-10-27) May 11, 2017 (2017-05-11)
3 TBA November 2, 2017 (2017-11-02) TBA
Broadcast[edit]
The show debuted on September 21, 2015 on CBS.[10] The first five episodes aired on Mondays, before it was moved on November 5, 2015, to a new time slot of 8:30 p.m. ET/PT (7:30 p.m. CT) on Thursdays, directly after CBS finished its NFL broadcasts.[11] In the United States, the first season airs on Netflix, with the second season also being available in Canada.[12]
In the UK all seasons are available on Amazon Prime and Season 1 is shown on Comedy Central
Reception[edit]
The first season on review aggregator website Rotten Tomatoes reports a 62% approval rating with an average rating of 6.6/10 based on 39 reviews. The website's consensus reads "Life in Pieces strong cast delivers funny, offbeat stories even if they're not always relatable".[13] On Metacritic, the series holds a score of 64 out of 100 based on 24 reviews, indicating "generally favorable reviews."[14]
Ratings[edit]
Season
Timeslot (ET)
Episodes
Premiered
Ended
TV season
Rank
Viewers
(in millions)
Date
Premiere
viewers
(in millions)
Date
Finale
viewers
(in millions)
1 Monday 8:30 p.m. (episodes 1-5)
Thursday 8:30 p.m. (episodes 6-22) 22 September 21, 2015 (2015-09-21) 11.28[15] March 31, 2016 (2016-03-31) 7.23[16] 2015–16 30 10.53[17]
2 Thursday 9:30 p.m. 22 October 27, 2016 (2016-10-27) 5.96[18] May 11, 2017 (2017-05-11) 5.97[19] 2016–17 40 8.15[20]
3 N/A November 2, 2017 (2017-11-02) 6.67[21] N/A N/A 2017–18 N/A N/A
References[edit]
Jump up ^ Andreeva, Nellie (May 8, 2015). "Limitless, Rush Hour, Criminal Minds Spinoff, Code, Life Among CBS Orders". Deadline.com. Retrieved 22 September 2015.
Jump up ^ Andreeva, Nellie (27 October 2015). "'Life In Pieces' Gets Full-Season Order At CBS". Deadline. Retrieved 3 November 2015.
Jump up ^ Andreeva, Nellie (May 11, 2016). "'Life In Pieces' Renewed For Season 2 By CBS". Deadline Hollywood. Retrieved May 11, 2016.
Jump up ^ "CBS Announces Its 2016-2017 Primetime Lineup". The Futon Critic. May 18, 2016. Retrieved May 18, 2016.
Jump up ^ Andreeva, Nellie (March 23, 2017). "CBS Renews 5 Freshman & 11 Returning Series, Including 'MacGyver', 'Superior Donuts', 'Life In Pieces' & 'Hawaii Five-0'". Deadline.com. Retrieved March 23, 2017.
Jump up ^ Andreeva, Nellie (June 1, 2017). "CBS Sets Fall 2017 Premiere Dates For 'Young Sheldon', '9 JKL' & Returning Series". Deadline Hollywood. Retrieved June 1, 2017.
Jump up ^ "Life In Pieces Has Our Jaws Hitting The Floor, But In A Good Way". CBS. August 5, 2015. Retrieved August 8, 2015.
^ Jump up to: a b c d e f g h i j k "Life in Pieces Cast". Retrieved October 15, 2015.
Jump up ^ "'Life In Pieces': Hunter King Upped To Series Regular For Season 2". Deadline.com. June 3, 2016. Retrieved August 11, 2016.
Jump up ^ Bibel, Sara (June 9, 2015). "CBS Announces Fall Premiere Dates: 'CSI' Finale on September 27, 'Supergirl' Debuts in Late October". TV by the Numbers. Retrieved June 12, 2015.
Jump up ^ Bibel, Sara (May 13, 2015). "CBS 2015-16 Primetime Schedule: 'Supergirl' to Monday in November, 'Limitless' on Tuesday, 'Code Black' Wednesday, 'CSI' Finale on September 27 'Rush Hour' & 'Criminal Minds: Beyond Borders' Held for Midseason". TV by the Numbers. Retrieved June 26, 2015.
Jump up ^ "Life In Pieces". Netflix. Netflix. Retrieved 25 December 2017.
Jump up ^ "Life in Pieces: Season 1". Rotten Tomatoes. Retrieved October 29, 2015.
Jump up ^ "Life in Pieces - Season 1 Reviews". Metacritic. Retrieved September 26, 2015.
Jump up ^ Kondolojy, Amanda (September 22, 2015). "Monday Final Ratings: 'The Big Bang Theory' Adjusted Up; 'Significant Mother', 'Life in Pieces' & 'Penn & Teller' Adjusted Down". TV by the Numbers. Retrieved September 22, 2015.
Jump up ^ Porter, Rick (April 1, 2016). "Thursday final ratings: 'Big Bang Theory' adjusts up, 'Scandal,' 'Life in Pieces' and 'The 100' adjust down". TV by the Numbers. Retrieved April 1, 2016.
Jump up ^ "Full 2015–16 TV Season Series Rankings". Deadline Hollywood. May 26, 2016. Retrieved May 26, 2016.
Jump up ^ Porter, Rick (October 28, 2016). "'The Good Place' and 'Chicago Med' adjust up, 'Pure Genius,' other CBS shows adjust down: Thursday final ratings". TV by the Numbers. Retrieved October 28, 2016.
Jump up ^ Welch, Alex (May 12, 2017). "'The Big Bang Theory,' 'Masterchef Junior' adjust up, 'The Blacklist' adjusts down: Thursday final ratings". TV by the Numbers. Retrieved May 12, 2017.
Jump up ^ "Final 2016-17 TV Rankings: 'Sunday Night Football' Winning Streak Continues". Deadline Hollywood. May 26, 2017. Retrieved May 26, 2017.
Jump up ^ Porter, Rick (November 3, 2017). "'Will & Grace' adjusts up, 'Sheldon' and other CBS shows adjust down: Thursday final ratings". TV by the Numbers. Retrieved November 3, 2017.
External links[edit]
Official website
Life in Pieces on IMDb
Life in Pieces at The Futon Critic
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Saratoga and North Creek Railway
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Coordinates: 43°04′58″N 73°48′36″W / 43.082790°N 73.810080°W / 43.082790; -73.810080
Saratoga and North Creek Railway
Saratoga and North Creek train at the Saratoga Springs station
Locale
Warren and Saratoga counties, New York, USA
Commercial operations
Built by
Adirondack Railway
Original gauge
4 ft 8 1⁄2 in (1,435 mm)
Preserved operations
Reporting mark
SNC
Preserved gauge
4 ft 8 1⁄2 in (1,435 mm)
Commercial history
Opened
1871
1889
D&H acquires the railroad
Closed
1989
Preservation history
1999
Upper Hudson River Railroad began operating
2010
Upper Hudson River Railroad closed
2011
Saratoga and North Creek Railway began operation
Headquarters
Saratoga Springs, New York
Website
sncrr.com
[show]Route map
Legend
Legend
to Tahawus, NY
North Creek
Riparius/Riverside
The Glen
Glen Hudson Campground
Thurman
Stony Creek/
1000 Acres Ranch
Hadley/Luzerne
Corinth
Amtrak to Fort Edward
Saratoga Springs
Amtrak to New York City
This diagram:
view
talk
edit
The Saratoga and North Creek Railway is a heritage railway that began operation in July 2011 in the upper Hudson River region of the Adirondack Mountains, in the U.S. state of New York.
The railroad currently operates between North Creek and Saratoga Springs, New York, where it connects with Amtrak's Ethan Allen Express and Adirondack services.
Contents
[hide]
1 History
2 Passenger service
3 Railbike tours
4 References
5 External links
History[edit]
The Saratoga and North Creek Railway operates over former Adirondack Railway trackage built by Thomas C. Durant in 1871. North Creek station is where Theodore Roosevelt learned he was to become president of the United States of America after President William McKinley was assassinated in 1901. During World War II, magnetite, ilmenite, and titanium were shipped by rail from Tahawus by the Delaware and Hudson Railway (D&H). The D&H, which acquired the Adirondack Line from William West Durant in 1889, ran through this region until September 1989 when the mine at Tahawus closed.
In 1998, the line was purchased by Warren County with plans to operate an excursion train to improve tourism and economic development in the area. In 1999, the Upper Hudson River Railroad began operating excursion trains south from North Creek to Riverside Station in Riparius. The Upper Hudson River Railroad lost their contract with Warren County on December 31, 2010, ending 11 years of operation.[1]
On April 8, 2011, it was announced that Iowa Pacific Holdings (IPH) would take over operation of the route effective July 1, 2011.[2] As part of the agreement, IPH agreed to operate a minimum of 182 tourist-oriented passenger trains over the line.[2] IPH began operating trains on July 14, 2011 as the Saratoga and North Creek Railroad. Unlike the Upper Hudson River Railroad, the Saratoga and North Creek operates over the entire 57 miles (92 km) between Saratoga Springs, New York and North Creek.[3]
With the creation of the Saratoga and North Creek Railway, regularly scheduled service returns to the line for the first time since the D&H ceased freight operations on November 17, 1989.[4]
On May 14, 2012, IPH received permission from the Surface Transportation Board to restore freight service on the derelict north end of the line as far as Newcomb.[5] Freight service began on the line in February 2013.[6]
On August 2, 2013, the rear locomotive of an SNCRR train derailed in Thurman. No injuries were reported, but the railroad was closed temporarily to allow for repairs.[7]
Passenger service[edit]
Regularly scheduled service runs once each day Friday through Monday from July 1 to October 31 and on Saturdays and Sundays during the fall and spring. The trip takes 2 hours and 12 minutes.[8]
A separate service, the Snow Train, runs on Fridays, Saturdays, and Sundays during the winter. Unlike the summer trains, the Snow Train has two trains each day in both directions.[9]
Railbike tours[edit]
In 2016, plans were floated for 3-hour pedal-powered railbike tours on a 10-mile section of unused railroad tracks between Moose Pond Club Road and North Creek.[10][11]
The tours opened in July, 2017 using two and four-person pedal-powered railbikes. Starting from the North Creek rail depot, tourists are driven to North River, where they pedal north for three miles along a fairly flat route which includes crossing the Hudson River on a trestle before returning on the same route.
The trip takes about two hours each way. The tours are operated by Revolution Rail, which pays the railway to use the line.[12]
The North End Local runs a shorter route between Thurman and North Creek twice a day on Fridays, Saturdays, and Sundays in July and August.[13] All other trains run the full length of the line between Saratoga Springs and North Creek.
References[edit]
Jump up ^ "Iowa Pacific may reopen line in New York State". Trains Magazine. December 17, 2010. Retrieved April 9, 2011.
^ Jump up to: a b "Iowa Pacific gets go-ahead to operate Upper Hudson River Railroad". Trains Magazine. April 8, 2011. Retrieved April 9, 2011.
Jump up ^ Nemeth, Tom (August 2011). "The Buzz in the Adirondacks". Railpace Newsmagazine.
Jump up ^ John Sesonske, Tom Trencansky (August 2011). "Saratoga & North Creek Debuts Operations". Railpace Newsmagazine.
Jump up ^ Thompson, Maury (May 14, 2012). "Federal board OKs rail freight line between North Creek and Newcomb". Post Star. Retrieved May 14, 2012.
Jump up ^ Post, Paul (20 Feb 2013). "Saratoga & North Creek Railway now hauling freight". The Saratogian. Retrieved 16 June 2014.
Jump up ^ Post, Paul (6 August 2013). "Saratoga & North Creek Railway closes after train goes off track". The Saratogian. Retrieved 6 August 2013.
Jump up ^ "Summer & Fall Schedule". Saratoga & North Creek Railway. Retrieved 16 June 2014.
Jump up ^ Snow Train Timetable
Jump up ^ http://www.timesunion.com/tuplus-business/article/Rail-bikes-would-open-up-High-Peaks-region-7351587.php
Jump up ^ http://www.adirondackdailyenterprise.com/news/local-news/2016/04/rail-bike-business-is-expanding/
Jump up ^ Lehman, Dave (July 14, 2017). "Rail bike company to start trips this weekend". The Post Star. Glens Falls, NY. Retrieved 23 July 2017.
Jump up ^ North End Local
External links[edit]
Wikimedia Commons has media related to Saratoga and North Creek Railway.
Saratoga and North Creek Railroad
Iowa Pacific Holdings
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Saratoga_and_North_Creek_Railway&oldid=804058192"
Categories:
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Railway companies established in 2011
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Saratoga Springs, New York
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Lever action
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Lever action is a type of firearm action which uses a lever located around the trigger guard area (often including the trigger guard itself) to load fresh cartridges into the chamber of the barrel when the lever is worked. This contrasts to bolt-action, semi-automatic, or selective-fire weapons. Most lever-action firearms are rifles, but some lever-action shotguns and a few pistols have also been made. One of the most famous lever-action firearms is the Winchester Model 1873 rifle, but many manufacturers—notably Marlin and Savage—also produce lever-action rifles. Even Colt's Mfg. Co. produced 1883 until 1885 6403 lever-action Colt-Burgess rifles. Mossberg produces the 464 in centerfire .30-30 and rimfire .22. While the term lever-action generally implies a repeating firearm, it is also sometimes —and incorrectly— applied to a variety of single-shot or falling-block actions that use a lever for cycling, such as the Martini–Henry or the Ruger No. 1.
Spencer-carbine M1865, .50 inch
Colt-Burgess rifle
Contents
[hide]
1 History
2 Usage in warfare
2.1 Lever-action shotguns
2.2 On other applications
3 Advantages and disadvantages
4 Cartridges
5 Other long gun actions
6 See also
7 References
8 External links
History[edit]
Colt Paterson Ring Lever rifle
Probably the first lever-action rifles on the market were Colt's 1st and 2nd Model Ring Lever rifles, both cap and ball rifles, produced by the Patent Arms Mfg. Co. Paterson, N.J.-Colt's Patent between 1837 and 1841. The ring-lever was located in front of the trigger. This loading-lever, when pulled, would index the cylinder to the next position and cock the internal hidden hammer.
The first significant lever-action design was the Spencer repeating rifle, a magazine-fed lever-operated breech-loading rifle designed by Christopher Spencer in 1860. It was fed from a removable seven-round tube magazine, enabling the rounds to be fired one after another, and which, when emptied, could be exchanged for another. Over 20,000 were made, and it was adopted by the United States and used during the American Civil War, marking the first adoption of a removable-magazine-fed infantry-and-cavalry rifle by any country.[citation needed]
Unlike later designs, the early Spencer's lever only served to unlock the falling-block action and load a new cartridge from the magazine; it did not cock the hammer, and thus the hammer had to be cocked after the lever was operated to prepare the rifle to fire. The Henry rifle, invented by Benjamin Tyler Henry, a gunsmith employed by Oliver Winchester in 1860, used a centrally located hammer, rather than the offset hammer typical of muzzleloading rifles, and this hammer was cocked by the rearward movement of the Henry's bolt. The Henry also placed the magazine under the barrel, rather than in the butt-stock, a trend followed by most tubular magazines since.
The Martini–Henry rifle was the main rifle of British and Empire forces from the early 1870s to the turn of the 20th century and remained in use to the end of World War I. It was used in some areas, either by civilians or by the local military, much longer. Variants copying the Martini–Henry mechanism but using more modern cartridges were also produced; as late as the 1970s a version taking the common Enfield .303 ammunition was common in Afghanistan.
John Marlin, founder of Marlin Firearms Company, New Haven, Connecticut, introduced Marlin's first lever-action repeating rifle as the Model 1881. This was chambered in rounds such as the 45/70 and 38/55. Its successor was the 1895 solid top design, which we know as the model 336 today. It also gave rise to the Marlin Model 1894, which is still in production today.
Inside of Marlin 39A receiver
By the 1890s, lever-actions had evolved into a form that would last for over a century. Both Marlin and Winchester released new model lever-action rifles in 1894. The Marlin rifle is still in production, whereas production of the Winchester 94 ceased in 2006. While externally similar, the Marlin and Winchester rifles are quite different internally; the Marlin has a single-stage lever action, while the Winchester has a double-stage lever. The double-stage action is easily seen when the Winchester's lever is operated, as first the entire trigger group drops down, unlocking the bolt, and then the bolt is moved rearward to eject the fired cartridge.
The fledgling Savage Arms Company became well known after the development of its popular hammerless Models 1895 and 1899 (which became named the Model 99) lever-action sporting rifles. The Models 1899/99 were produced from introduction in 1899 until the expense of producing the rifle, and declining interest in lever-action rifles from the 1950s on, resulted in dropping the Model 99 from production in 2000. Unlike most Winchester and the Marlin lever-action rifles, which used a tubular magazine requiring round-nose or flat-nose bullets, Arthur Savage designed his rifle using a rotary magazine. This allowed the 99 to use cartridges with spitzer pointed bullets for increased ballistic performance. The 99 was produced in many different cartridges and several different model variations. The final models eliminated the very expensive-to-produce rotary magazine, using a detachable box magazine instead. But the 99 was still very expensive to produce when compared to the other lever-action rifles, and the Savage bolt-action rifles and economics determined the fate of the rifle.
More recently, Sturm Ruger and Company introduced a number of new lever-action designs in the 1990s, unusual because most lever action designs date from before World War II, in the period before reliable semi-automatic rifles became widely available.
Usage in warfare[edit]
The Henry Lever Action was used in the US Civil War. Henry Lever Action firearms were used in the US until the Winchester Model 1866 rifle replaced it. The Spencer repeating rifle was also used in the US Civil War. Additionally, rifles using the lever-action design were used extensively during the 1930s by irregular forces in the Spanish Civil War. Typically, these were Winchesters or Winchester copies of Spanish manufacture. At least 9,000 Model 1895 rifles are known to have been provided by the Soviet Union in 1936 to the Spanish Republicans for use in the Spanish Civil War.[1] Both the Russian Empire and the United States adopted the Winchester Model 1895 as a military weapon.[2]
Lever-action shotguns[edit]
A modern reproduction of the Winchester Model 1887 lever-action shotgun
Early attempts at repeating shotguns invariably centered around either bolt-action or lever-action designs, drawing obvious inspiration from the repeating rifles of the time. The earliest successful repeating shotgun was the lever-action Winchester Model 1887, designed by John Browning in 1885 at the behest of the Winchester Repeating Arms Company, who wanted to market a repeating shotgun. The lever-action design was chosen for reasons of brand recognition, Winchester being best known for manufacturing lever-action firearms at the time, despite the protestations of Browning, who pointed out that a slide-action design would be much better for a shotgun. Initially chambered for black powder shotgun shells (as was standard at the time), the Model 1887 gave rise to the Winchester Model 1901, a strengthened version chambered for 10ga smokeless powder shells. Their popularity waned after the introduction of slide-action shotguns such as the Winchester Model 1897, and production was discontinued in 1920. Modern reproductions are (or have been), however, manufactured by Armi Chiappa in Italy, Norinco in China and ADI Ltd. in Australia, while Winchester continued to manufacture the .410-bore Model 9410, effectively a Winchester Model 94 chambered for .410-bore shotgun shells, until 2006.
French Firearm Manufacturer Verny-Carron has released its Stop and Go Lever action shotgun called the Veloce. It is a unique action which self unloads a fired cartridge but requires a side mounted lever to allow the shotgun to reload and reset the trigger.
In more recent times lever action shotguns have seen a resurgence in some markets with the Turkish made Adler A110 Lever action shotgun selling extremely well in the Australian marketplace with over 7000 ordered in under 2 week they are also being imported into North America as well. The success of the Adler in these markets has sparked several other manufactures in Turkey to begin development of and production of their own lever action shotguns. Australian firearm laws strictly control pump and semi-automatic actions while lever-operation falls into a more lenient category, hence the recent popularity of the action in that country.
On other applications[edit]
M1895 operating mechanism showing the lever in the forward (top) and rear (bottom) positions
A one-off example of lever-action reloading on automatic firearms is the M1895 Colt–Browning machine gun. This weapon had a swinging lever beneath its barrel that was actuated by a gas bleed in the barrel, unlocking the breech to reload. This unique operation gave the nickname "potato digger," as the lever swung each time the weapon fired and would dig into the ground if the weapon was not situated high enough on its mount.
The Knötgen automatic rifle is another example.
Advantages and disadvantages[edit]
While lever-action rifles were (and are) popular with hunters and sporting shooters, they were not widely accepted by the military. One significant reason for this was that it is harder to fire a lever-action from the prone position (compared to a straight-pull or rotating-bolt bolt-action rifle), and while possessing a greater rate of fire (contemporary Winchester advertisements claimed their rifles could fire 2 shots a second) than bolt-action rifles, lever-action firearms are also generally fed from a tubular magazine as did most of the bolt actions of that time which limits the type of ammunition that can be used in them. Pointed centerfire spitzer bullets, for example, can cause explosions in a tubular magazine, as the point of each cartridge's projectile rests on the primer of the next cartridge in the magazine (elastomer-tipped Hornady LEVERevolution ammunition overcomes this problem).[3] The tubular magazine may also have a negative impact on the harmonics of the barrel, which limits the theoretical accuracy of the rifle. A tubular magazine under the barrel also pushes the center of gravity forward, which alters the balance of the rifle in ways that are desirable for shooting off hand from a standing position to some shooters. However, there are some lever rifles—such as the Winchester Model 1895, which saw service with the Russian Army in World War I—that use a box magazine. Furthermore, many of the newer lever-action rifles are capable of shooting groups smaller than 1 minute of angle, making them equal to the accuracy of most modern bolt-action rifles as than in the past.
Henry rifle, toggle-lock
Another explanation for the lack of widespread use of lever action designs stems from the initial inability to fire high-pressure cartridges. Safe operation could only be carried out by using low-pressure cartridges in the toggle-lock lever action rifles such as the Henry rifle and the following Winchester Model 1866, Model 73 and Model 76 (which was used by the mounted police of Canada). The new lever action designs, notably the Winchester Model 1886, Model 92 Model 94 and the Model 1895 (in 7.62x54R, a Russian military cartridge), with a strong locking-block action designed by John Moses Browning, were capable of firing higher pressure cartridges. These rifles became available in the late 19th century, too expensive to manufacture, militaries worldwide had put cheap bolt action rifles into service and were unwilling to invest into producing a lever action rifle after having done with an inexpensive bolt action design.
Due to the higher rate of fire and shorter overall length than most bolt-action rifles, lever-actions have remained popular to this day for sporting use, especially short- and medium-range hunting in forests, scrub, or bushland. Lever-action firearms have also been used in some quantity by prison guards in the United States, as well as by wildlife authorities/game wardens in many parts of the world.
An additional advantage over typical bolt-action rifles is the lack of handedness: lever-actions like pump-actions are frequently recommended as ambidextrous in sporting guidebooks.
Cartridges[edit]
The cartridges for lever action rifles have a wide variety of calibres, bullet shapes and powder loads, but they fall into two basic categories: Low-pressure cartridges with rounded bullets, and high-pressure cartridges with aerodynamic pointed ("spitzer") bullets.
Some lever actions are not as strong as bolt-action or semi-automatic rifle actions. The weaker actions utilize low- and medium-pressure cartridges, somewhat similar to high-powered pistol ammunition. To increase the bullet's energy at the relatively low velocities, these often have larger, heavier bullets than other types of rifles. The most common cartridge is the .30-30, introduced by Winchester with the Model 1894. Other common cartridges include: .38 Special/.357 Magnum, .44 Special/.44 Magnum, .41 Magnum, .444 Marlin, .45-70, .45 Colt, .32-20 Winchester, .35 Remington, .308 Marlin Express, .22 calibre rimfire, and .300 Savage. There is dispute about which of these cartridges can safely be used to hunt large game or large predators. Even in the largest calibres, the low velocities give these cartridges much lower energies than Elephant gun cartridges with comparable calibres. However, even the smallest cartridges fit lightweight, handy rifles that can be excellent for hunting small herbivores, pest control and personal defense.
Some stronger, larger pistols (usually revolvers) also accept some of these cartridges, permitting use of the same ammunition in both a pistol and rifle. The rifle's longer barrel and better accuracy permits higher velocities, longer ranges and a wider selection of game. A pistol provides extra security.
Some of these cartridges (e.g. the .45-70) are developmental descendants of very early black-powder metallic cartridges. When metallic cartridges and lever-actions were first invented, very small, portable kits were developed for hand-reloading and bullet-molding (so called "cowboy reloading kits"). These kits are still available for most low-pressure lever-action cartridges.[4]
Stronger lever actions, such as the action of the Marlin Model 1894 can utilize high-pressure cartridges. Lever-action designs with strong, rotary locking bolts (such as the Browning BLR with seven locking lugs) safely use very high-powered cartridges like the 300 Winchester mag, 300 WSM and 7 MM Remington magnum. Tilting block designs such as the Savage Model 99 are also strong enough to handle high pressures.
Many lever actions have a tubular magazine under the barrel. To operate safely, cartridges for these have bullets with rounded tips, and some use rim-fire primers rather than center-fire primers. The safety problem is that long-range aerodynamic supersonic bullets are pointed. In a tubular magazine the points can accidentally fire center-fire cartridges. A related problem is that some pointed bullets have fragile tips, and can be damaged in a tubular magazine. So, some lever actions such as the Savage Model 99 can be fed from either box or rotary magazines. The Winchester Model 1895 also uses a box magazine, and is chambered for .30-06 and other powerful military cartridges. More recently, spitzer bullets with elastomeric tips have been developed.[5]
Lever-action shotguns such as the Winchester Model 1887 were chambered in 10 or 12-gauge black powder shotgun shells, whereas the Model 1901 was chambered for 10 gauge smokeless shotshells. Modern reproductions are chambered for 12 gauge smokeless shells, while the Winchester Model 9410 shotgun is available in .410 bore.
Other long gun actions[edit]
Bolt action
Pump action
Break-action
Falling-block action
Rolling block
Semi-automatic rifle
See also[edit]
Antique guns
Henry Rifle
Colt-Burgess rifle
Marlin 336
Mossberg model 464
Spencer repeating rifle
Volcanic Repeating Arms
Winchester rifle
Winchester M1887
Martini–Henry
References[edit]
Jump up ^ Mercaldo, Luke; Firestone, Adam; Vanderlinden, Anthony (2011). Allied Rifle Contracts in America. Wet Dog Publications. p. 83. ISBN 0-9707997-7-2.
Jump up ^ Mercaldo, Luke; Firestone, Adam; Vanderlinden, Anthony (2011). Allied Rifle Contracts in America. Wet Dog Publications. pp. 77–78. ISBN 0-9707997-7-2.
Jump up ^ John Taffin (February 2007), "Seven revolution: it's not your grandpa's .30-.30", Guns Magazine, archived from the original on 2010-06-09
Jump up ^ "The Best Portable Reloading Press". Reloader Addict. Retrieved 29 July 2017.
Jump up ^ "Spitzer Bullets for .30-30 Reloaders: Boing, Boing, Boing!". Real Guns. Retrieved 29 July 2017.
External links[edit]
The All-American Lever Gun - Rifle Shooter (dead link)
Hunting with lever-action rifle (dead link)
Retrieved from "https://en.wikipedia.org/w/index.php?title=Lever_action&oldid=833838509"
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Peripheral nervous system
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Peripheral nervous system
The human nervous system. Blue is PNS; yellow is CNS.
Identifiers
Acronym(s)
PNS
TA
A14.2.00.001
FMA
9903
Anatomical terms of neuroanatomy
[edit on Wikidata]
The peripheral nervous system (PNS) is one of the two components of the nervous system, the other part is the central nervous system (CNS). The PNS consists of the nerves and ganglia outside the brain and spinal cord.[1] The main function of the PNS is to connect the CNS to the limbs and organs, essentially serving as a relay between the brain and spinal cord and the rest of the body.[2] Unlike the CNS, the PNS is not protected by the vertebral column and skull, or by the blood–brain barrier, which leaves it exposed to toxins and mechanical injuries. The peripheral nervous system is divided into the somatic nervous system and the autonomic nervous system. In the somatic nervous system, the cranial nerves are part of the PNS with the exception of the optic nerve (cranial nerve II), along with the retina. The second cranial nerve is not a true peripheral nerve but a tract of the diencephalon.[3] Cranial nerve ganglia originated in the CNS. However, the remaining ten cranial nerve axons extend beyond the brain and are therefore considered part of the PNS.[4] The autonomic nervous system is an involuntary control of smooth muscle and glands. The connection between CNS and organs allows the system to be in two different functional states: sympathetic and parasympathetic.
Contents
[hide]
1 Structure
1.1 Somatic nervous system
1.1.1 Cervical spinal nerves (C1–C4)
1.1.2 Brachial plexus (C5–T1)
1.1.3 Lumbosacral plexus (L1–Co1)
1.2 Autonomic nervous system
1.2.1 Sympathetic nervous system
1.2.2 Parasympathetic nervous system
2 Disease
3 See also
4 References
5 External links
Structure[edit]
The peripheral nervous system is divided into the somatic nervous system, and the autonomic nervous system. The somatic nervous system is under voluntary control, and transmits signals from the brain to end organs such as muscles. The sensory nervous system is part of the somatic nervous system and transmits signals from senses such as taste and touch (including fine touch and gross touch) to the spinal cord and brain. The autonomic nervous system is a 'self-regulating' system which influences the function of organs outside voluntary control, such as the heart rate, or the functions of the digestive system.
Somatic nervous system[edit]
See also: List of nerves of the human body
The somatic system includes the sensory nervous system and the somatosensory system and consists of sensory nerves and somatic nerves, and many nerves which hold both functions.
In the head and neck, cranial nerves carry somatosensory data. There are twelve cranial nerves, ten of which originate from the brainstem, and mainly control the functions of the anatomic structures of the head with some exceptions. The nuclei of the olfactory nerve and the optic nerves lie in the forebrain and thalamus, respectively, and are thus not considered to be true cranial nerves. One unique cranial nerve is the vagus nerve, which receives sensory information from organs in the thorax and abdomen. The accessory nerve is responsible for innervating the sternocleidomastoid and trapezius muscles, neither of which being exclusively in the head.
For the rest of the body, spinal nerves are responsible for somatosensory information. These arise from the spinal cord. Usually these arise as a web ("plexus") of interconnected nerves roots that arrange to form single nerves. These nerves control the functions of the rest of the body. In humans, there are 31 pairs of spinal nerves: 8 cervical, 12 thoracic, 5 lumbar, 5 sacral and 1 coccygeal. These nerve roots are named according to the spinal vertebrata which they are adjacent to. In the cervical region, the spinal nerve roots come out above the corresponding vertebrae (i.e., nerve root between the skull and 1st cervical vertebrae is called spinal nerve C1). From the thoracic region to the coccygeal region, the spinal nerve roots come out below the corresponding vertebrae. It is important to note that this method creates a problem when naming the spinal nerve root between C7 and T1 (so it is called spinal nerve root C8). In the lumbar and sacral region, the spinal nerve roots travel within the dural sac and they travel below the level of L2 as the cauda equina.
Cervical spinal nerves (C1–C4)[edit]
Further information: Cervical plexus
The first 4 cervical spinal nerves, C1 through C4, split and recombine to produce a variety of nerves that serve the neck and back of head.
Spinal nerve C1 is called the suboccipital nerve, which provides motor innervation to muscles at the base of the skull. C2 and C3 form many of the nerves of the neck, providing both sensory and motor control. These include the greater occipital nerve, which provides sensation to the back of the head, the lesser occipital nerve, which provides sensation to the area behind the ears, the greater auricular nerve and the lesser auricular nerve.
The phrenic nerve is a nerve essential for our survival which arises from nerve roots C3, C4 and C5. It supplies the thoracic diaphragm, enabling breathing. If the spinal cord is transected above C3, then spontaneous breathing is not possible.
Brachial plexus (C5–T1)[edit]
Further information: Brachial plexus
The last four cervical spinal nerves, C5 through C8, and the first thoracic spinal nerve, T1, combine to form the brachial plexus, or plexus brachialis, a tangled array of nerves, splitting, combining and recombining, to form the nerves that subserve the upper-limb and upper back. Although the brachial plexus may appear tangled, it is highly organized and predictable, with little variation between people. See brachial plexus injuries.
Lumbosacral plexus (L1–Co1)[edit]
The anterior divisions of the lumbar nerves, sacral nerves, and coccygeal nerve form the lumbosacral plexus, the first lumbar nerve being frequently joined by a branch from the twelfth thoracic. For descriptive purposes this plexus is usually divided into three parts:
lumbar plexus
sacral plexus
pudendal plexus
Autonomic nervous system[edit]
The autonomic nervous system controls involuntary responses to regulate physiological functions.[5] The brain and spinal cord from the central nervous system are connected with organs that have smooth muscle, such as the heart, bladder, and other cardiac, exocrine, and endocrine related organs, by ganglionic neurons.[5] The most notable physiological effects from autonomic activity are pupil constriction and dilation, and salivation of saliva.[5] The autonomic nervous system is always activated, but is either in the sympathetic or parasympathetic state.[5] Depending on the situation, one state can overshadow the other, resulting in a release of different kinds of neurotransmitters.[5] There is a lesser known division of the autonomic nervous system known as the enteric nervous system.[6] Located only around the digestive tract, this system allows for local control without input from the sympathetic or the parasympathetic branches, though it can still receive and respond to signals from the rest of the body.[6] The enteric system is responsible for various functions related to gastrointestinal system.[6]
Sympathetic nervous system[edit]
The sympathetic system is activated during a “fight or flight” situation in which great mental stress or physical danger is encountered.[5] Neurotransmitters such as norepinephrine, and epinephrine are released,[5] which increases heart rate and blood flow in certain areas like muscle, while simultaneously decreasing activities of non-critical functions for survival, like digestion.[6] The systems are independent to each other, which allows activation of certain parts of the body, while others remain rested.[6]
Parasympathetic nervous system[edit]
Primarily using the neurotransmitter acetylcholine (ACh) as a mediator, the parasympathetic system allows the body to function in a “rest and digest” state.[6] Consequently, when the parasympathetic system dominates the body, there are increases in salivation and activities in digestion, while heart rate and other sympathetic response decrease.[6] Unlike the sympathetic system, humans have some voluntary controls in the parasympathetic system. The most prominent examples of this control are urination and defecation.[6]
Disease[edit]
Main article: Peripheral neuropathy
Diseases of the peripheral nervous system can be specific to one or more nerves, or affect the system as a whole.
Any peripheral nerve or nerve root can be damaged, called a mononeuropathy. Such injuries can be because of injury or trauma, or compression. Compression of nerves can occur because of a tumour mass or injury. Alternatively, if a nerve is in an area with a fixed size it may be trapped if the other components increase in size, such as carpal tunnel syndrome and tarsal tunnel syndrome. Common symptoms of carpal tunnel syndrome include pain and numbness in the thumb, index and middle finger. In peripheral neuropathy, the function one or more nerves are damaged through a variety of means. Toxic damage may occur because of diabetes (diabetic neuropathy), alcohol, heavy metals or other toxins; some infections; autoimmune and inflammatory conditions such as amyloidosis and sarcoidosis.[5] Peripheral neuropathy is associated with a sensory loss in a "glove and stocking" distribution that begins at the peripheral and slowly progresses upwards, and may also be associated with acute and chronic pain. Peripheral neuropathy is not just limited to the somatosensory nerves, but the autonomic nervous system too (autonomic neuropathy).[5]
See also[edit]
Wikimedia Commons has media related to Peripheral nervous system.
Connective tissue in the peripheral nervous system
Preferential motor reinnervation
References[edit]
Jump up ^ "peripheral nervous system" at Dorland's Medical Dictionary
Jump up ^ "Slide show: How your brain works - Mayo Clinic". mayoclinic.com. Retrieved 17 June 2016.
Jump up ^ Board Review Series: Neuroanatomy, 4th Ed., Lippincott Williams & Wilkins, Maryland 2008, p. 177. ISBN 978-0-7817-7245-7.
Jump up ^ James S. White (21 March 2008). Neuroscience. McGraw-Hill Professional. pp. 1–. ISBN 978-0-07-149623-0. Retrieved 17 November 2010.
^ Jump up to: a b c d e f g h i Laight, David (September 2013). "Overview of peripheral nervous system pharmacology". Nurse Prescribing. ISSN 1479-9189.
^ Jump up to: a b c d e f g h Matic, Agnella Izzo (2014). "Introduction to the Nervous System, Part 2: The Autonomic Nervous System and the Central Nervous System". AMWA Journal: American Medical Writers Association Journal (AMWA J). ISSN 1075-6361.
This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. (November 2007) (Learn how and when to remove this template message)
External links[edit]
Peripheral nervous system photomicrographs
Peripheral Neuropathy from the US NIH
Neuropathy: Causes, Symptoms and Treatments from Medical News Today
Peripheral Neuropathy at the Mayo Clinic
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Mannose 6-phosphate receptor
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Cation-independent mannose-6-phosphate receptor repeat
Identifiers
Symbol
CIMR
Pfam
PF00878
InterPro
IPR000479
SCOP
1e6f
SUPERFAMILY
1e6f
[show]Available protein structures:
Pfam
structures
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Cation-dependent mannose-6-phosphate receptor
Identifiers
Symbol
M6PR
Entrez
4074
HUGO
6752
OMIM
154540
RefSeq
NM_002355
UniProt
P20645
Other data
Locus
Chr. 12 p13
Cation-independent mannose-6 phosphate receptor
Identifiers
Symbol
IGF2R
Entrez
3482
HUGO
5467
OMIM
147280
RefSeq
NM_000876
UniProt
P11717
Other data
Locus
Chr. 6 q25q27
The mannose 6-phosphate receptors (MPRs) are transmembrane glycoproteins that target enzymes to lysosomes in vertebrates.[1]
Mannose 6-phosphate receptors bind newly synthesized lysosomal hydrolases in the trans-Golgi network (TGN) and deliver them to pre-lysosomal compartments. There are two different MPRs, one of ~300kDa and a smaller, dimeric receptor of ~46kDa.[2][3] The larger receptor is known as the cation-independent mannose 6-phosphate receptor (CI-MPR), while the smaller receptor (CD-MPR) requires divalent cations to efficiently recognize lysosomal hydrolases.[3] While divalent cations are not essential for ligand binding by the human CD-MPR, the nomenclature has been retained.[4]
Both of these receptors bind terminal mannose 6-phosphate with similar affinity (CI-MPR = 7 μM, CD-MPR = 8 μM)[5] and have similar signals in their cytoplasmic domains for intracellular trafficking.[6]
Contents
[hide]
1 History
2 Function
2.1 Mechanism of targeting
2.2 Knockout mice studies
3 Structure
3.1 Mannose 6-phosphate Binding
4 CI-MPR and Cancer
5 References
6 Further reading
7 External links
History[edit]
Elizabeth Neufeld was studying patients who had multiple inclusion bodies present in their cells.[7] Due to the large amount of inclusion bodies she named this condition I-cell disease. These inclusion bodies represented lysosomes that were filled with undigestable material. At first Neufeld thought these patients must have a lack of lysosomal enzymes. . Further study showed that all of the lysosomal enzymes were being made but they were being incorrectly targeted. Instead of being sent to the lysosome, they were being secreted. Furthermore, these mis-targeted enzymes were found to not be phosphorylated. Therefore, Neufeld suggested that I-cell disease was caused by a deficiency in the enzymes that add a specific mannose 6-phosphate tag onto lysosomal enzymes so they can be targeted to the lysosome.
Studies of I-cell disease led to the discovery of the receptors that bind to this specific tag. Firstly the CI-MPR was discovered and isolated through the use of affinity chromatography. However scientists discovered that some of the lysosomal enzymes still reached the lysosome in the absence of the CI-MPR. This led to the identification of another mannose 6-phosphate binding receptor, the CD-MPR, which binds its ligand in the presence of a divalent cation such as Mn2+.[8][9]
The genes for each receptor have been cloned and characterised. It is thought that they have evolved from the same ancestral gene as there is conservation in some of their intron/ exon borders and there is a homology in their binding domains.[7]
Function[edit]
The main function of the MPRs is to target lysosomal enzymes to the lysosome.
Mechanism of targeting[edit]
Lysosomal enzymes are synthesised in the rough endoplasmic reticulum along with a range of other secretory proteins. A specific recognition tag has evolved to prevent these harmful lysosomal enzymes from being secreted and to ensure they are targeted to the lysosome.[7] This tag is a mannose 6-phosphate residue.
Once the lysosomal enzyme has been translocated into the rough endoplasmic reticulum an oligosaccharide composed of Glc3Man9GlcNAc2 is transferred en bloc to the protein.[1] The oligosaccharide present on lysosomal enzymes is processed in the same manner as other secretory proteins whilst it is translocated from the endoplasmic reticulum to the cis-Golgi.
An image displaying the overall structure of the CI-MPR and the CD-MPR. This image has been adapted from an 'Introduction to Glycobiology' [1]
In the cis-Golgi a GlcNAc phosphotransferase (EC 2.7.8.17) adds a GlcNAc-1-phosphate residue onto the 6-hydroxyl group of a specific mannose residue within the oligosaccharide.[10] This forms a phosphodiester: Man-phosphate-GlcNAc. Once the phosphodiester has been formed the lysosomal enzyme will be translocated through the Golgi apparatus to the trans-Golgi. In the trans-Golgi a phosphodiesterase (EC 3.1.4.45) will remove the GlcNAc residue exposing the mannose 6-phosphate tag, allowing the lysosomal enzymes to bind to the CI-MPR and the CD-MPR. The MPR-lysosomal enzyme complex is translocated to a pre-lysosomal compartment, known as an endosome, in a clathrin-coated vesicle.[11][12] This targeting away from the secretory pathway is achieved by the presence of a specific sorting signal, an acidic cluster/dileucine motif, in the cytoplasmic tails of the MPRs.[13] Both MPRs bind their ligands most effectively at pH 6 – 7; thus enabling the receptors to bind to the lysosomal enzymes in the trans-Golgi and release them in the acidified environment of the endosome. Once the enzyme has dissociated from the mannose 6-phosphate receptor, it is translocated from the endosome to the lysosome where the phosphate tag is removed from the enzyme.
MPRs are not found in the lysosomes; they cycle mainly between the trans-Golgi network and endosomes. The CI-MPR is also present on the cell surface. Around 10-20% of the CI-MPR can be found at the cell membrane.[14] Its function here is to capture any mannose 6-phosphate tagged enzymes that have accidentally entered the secretory pathway. Once it binds to a lysosomal enzyme the receptor becomes internalised rapidly. Internalisation is mediated by a sorting signal in its cytoplasmic tail – a YSKV motif.[13] This ensures that all harmful lysosomal enzymes will be targeted to the lysosome.
Knockout mice studies[edit]
CI-MPR
Mice lacking the CI-MPR die at day 15 of gestation due to cardiac hyperplasia.[7] The mice suffer from abnormal growth because they are unable to regulate the levels of free IGF-II (insulin-like growth factor type II). Death of the mice can be prevented if the IGF-II allele is also knocked out. Further analysis of the embryos also showed that they display defects in the targeting of lysosomal enzymes as they have an increased level of phosphorylated lysosomal enzymes in their amniotic fluid. Approximately 70% of lysosomal enzymes are secreted in the absence of the CI-MPR – this suggests that the CD-MPR is unable to compensate for its loss.[1]
CD-MPR
When the CD-MPR is knocked out in mice we observe mice that appear healthy apart from the fact that they have defects in the targeting of multiple lysosomal enzymes. These mice display elevated levels of phosphorylated lysosomal enzymes in their blood and they accumulate undigested material in their lysosomes.[7]
From these knockout mice we can deduce that both receptors are needed for the efficient targeting of lysosomal enzymes. If we compare the lysosomal enzymes that are secreted by the two different knockout cell lines we see different sets of enzymes. This suggests that each MPR interacts preferentially with a subset of lysosomal enzymes.
Structure[edit]
The CI-MPR and CD-MPR are structurally distinct receptors however they share an overall general structure as they are both type I integral membrane proteins. Both receptors have a large N-terminal extracytoplasmic domain, one transmembrane domain and a short C-terminal cytoplasmic tail. These cytoplasmic tails contain multiple sorting signals;[15] some of which can be either phosphorylated or palmitoylated.[13]
The first 3 N-terminal domains (Domains 1, 2 and 3) of the cation-independent mannose 6-phosphate receptor with its ligand bound. Image generated from PDB file: = 1SZ0 1SZ0 using PyMol.
CI-MPR: The CI-MPR is ~300 kDa.[16] The N-terminal extracytoplasmic domain contains 15 contiguous P-type carbohydrate recognition domains.[16] They are referred to as MRH (mannose 6-phosphate receptor homology) domains. The domains are homologous because they have:
A similar size - each one has around 150 amino acid residues
Conserved amino acid residues – between 14-38% sequence identity [13]
Conserved positioning of 6 specific Cysteine residues that are involved in forming disulphide bonds [13]
The structure of 7 out of the 15 domains has been determined, using X-ray crystallography, and they seem to share a similar fold.[16] The CI-MPR exists mainly as a dimer in the membrane. Domains 3, 5 and 9 have been found to bind to mannose 6-phosphate. Domains 3 and 9 can bind to mannose 6-phosphate with high affinity. Domain 5 only binds Man-6-phosphate with a weak affinity. However domain 5 has also been shown to bind to the phosphodiester, Man-phosphate-GlcNAc.[16] This is a safety mechanism for the cell – it means it is able to bind to lysosomal enzymes that have escaped the action of the enzyme that removes the GlcNAc residue. Combining these 3 domains allows the CI-MPR to bind to a wide range of phosphorylated glycan structures. Domain 11 binds to IGF-II.
CD-MPR: The CD-MPR is much smaller than the CI-MPR – it is only ~46 kDa.[16] Its N-terminal extracytoplasmic domain contains only 1 P-type carbohydrate recognition domain. The CD-MPR exists mainly as a dimer in the membrane. However monomeric and tetrameric forms are also thought to exist as well.[17] The equilibrium between these different oligomers is affected by pH, temperature and presence of mannose 6-phosphate residues. Each monomer forms a 9 stranded ß-barrel which can bind to a single mannose 6-phosphate residue.
The cation-dependent mannose 6-phosphate receptor with its ligand bound. The purple sphere represents the cation, Mn2+. Image generated from PDB file: = 1C39 1C39 using PyMol.
Mannose 6-phosphate Binding[edit]
The CI-MPR and CD-MPR bind mannose 6-phosphate in a similar fashion. Both form a set of hydrogen bonds between key residues and characteristic hydroxyl groups on the mannose residue. Hydrogen bonds to hydroxyl groups at positions 2, 3 and 4 make the site specific for mannose alone.
Both MPRs share 4 residues that are essential for ligand binding. Mutation of any of these residues results in the loss of mannose 6-phosphate binding.[16] These residues are glutamine, arginine, glutamic acid and tyrosine and are responsible for forming the hydrogen bonds that contact specific hydroxyl groups in the mannose residue.
A wide range of N-glycan structures can be present on lysosomal enzymes. These glycans can vary in:
Type – hybrid or high mannose structures
Size
Presence of the phosphomonoester (mannose 6-phosphate) or phosphodiester (Man-phosphate-GlcNAc)
Number of mannose 6-phosphate tags
Location of the mannose 6-phosphate tag
The CI-MPR and CD-MPR are able to bind to this wide range of N-glycan structures by having a different binding site architecture.[1] The MPRs also bind to the phosphate group in a slightly different manner. Domain 3 of the CI-MPR uses Ser-386 and an ordered water molecule to bind to the phosphate moiety. On the other hand, the CD-MPR uses residues Asp-103, Asn-104 and His-105 to form favourable hydrogen bonds to the phosphate group.[16] The CD-MPR also contains a divalent cation Mn2+ which forms favourable hydrogen bonds with the phosphate moiety.
CI-MPR and Cancer[edit]
It is well-established that the CI-MPR binds mannose 6-phosphate but there is a growing body of evidence that suggests the CI-MPR also binds to unglycosylated IGF-II. It is thought that when the CI-MPR is present on the cell surface, domain 11 will bind to any IGF-II free in the extracellular matrix. The receptor is then rapidly internalised, along with IGF-II, through a YSKV motif present in the CI-MPR’s cytoplasmic tail.[13] IGF-II will then be targeted to the lysosome where it will be degraded. This regulates the level of free IGF-II in the body.
This function of the CI-MPR was determined through the use of knockout mice. It was observed that CI-MPR deficient mice had an increased level of free IGF-II and enlarged organs (around a 30% increase in size [7]). These mice die at day 15 of gestation due to cardiac hyperplasia.[7] Death of the mice could be prevented when the IGF-II allele was also knocked out. When the CI-MPR and the IGF-II allele are knocked out we see a normal mouse as there is no longer a growth factor present that needs to be regulated.
Due to CI-MPR’s ability to modulate the levels of IGF-II it has been suggested it may play a role as a tumour suppressor.[13] Studies of multiple human cancers have shown that a loss of the CI-MPR function is associated with a progression in tumourigenesis.[18] Loss of heterozygosity (LOH) at the CI-MPR locus has been displayed in multiple cancer types including liver and breast.[13][19] However this is a relatively new concept and many more studies will have to investigate the relationship between the CI-MPR and cancer.
References[edit]
^ Jump up to: a b c d e Drickamer K, Taylor ME (2011). Introduction to glycobiology (3rd ed.). Oxford [u.a.]: Oxford University Press. pp. 177–181. ISBN 0199569118.
Jump up ^ Hoflack B, Kornfeld S (July 1985). "Lysosomal enzyme binding to mouse P388D1 macrophage membranes lacking the 215-kDa mannose 6-phosphate receptor: evidence for the existence of a second mannose 6-phosphate receptor". Proc. Natl. Acad. Sci. U.S.A. 82 (13): 4428–32. PMC 391114  . PMID 3160044. doi:10.1073/pnas.82.13.4428.
^ Jump up to: a b Hoflack B, Kornfeld S (October 1985). "Purification and characterization of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver". J. Biol. Chem. 260 (22): 12008–14. PMID 2931431.
Jump up ^ Junghans U, Waheed A, von Figura K (September 1988). "The 'cation-dependent' mannose 6-phosphate receptor binds ligands in the absence of divalent cations". FEBS Lett. 237 (1–2): 81–4. PMID 2971570. doi:10.1016/0014-5793(88)80176-5.
Jump up ^ Tong PY, Kornfeld S (May 1989). "Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor". J. Biol. Chem. 264 (14): 7970–5. PMID 2542255.
Jump up ^ Johnson KF, Chan W, Kornfeld S (December 1990). "Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain". Proc. Natl. Acad. Sci. U.S.A. 87 (24): 10010–4. PMC 55304  . PMID 2175900. doi:10.1073/pnas.87.24.10010.
^ Jump up to: a b c d e f g Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler M (2009). "P-type Lectins". Essentials of glycobiology (2nd ed.). Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press. ISBN 0879697709.
Jump up ^ Hoflack, B.; Komfeld, S. (1985). "Lysosomal enzyme binding to mouse P388D1 macrophage membranes lacking the 215 kDa mannose 6-phosphate receptor: evidence for the existence of a second mannose 6-phosphate receptor". Proc. Natl. Acad. Sci. 82: 4428–32. PMC 391114  . PMID 3160044. doi:10.1073/pnas.82.13.4428.
Jump up ^ Hoflack B, Kornfeld S (1985). "Purification and characterisation of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver". J. Biol. Chem. 260 (22): 12008–14. PMID 2931431.
Jump up ^ Reitman ML, Kornfeld S (1981). "Lysosomal enzymes targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes". J. Biol. Chem. 256 (23): 11977–80. PMID 6457829.
Jump up ^ Duncan JR, Kornfeld S (March 1988). "Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus". J. Cell Biol. 106 (3): 617–28. PMC 2115106  . PMID 2964450. doi:10.1083/jcb.106.3.617.
Jump up ^ Le Borgne R, Hoflack B (1997). "Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN". J. Cell Biol. 137 (2): 335–45. PMC 2139777  . PMID 9128246. doi:10.1083/jcb.137.2.335.
^ Jump up to: a b c d e f g h Ghosh P, Dahms NM, Kornfeld S (2003). "Mannose 6-phosphate receptors: New twists in the tale.". Nature Reviews Molecular Cell Biology. 4 (3): 202–212. PMID 12612639. doi:10.1038/nrm1050.
Jump up ^ Pohlmann, R.; Nagel, G.; Hille, A.; Wendland, M.; Waheed, A.; Braulke, T. & von Figura, K. (1989). "Mannose 6-phosphate specific receptors: structure and function". Biochem Soc Trans. 17: 15.
Jump up ^ Johnson KF, Chan W, Kornfeld S (1990). "Cation-dependent mannose 6-phosphate receptor contains two internalisation signal in its cytoplasmic domain". Proc. Natl. Acad. Sci. 87: 10010–4. PMC 55304  . PMID 2175900. doi:10.1073/pnas.87.24.10010.
^ Jump up to: a b c d e f g Bohnsack RN, Song X, Olson LJ, Kudo M, Gotschall RR, Canfield WM, Cummings RD, Smith DF, Dahms NM (2009). "Cation-independent Mannose 6-phosphate Receptor A Composite of Distinct Phosphomannosyl Binding Sites". Journal of Biological Chemistry. 284 (50): 35215–35226. PMC 2787381  . PMID 19840944. doi:10.1074/jbc.M109.056184.
Jump up ^ Tong PY, Kornfeld S (1989). "Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor". J. Biol. Chem. 264 (14): 7970–5. PMID 2542255.
Jump up ^ De Souza AT, Hankins GR, Washington MK, Orton TC, Jirtle RL (1996). "M6P/IGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity". Nat. Genet. 11 (4): 447–9. PMID 7493029. doi:10.1038/ng1295-447.
Jump up ^ De Souza AT, Hankins GR, Washington MK, Fine RL, Orton TC, Jirtle RL (1995). "Frequent loss of heterozygosity on 6q at the mannose 6-phosphate/insulin-like growth factor II receptor locus in human hepatocellular tumors". Oncogene. 10 (9): 1725–9. PMID 7753549.
Further reading[edit]
Duncan JR, Kornfeld S (1988). "Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus". J. Cell. Biol. 106: 617–28. PMC 2115106  . PMID 2964450. doi:10.1083/jcb.106.3.617.
Junghans U, Waheed A, von Figura K (1988). "The 'cation-dependent' mannose 6-phosphate receptor binds ligands in the absence of divalent cations". FEBS Lett. 237 (1-2): 81–4. PMID 2971570. doi:10.1016/0014-5793(88)80176-5.
Hawkes C, Kar S (2004). "The insulin-like growth factor-II/mannose-6-phosphate receptor: structure, distribution and function in the central nervous system". Brain Res. Brain Res. Rev. 44 (2–3): 117–40. PMID 15003389. doi:10.1016/j.brainresrev.2003.11.002.
Killian JK, Jirtle RL (1999). "Genomic structure of the human M6P/IGF2 receptor". Mamm. Genome. 10 (1): 74–7. PMID 9892739. doi:10.1007/s003359900947.
Ishiwata T, Bergmann U, Kornmann M, Lopez M, Beger HG, Korc M (1997). "Altered expression of insulin-like growth factor II receptor in human pancreatic cancer". Pancreas. 15 (4): 367–73. PMID 9361090. doi:10.1097/00006676-199711000-00006.
External links[edit]
Imperial College Lectins Research Information
UniProtKB/ Swiss-Prot entry for the human cation-independent mannose 6-phosphate receptor
UniProtKB/ Swiss-Prot entry for the human cation-dependent mannose 6-phosphate receptor
Retrieved from "https://en.wikipedia.org/w/index.php?title=Mannose_6-phosphate_receptor&oldid=725754549"
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