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Meninges
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Meninges
The meninges: dura mater, arachnoid mater and pia mater
Details
Artery
middle meningeal artery, meningeal branches of the ascending pharyngeal artery, accessory meningeal artery, branch of anterior ethmoidal artery, meningeal branches of vertebral artery
Nerve
middle meningeal nerve, nervus spinosus
Identifiers
Latin
Meninges
MeSH
A08.186.566
Dorlands
/Elsevier
12523818
TA
A14.1.01.001
FMA
231572
Anatomical terminology
[edit on Wikidata]
The meninges (/məˈnɪndʒiːz/,[1][2] singular: meninx (/ˈmiːnɪŋks/ or /ˈmɛnɪŋks/[3]), from Ancient Greek: μῆνιγξ, translit. mēninx, lit. 'membrane',[4] adjectival: meningeal /məˈnɪndʒəl/) are the three membranes that envelop the brain and spinal cord. In mammals, the meninges are the dura mater, the arachnoid mater, and the pia mater. Cerebrospinal fluid is located in the subarachnoid space between the arachnoid mater and the pia mater. The primary function of the meninges is to protect the central nervous system.
Contents
[hide]
1 Structure
1.1 Dura mater
1.2 Arachnoid mater
1.3 Pia mater
1.4 Leptomeninges
1.5 Spaces
2 Clinical significance
3 Other animals
4 Additional images
5 References
Structure[edit]
Dura mater[edit]
Main article: Dura mater
The dura mater (Latin: tough mother) (also rarely called meninx fibrosa or pachymeninx) is a thick, durable membrane, closest to the skull and vertebrae. The dura mater, the outermost part, is a loosely arranged, fibroelastic layer of cells, characterized by multiple interdigitating cell processes, no extracellular collagen, and significant extracellular spaces. The middle region is a mostly fibrous portion. It consists of two layers: the endosteal layer, which lies closest to the calvaria (skullcap), and the inner meningeal layer, which lies closer to the brain. It contains larger blood vessels that split into the capillaries in the pia mater. It is composed of dense fibrous tissue, and its inner surface is covered by flattened cells like those present on the surfaces of the pia mater and arachnoid mater. The dura mater is a sac that envelops the arachnoid mater and surrounds and supports the large dural sinuses carrying blood from the brain toward the heart.
The dura has four areas of infolding:
Falx cerebri, the largest, sickle-shaped; separates the cerebral hemispheres. Starts from the frontal crest of frontal bone and the crista galli running to the internal occipital protuberance.
Tentorium cerebelli, the second largest, crescent-shaped; separates the occipital lobes from cerebellum. The falx cerebri attaches to it giving a tentlike appearance.
Falx cerebelli, vertical infolding; lies inferior to the tentorium cerebelli, separating the cerebellar hemispheres.
Diaphragma sellae, smallest infolding; covers the pituitary gland and sella turcica.
Arachnoid mater[edit]
Main article: Arachnoid mater
The middle element of the meninges is the arachnoid mater, so named because of its spider web-like appearance. It cushions the central nervous system. This thin, transparent membrane is composed of fibrous tissue and, like the pia mater, is covered by flat cells also thought to be impermeable to fluid.
The shape of the arachnoid does not follow the convolutions of the surface of the brain and so looks like a loosely fitting sac. In particular, in the region of the brain a large number of fine filaments called arachnoid trabeculae pass from the arachnoid through the subarachnoid space to blend with the tissue of the pia mater. The arachnoid is composed of an outermost portion (arachnoid barrier cell layer) with tightly packed cells and no extracellular collagen; that is why it is considered to represent an effective morphological and physiological meningeal barrier between the cerebrospinal fluid and subarachnoid space and the blood circulation in the dura.
The arachnoid barrier layer is characterized by a distinct continuous basal lamina on its inner surface toward the innermost collagenous portion of the arachnoid reticular layer.
Pia mater[edit]
Main article: Pia mater
The pia mater (Latin: tender mother[5]) is a very delicate membrane. It is the meningeal envelope that firmly adheres to the surface of the brain and spinal cord, following all of the brain's contours (the gyri and sulci). It is a very thin membrane composed of fibrous tissue covered on its outer surface by a sheet of flat cells thought to be impermeable to fluid. The pia mater is pierced by blood vessels to the brain and spinal cord, and its capillaries nourish the brain.
Leptomeninges[edit]
The arachnoid and pia mater together are sometimes called the leptomeninges,[6] literally "thin meninges" (Greek: λεπτός leptos - thin). Acute meningococcal meningitis can lead to an exudate within the leptomeninges along the surface of the brain.[7] Because the arachnoid is connected to the pia by cob-web like strands, it is structurally continuous with the pia, hence the name pia-arachnoid or leptomeninges. They are responsible for the production of beta-trace protein (prostaglandin D synthase) a major cerebrospinal fluid protein . [8][9]
Spaces[edit]
Main article: Subarachnoid space
The subarachnoid space is the space that normally exists between the arachnoid and the pia mater, which is filled with cerebrospinal fluid.
The dura mater is attached to the skull, whereas in the spinal cord, the dura mater is separated from the bone (vertebrae) by a space called the epidural space, which contain fat and blood vessels. The arachnoid is attached to the dura mater, while the pia mater is attached to the central nervous system tissue. When the dura mater and the arachnoid separate through injury or illness, the space between them is the subdural space. There is a subpial space underneath the pia mater that separates it from the glia limitans.
Clinical significance[edit]
There are three types of hemorrhage involving the meninges:[10]
A subarachnoid hemorrhage is acute bleeding under the arachnoid; it may occur spontaneously or as a result of trauma.[11]
A subdural hematoma is a hematoma (collection of blood) located in a separation of the arachnoid from the dura mater. The small veins that connect the dura mater and the arachnoid are torn, usually during an accident, and blood leaks into this area.
An epidural hematoma may arise after an accident or spontaneously.
Other medical conditions that affect the meninges include meningitis (usually from fungal, bacterial, or viral infection) and meningiomas that arise from the meninges, or from meningeal carcinomatoses (tumors) that form elsewhere in the body and metastasize to the meninges.
Other animals[edit]
In fish, there is a single membrane known as the primitive meninx. In other vertebrates – amphibians, reptiles and birds, the meninges include a thick outer dura mater and a thick inner secondary meninx. In the early 1900s, Giuseppe Sterzi an Italian anatomist carried out comparative studies on the meninges from the lancelet to man. Contrary to previous reports the spinal meninges were seen to be very simple, both in the adult lower vertebrates and in the early developmental stages of the more advanced vertebrates. From the mesenchyme surrounding the neural tube only a single leaflet forms the primitive meninx. In the following phylogenetic and ontogenetic stages, the latter divides into an internal leaflet: the secondary meninx, and into an external one: the dura mater. Finally, in higher vertebrates, even the secondary meninx divides into the arachnoid and the pia. In the same animals, Sterzi demonstrated that, while in the spinal medulla the dura keeps its identity, in the skull it fuses with the periosteum. He also demonstrated the continuity of all meninges with the envelopes of nerves and with the filum terminale.
Mammals (as higher vertebrates) retain the dura mater, and the secondary meninx divides into the arachnoid and pia mater.[12]
Additional images[edit]
Diagrammatic representation of a section across the top of the skull
Diagrammatic section of scalp.
References[edit]
Jump up ^ OED 2nd edition, 1989.
Jump up ^ Entry "meninges" in Merriam-Webster Online Dictionary, retrieved 2012-07-28.
Jump up ^ Entry "meninx" in Merriam-Webster Online Dictionary, retrieved 2012-07-28.
Jump up ^ μῆνιγξ. Liddell, Henry George; Scott, Robert; A Greek–English Lexicon at the Perseus Project.
Jump up ^ Entry "pia mater" in Merriam-Webster Online Dictionary, retrieved 2015-11-27.
Jump up ^ "leptomeninges - definition of leptomeninges in English | Oxford Dictionaries". Oxford Dictionaries | English.
Jump up ^ Kumar, Vinay (2015). Robbins and Cotran Pathologic Mechanisms of Disease. Philadelphia: Elsevier Saunders. p. 1273. In acute meningitis, an exudate is evident within the leptomeninges over the surface of the brain (Fig. 28-21).
Jump up ^ Yamashima, Tetsumori; Sakuda, Kazushige; Tohma, Yasuo; Yamashita, Junkoh; Oda, Hiroshi; Irikura, Daisuke; Eguchi, Naomi; Beuckmann, Carsten T.; Kanaoka, Yoshihide; Urade, Yoshihiro; Hayaishi, Osamu (1 April 1997). "Prostaglandin D Synthase (β-Trace) in Human Arachnoid and Meningioma Cells: Roles as a Cell Marker or in Cerebrospinal Fluid Absorption, Tumorigenesis, and Calcification Process". Journal of Neuroscience. pp. 2376–2382. Retrieved 10 October 2017.
Jump up ^ attribution, no. "Prostaglandin D2 synthase". TheFreeDictionary.com. Retrieved 10 October 2017.
Jump up ^ "Overview of Adult Traumatic Brain Injuries" (PDF). Orlando Regional Healthcare, Education and Development. 2004. Archived from the original (PDF) on February 27, 2008.
Jump up ^ van Gijn J, Kerr RS, Rinkel GJ (2007). "Subarachnoid haemorrhage". Lancet. 369 (9558): 306–18. doi:10.1016/S0140-6736(07)60153-6. PMID 17258671.
Jump up ^ Kardong, Kenneth V. (1995). Vertebrates: Comparative Anatomy, Funuction, Evolution. Dubuque, Iowa: Wm. C. Brown Publishers. p. 539. ISBN 0-697-21991-7.
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Proton pump
From Wikipedia, the free encyclopedia
Jump to: navigation, search
This article is about biochemical proton pumps. For generators of proton beams, see synchrotron and cyclotron.
A proton pump is an integral membrane protein that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction:
H+
[on one side of a biological membrane] + energy ⇌ H+
[on the other side of the membrane]
Mechanisms are based on energy-induced conformational changes of the protein structure or on the Q cycle.
During evolution, proton pumps have arisen independently on multiple occasions. Thus, not only throughout nature but also within single cells, different proton pumps that are evolutionarily unrelated can be found. Proton pumps are divided into different major classes of pumps that utilize different sources of energy, have different polypeptide compositions and evolutionary origins.
Contents
[hide]
1 Function
2 Diversity
3 Electron transport driven proton pumps
3.1 Electron Transport Complex I
3.2 Electron Transport Complex III
3.3 The cytochrome b6f complex
3.4 Electron Transport Complex IV
4 ATP driven proton pumps
4.1 P-type proton ATPase
4.2 V-type proton ATPase
4.3 F-type proton ATPase
5 Pyrophosphate driven proton pumps
6 Light driven proton pumps
7 See also
8 References
9 External links
Function[edit]
It should be observed that transport of the positively charged proton typically is electrogenic, i.e. it generates an electrical field across the membrane also called the membrane potential. Proton transport becomes electrogenic if not neutralized electrically by transport of either a corresponding negative charge in the same direction or a corresponding positive charge in the opposite direction. An example of a proton pump that is not electrogenic, is the proton/potassium pump of the gastric mucosa which catalyzes a balanced exchange of protons and potassium ions.
The combined transmembrane gradient of protons and charges created by proton pumps is called an electrochemical gradient. An electrochemical gradient represents a store of energy (potential energy) that can be used to drive a multitude of biological processes such as ATP synthesis, nutrient uptake and action potential formation.
In cell respiration, the proton pump uses energy to transport protons from the matrix of the mitochondrion to the inter-membrane space.[1] It is an active pump that generates a proton concentration gradient across the inner mitochondrial membrane because there are more protons outside the matrix than inside. The difference in pH and electric charge (ignoring differences in buffer capacity) creates an electrochemical potential difference that works similar to that of a battery or energy storing unit for the cell.[2] The process could also be seen as analogous to cycling uphill or charging a battery for later use, as it produces potential energy. The proton pump does not create energy, but forms a gradient that stores energy for later use.[3]
Diversity[edit]
The energy required for the proton pumping reaction may come from light (light energy; bacteriorhodopsins), electron transfer (electrical energy; electron transport complexes I, III and IV) or energy-rich metabolites (chemical energy) such as pyrophosphate (PPi; proton-pumping pyrophosphatase) or adenosine triphosphate (ATP; proton ATPases).
Electron transport driven proton pumps[edit]
Electron Transport Complex I[edit]
Main article: NADH dehydrogenase (ubiquinone)
Complex I (EC 1.6.5.3) (also referred to as NADH:ubiquinone oxidoreductase or, especially in the context of the human protein, NADH dehydrogenase) is a proton pump driven by electron transport. It belongs to the H+ or Na+-translocating NADH Dehydrogenase (NDH) Family (TC# 3.D.1), a member of the Na+ transporting Mrp superfamily. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and, in eukaryotes, it is located in the inner mitochondrial membrane. This enzyme helps to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.
Electron Transport Complex III[edit]
Main article: Coenzyme Q – cytochrome c reductase
Complex III ((EC 1.10.2.2)) (also referred to as cytochrome bc1 or the coenzyme Q : cytochrome c – oxidoreductase) is a proton pump driven by electron transport. Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). Complex III is present in the inner mitochondrial membrane of all aerobic eukaryotes and the inner membranes of most eubacteria. This enzyme helps to establish a transmembrane difference of proton electrochemical potential that the ATP synthase of mitochondria then uses to synthesize ATP.
The cytochrome b6f complex[edit]
Main article: Cytochrome b6f complex
The cytochrome b6f complex (EC 1.10.99.1) (also called plastoquinol—plastocyanin reductase) is an enzyme related to Complex III but found in the thylakoid membrane in chloroplasts of plants, cyanobacteria, and green algae. This proton pump is driven by electron transport and catalyzes the transfer of electrons from plastoquinol to plastocyanin. The reaction is analogous to the reaction catalyzed by Complex III (cytochrome bc1) of the mitochondrial electron transport chain. This enzyme helps to establish a transmembrane difference of proton electrochemical potential that the ATP synthase of chloroplasts then uses to synthesize ATP.
Electron Transport Complex IV[edit]
Main article: Cytochrome c oxidase
Complex IV (EC 1.9.3.1) (also referred to as cytochrome c oxidase), is a proton pump driven by electron transport. This enzyme is a large transmembrane protein complex found in bacteria and inner mitochondrial membrane of eukaryotes. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water and in addition translocates four protons across the membrane. This enzyme helps to establish a transmembrane difference of proton electrochemical potential that the ATP synthase of mitochondria then uses to synthesize ATP.
ATP driven proton pumps[edit]
Main article: Proton ATPase
Adenosine triphosphate (ATP) driven proton pumps (also referred to as proton ATPases or H+
-ATPases) are proton pumps driven by the hydrolysis of adenosine triphosphate (ATP). Three classes of proton ATPases are found in nature. In a single cell (for example those of fungi and plants), representatives from all three groups of proton ATPases may be present.
P-type proton ATPase[edit]
Main article: Plasma membrane H+-ATPase
The plasma membrane H+
-ATPase is a single subunit P-type ATPase found in the plasma membrane of plants, fungi, protists and many prokaryotes.
The plasma membrane H+
-ATPase creates the electrochemical gradients in the plasma membrane of plants, fungi, protists, and many prokaryotes. Here, proton gradients are used to drive secondary transport processes. As such, it is essential for the uptake of most metabolites, and also for responses to the environment (e.g., movement of leaves in plants).
Humans (and probably other mammals) have a gastric hydrogen potassium ATPase or H+/K+ ATPase that also belongs to the P-type ATPase family. This enzyme functions as the proton pump of the stomach, primarily responsible for the acidification of the stomach contents (see gastric acid).
V-type proton ATPase[edit]
Main article: V-ATPase
The V-type proton ATPase is a multisubunit enzyme of the V-type. It is found in various different membranes where it serves to acidify intracellular organelles or the cell exterior.
F-type proton ATPase[edit]
Main article: F-ATPase
The F-type proton ATPase is a multisubunit enzyme of the F-type (also referred to as ATP synthase or FOF1 ATPase). It is found in the mitochondrial inner membrane where is functions as a proton transport-driven ATP synthase.
In mitochondria, reducing equivalents provided by electron transfer or photosynthesis power this translocation of protons. For example, the translocation of protons by cytochrome c oxidase is powered by reducing equivalents provided by reduced cytochrome c. ATP itself powers this transport in the plasma membrane proton ATPase and in the ATPase proton pumps of other cellular membranes.
The FoF1 ATP synthase of mitochondria, in contrast, usually conduct protons from high to low concentration across the membrane while drawing energy from this flow to synthesize ATP. Protons translocate across the inner mitochondrial membrane via proton wire. This series of conformational changes, channeled through the a and b subunits of the FO particle, drives a series of conformational changes in the stalk connecting the FO to the F1 subunit. This process effectively couples the translocation of protons to the mechanical motion between the Loose, Tight, and Open states of F1 necessary to phosphorylate ADP.
In bacteria and ATP-producing organelles other than mitochondria, reducing equivalents provided by electron transfer or photosynthesis power the translocation of protons.
CF1 ATP ligase of chloroplasts correspond to the human FOF1 ATP synthase in plants.
Pyrophosphate driven proton pumps[edit]
Main article: Proton pumping pyrophosphatase
Proton pumping pyrophosphatase (also referred to as HH+
-PPase or vacuolar-type inorganic pyrophosphatases (V-PPase; V is for vacuolar)) is a proton pump driven by the hydrolysis of inorganic pyrophosphate (PPi). In plants, HH+
-PPase is localized to the vacuolar membrane (the tonoplast). This membrane of plants contains two different proton pumps for acidifying the interior of the vacuole, the V-PPase and the V-ATPase.
Light driven proton pumps[edit]
Main article: Bacteriorhodopsin
Bacteriorhodopsin is a light-driven proton pump and is used by Archaea, most notably in Halobacteria. Light is absorbed by a retinal pigment covalently linked to the protein, that result in a conformational change of the molecule that is transmitted to the pump protein associated with proton pumping.
See also[edit]
Active transport
Chemiosmosis
Cytochrome
Protonophore
Proton-pump inhibitor
Uncoupling protein
2,4-Dinitrophenol
V-ATPase
References[edit]
Jump up ^ Yoshikawa, Shinya; Shimada, Atsuhiro; Shinzawa-Itoh, Kyoko (2015). "Chapter 4, Section 4 Proton Pump Mechanism". In Peter M.H. Kroneck and Martha E. Sosa Torres. Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases. Metal Ions in Life Sciences. 15. Springer. pp. 108–111. doi:10.1007/978-3-319-12415-5_4.
Jump up ^ Campbell, N.A., 2008. Resource Acquisition and Transport in Vascular Plants. 8th ed., Biology. San Francisco: Pearson Benjamin Cummings.
Jump up ^ Nature, Structural biology: Piston drives a proton pump. by Tomoko Ohnishi, 26 May 2010
External links[edit]
Proton pump animation
Proton Pumps at the US National Library of Medicine Medical Subject Headings (MeSH)
[show]
v
t
e
Membrane transport protein: ion pumps, ATPases / ATP synthase (TC 3A2-3A3)
F-, V-, and A-type ATPase (3.A.2)
H+ (F-type)
H+ transporting, mitochondrial: ATP5A1
ATP5B
ATP5C1
ATP5C2
ATP5D
ATP5E
ATP5F1
ATP5G1
ATP5G2
ATP5G3
ATP5H
ATP5I
ATP5J
ATP5J2
ATP5L
ATP5L2
ATP5O
ATP5S
H+ (V-type)
H+ transporting, lysosomal: ATP6AP1
ATP6AP2
ATP6V1A
ATP6V1B1
ATP6V1B2
ATP6V1C1
ATP6V1C2
ATP6V1D
ATP6V1E1
ATP6V1E2
ATP6V1F
ATP6V1G1
ATP6V1G2
ATP6V1G3
ATP6V1H
ATP6V0A1
ATP6V0A2
ATP6V0A4
ATP6V0B
ATP6V0C
ATP6V0D1
ATP6V0D2
ATP6V0E
ATP6V0E1
TCIRG1
A-ATPase
found in Archea
P-type ATPase (3.A.3)
3.A.3.1.1: Na+/K+ transporting: ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
ATP1G1
3.A.3.1.2: H+/K+
H+/K+ exchanging: ATP4A
ATP4B
3.A.3.1.4: H+/K+ transporting, nongastric: ATP12A
3.A.3.2: Ca2+ (SERCA, PMCA, SPCA) / Ca2+ transporting: ATP2A1
ATP2A2
ATP2A3
ATP2B1
ATP2B2
ATP2B3
ATP2B4
ATP2C1
3.A.3.5: Cu2+ transporting: ATP7A
ATP7B
3.A.3.8.8: flippase: ATP8A2
Other/ungrouped:
Na+/K+ – H+
Mg2+ transporting: ATP3
Class I, type 8: ATP8A1
ATP8B1
ATP8B2
ATP8B3
ATP8B4
Class II, type 9: ATP9A
ATP9B
Class V, type 10: ATP10A
ATP10B
ATP10D
Class VI, type 11: ATP11A
ATP11B
ATP11C
type 13: ATP13A1
ATP13A2
ATP13A3
ATP13A4
ATP13A5
see also ATPase disorders
[show]
v
t
e
Ion pump: proton pumps: Oxidoreduction-driven transporters (TC 3D)
ETC
ETC Complex I
ETC Complex III
ETC Complex IV
Other
Cytochrome b6f complex
Inorganic pyrophosphatase
V-ATPase
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Vasaloppet
From Wikipedia, the free encyclopedia
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Vasaloppet
Jørgen Aukland, Norway, winning the 2013 men's event
Status
Active
Genre
Sports event
Date(s)
First Sunday in March
Frequency
Annually
Location(s)
Sälen–Mora
Country
Sweden
Years active
96[1]
Inaugurated
1922 (1922)[1]
Founder
Anders Pers[1]
Participants
15,800[2]
Attendance
70,200 (2015)[3]
Budget
SEK 120 million (2012)[4]
Activity
Cross-country skiing
Organised by
IFK Mora
Sälens IF
[4]
Sponsor
Volvo
IBM
Preem
Stadium AB
[5]
Vasaloppet (Swedish for 'the Vasa-race') is an annual long distance cross-country ski race held on the first Sunday of March. The 90 km (56 mi) course starts in the village of Sälen and ends in the town of Mora in northwestern Dalarna, Sweden. It is the oldest cross-country ski race in the world, as well as the one with the highest number of participants.
The race was inspired by a notable journey made by King Gustav Vasa when he was fleeing from Christian II's soldiers in 1520. The modern competition started in 1922 and it has been a part of the Worldloppet events since 1978.
Contents
[hide]
1 Origin
2 History
2.1 Women's participation
2.2 Motto
2.3 Kranskulla and kransmas
3 The race
3.1 Organization
3.2 Stations
3.3 Track profile
3.4 The Rope
4 World cup race
5 Vasaloppet week
6 Statistics
6.1 Multiple winners
6.2 Time
6.3 Average times
6.4 Winners' nationalities
7 Winners
7.1 Men
7.2 Women
8 Sister races
9 Notable participants
10 See also
11 References
12 External links
Origin[edit]
In 1520, the young nobleman Gustav Ericsson Vasa was fleeing from the troops of Christian II, king of Denmark, Sweden and Norway (the Kalmar Union). Much of the Swedish nobility was in opposition to the king, and had nicknamed him Christian the Tyrant. In a move to silence the opposition, Christian invited the Swedish aristocracy to a reconciliation party in Stockholm, only to have them, including Gustav's parents, massacred in what came to be known as the Stockholm Bloodbath.[1]
Gustav fled through Dalarna, fearing for his life if he were discovered by the king's troops. He spoke to the men of Mora at a gathering and tried to convince them to raise a levy and start a rebellion against King Christian. The men refused to join the rebellion, and Gustav started out west, toward Norway to seek refuge. However, the men in Mora changed their minds after hearing that the Danish rulers had decided to raise taxes, and now they wanted to join the rebellion with Gustav as their leader. They sent out the two best skiers in the county, two brothers from Mora, Lars and Engelbrekt, to search for him and they caught up with him at Sälen. On 6 June 1523, Gustav Vasa was crowned King of Sweden, after having defeated the Danish king Christian and dissolved the Kalmar Union. Since that day, Sweden has been an independent nation.[1]
While Gustav traveled from Mora to Sälen, the modern race is run the opposite way, finishing in Mora.[1]
History[edit]
Ernst Alm, first winner, 1922
Vasaloppet is the oldest cross-country ski race in the world as well as the one with the highest number of participants. In the past it was also the longest race, until it was surpassed by Pendlerrennet. The idea for the race was published in Westmanlands Läns Tidning on 10 February 1922 by Anders Pers from Mora. On 5 March 1922, the board of IFK Mora decided to organize a trial race. Newspaper Dagens Nyheter sponsored the race with SEK 1,000 and with finances secured the first race was held on 19 March 1922. 136 participants registered for the race and 119 started. The winner was 22 year-old Ernst Alm from Norsjö Sports Club in 7:32:49.[1] He is also the youngest ever winner of the race.
In the 80th race, held on 7 March 2004, about 15,500 skiers competed in the main event. More than 40,000 participated in one of the seven different races held during the first week of March. Vasaloppet is one of the races in the long distance cup Ski Classics.
When Swedish Prime Minister Olof Palme was assassinated just two days before the race in 1986, a cancellation of that year's race was considered. However, the race proceeded as planned with the 10,000 participants observing a moment of silence before the start.[6]
Women's participation[edit]
Kransmas Erik Smedhs and Vibeke Skofterud, 2012
Women winners in Vasaloppet have received awards since 1997. Before that, in 1922–23 and 1981–96, women were allowed to race, but did not receive awards. The first woman to participate was Margit Nordin from Grängesberg in 1923, at 10:09:42. Falu Kuriren wrote about the event: "... an incredible ovation greeted the only lady competitor, Miss Margit Nordin. Miss Nordin was lifted high on strong arms and she received flowers and cheers".[7]
Through the years following the first race, there were many heated debates about women's participation. A majority of officials, mostly male, within sports organizations as well as in society in general, were opposed to women in the race. This led to women being banned from the race from 1924 until 1980. The ban was introduced because it was considered bad for women's health to participate in such a competition. The ban was criticized, especially after 1960. Some defended the ban saying that allowing women would diminish the race's reputation as a tough challenge. Several women did nevertheless participate during the ban, disguised as men.[7] Two of the women who disguised themselves in 1978, Birgitta Westhed and Britt Dohsé, were assisted by professional make-up artist from the Gothenburg City Theatre, who changed their looks using wigs, moustache and a full beard.[8]
Motto[edit]
Finish portal
The motto of Vasaloppet I fäders spår för framtids segrar ('In [our] fathers' tracks for future victories') is written on a portal erected over the finish line in Mora. At the first race, the finish line was simply marked with white board between two flag poles with the word Mål ('Finish') on it. The second year a more stately portal with the motto was fashioned. In 1986, the portal was made permanent and has since become a significant landmark in Mora.[9]
Kranskulla and kransmas[edit]
A tradition connected to the race is the custom to choose a kranskulla. This is a woman who is given the honor of hanging a laurel victory wreath abound the neck of the winner of the race as he cross the finish line. She is dressed in the traditional folk costume of Dalarna. With the event of the women's race, Tjejvasan in 1988, a male kransmas was also appointed. During the year they have been appointed for, the kranskulla and kransmas serve as ambassadors for the race.[10][11]
The race[edit]
Organization[edit]
The race is organized by the non-profit organization Vasaloppsföreningen Sälen-Mora that was registered with the Swedish Companies Registration Office in 1992 and is owned by two local sports clubs, IFK Mora and Sälens IF. The organization has approximately 35 year-round employees who work with planning, preparing and developing the events.[12][13]
Stations[edit]
Traditionally since 1958, blåbärssoppa ('bilberry-soup') made by Ekströms food company, is served at the stations along the course. The Swedish word for bilberry, blåbär, literally means 'blueberry', but the beverage is not made from the North American blueberry. About 50,000 liters is served during the Vasaloppet week.[14] In addition, sports drinks and "Vasaloppet buns" are also served. Coffee is served at the Eldris station.[15]
For a number of years, Ekströms had the logo for their blåbärssoppa printed on the number tags worn by the participants in the race. The word blåbär was printed in large bold letters, which resulted in the participants being called blåbär— a double meaning and pun since the word is also used to describe a "rookie".[16][17][18]
Vasaloppet stations
A cup of blåbärssoppa
Assar Rönnlund as blåbär 108 in 1967
Berga by, 0 km (0 mi)
Smågan, 11 km (6.8 mi)
Mångsbodarna, 24 km (15 mi)
Risberg, 35 km (22 mi)
Evertsberg, 47 km (29 mi)
Oxberg, 62 km (39 mi)
Hökberg, 71 km (44 mi)
Eldris, 81 km (50 mi)
Mora, 90 km (56 mi)
Track profile[edit]
Location
Distance
Elevation
Coordinates
Berga 0 km (0 mi) 350 m (1,150 ft) 61°06′20″N 13°18′15″E / 61.105556°N 13.304167°E / 61.105556; 13.304167
Sprängsbackarna 5 km (3.1 mi) 525 m (1,722 ft) 61°07′49″N 13°20′20″E / 61.130197°N 13.338928°E / 61.130197; 13.338928
Smågan 11 km (6.8 mi) 480 m (1,570 ft) 61°07′27″N 13°25′35″E / 61.124093°N 13.426329°E / 61.124093; 13.426329
Långheden 17 km (11 mi) 520 m (1,710 ft) 61°05′44″N 13°30′32″E / 61.095614°N 13.509009°E / 61.095614; 13.509009
Mångsbodarna 24 km (15 mi) 425 m (1,394 ft) 61°04′46″N 13°37′09″E / 61.079390°N 13.619093°E / 61.079390; 13.619093
Tennäng 29 km (18 mi) 315 m (1,033 ft) 61°04′45″N 13°41′16″E / 61.079165°N 13.687726°E / 61.079165; 13.687726
Risberg 35 km (22 mi) 420 m (1,380 ft) 61°05′08″N 13°46′23″E / 61.085556°N 13.773056°E / 61.085556; 13.773056
Lyttran 37 km (23 mi) 380 m (1,250 ft) 61°05′38″N 13°48′23″E / 61.093893°N 13.806360°E / 61.093893; 13.806360
Evertsberg 47 km (29 mi) 430 m (1,410 ft) 61°08′18″N 13°57′46″E / 61.138376°N 13.962904°E / 61.138376; 13.962904
Björnarvet 57 km (35 mi) 215 m (705 ft) 61°06′47″N 14°06′26″E / 61.113132°N 14.107093°E / 61.113132; 14.107093
Kvarnbäcken 60 km (37 mi) 265 m (869 ft) 61°06′57″N 14°09′02″E / 61.115937°N 14.150596°E / 61.115937; 14.150596
Oxberg 62 km (39 mi) 230 m (750 ft) 61°06′53″N 14°10′36″E / 61.114820°N 14.176688°E / 61.114820; 14.176688
Hökberg 71 km (44 mi) 250 m (820 ft) 61°04′30″N 14°18′34″E / 61.074956°N 14.309514°E / 61.074956; 14.309514
Eldris 81 km (50 mi) 205 m (673 ft) 61°00′55″N 14°24′36″E / 61.015236°N 14.410089°E / 61.015236; 14.410089
Mora 90 km (56 mi) 165 m (541 ft) 61°00′27″N 14°32′44″E / 61.007490°N 14.545555°E / 61.007490; 14.545555
The Rope[edit]
The Rope, also referred to as "The Dreaded Rope",[19] is a series of ropes drawn across the track at certain times to prevent participants, who have no chance of reaching the finish line in Mora before the area is closed, to continue.[20] The ropes in Vasaloppet are drawn at seven of the stations: Smågan, Mångsbodarna, Risberg, Evertsberg, Oxberg, Hökberg and Eldris.[19] The race starts at 8:00 a.m. and the finish area is closed at 8:15 p.m. just before the prize ceremony.[2][21][22]
World cup race[edit]
Since 1978, Vasaloppet is included in the Worldloppet Ski Federation, a series of long-distance cross-country skiing races.[23] In 2006, the Vasaloppet was included in the FIS Cross-Country World Cup; a large complement of World Cup racers joined the men's field for the full 90 km (56 mi) distance. Owing to the distance—40 km (25 mi) longer than the longest race usually skied in the World Cup—as well as the proximity to the just-concluded Olympic Games in Turin, the race was again dominated by long-distance specialists rather than World Cup racers. Daniel Tynell won the race, just ahead of Jerry Ahrlin, while Anders Aukland – who has skied on both the Norwegian national World Cup team and in marathons like the Vasaloppet – finished third. The women's World Cup Vasaloppet was held over 45 km (28 mi) the previous day, rather than being integrated with the full Vasaloppet. Marit Bjørgen from Norway won, though the field included only World Cup racers, since the marathon specialists chose to race in the full-distance event the next day.
Vasaloppet week[edit]
Kortvasan start in Oxberg, 2006
The week preceding Vasaloppet is known as Vasaloppet week. Races held during this week include:
Kortvasan (short – 30 km (19 mi))
Tjejvasan (ladies – 30 km (19 mi))
Halvvasan (half – 45 km (28 mi))
Ungdomsvasan (9–16 years old – 3–9 km (1.9–5.6 mi))
Öppet spår (non-competitive – 90 km (56 mi))
Stafettvasan (relay – 90 km (56 mi))
Nattvasan (two-person teams make the original race at night in darkness – 90 km (56 mi))
Vasaloppet (original – 90 km (56 mi))
Statistics[edit]
Multiple winners[edit]
Men
Nils 'Mora-Nisse' Karlsson has the most titles, with 9. Janne Stefansson (7), Jan Ottosson (4), Arthur Häggblad (4), Bengt Hassis (3), Oskar Svärd (3), Daniel Tynell, Jörgen Brink (3) and John Kristian Dahl (3) are the only other racers with more than two titles. Six men have two titles.
Women
Sofia Lind has the most titles, with 4. Four women have two titles.
Time[edit]
The average winning time is 5:11:38 (a per-kilometer average of 3:28). The record winning time is 3:38:41 (2:26 per kilometer), set by Jörgen Brink of Sweden in 2012. Only ten winners have finished in less than four hours.
The ten fastest times include six Swedes, three Norwegians, and one Swiss; Jörgen Brink, Sweden appear twice in the list of the ten fastest times. Of the ten fastest times, two occurred in the 1980s, two in the 1990s, two in the 2000s and four in the 2010s.
In 2012 course records were set for both men and women. Before that the fastest year was 1998, also with course records for both men and women.
Ten fastest times
2012: Jörgen Brink (SWE) – 3:38:41
1998: Peter Göransson (SWE) – 3:38:57
2004: Anders Aukland (NOR) – 3:48:42
1986: Bengt Hassis (SWE) – 3:48:55
2013: Jørgen Aukland (NOR) – 3:50:49
2005: Oskar Svärd (SWE) – 3:51:47
2011: Jörgen Brink (SWE) – 3:51:51
1992: Jan Ottosson (SWE) – 3:57:04
2017: John Kristian Dahl (NOR) - 3:57:18
1983: Konrad Hallenbarter (SUI) – 3:58:08
Average times[edit]
Average times per decade have declined in each ten-year span, with the sharpest drop between decade averages occurring in the 1960s, for which the average winning time was 31:45 faster than the average winning time of the 1950s. The average winning time in the 1970s was 16:07 faster than the 1960s, the 1980s average was 24:09 faster than the 1970s, and the 1990s average was 13:06 faster than the 1980s. The average winning time in the 2000s is only 2:18 faster than the 1990s, however. As of 2011 the average winning time so far in the 2010s is 12:12 faster than the 2000s.
Winners' nationalities[edit]
Sweden is the most prolific producer of winners, with 74 titles (including two all-Sweden ties, in 1928 and 1988), or 90% of the 82 contested races. (The race was canceled in 1932, 1934, and 1990). Norway has produced five winners: Ole Ellefsæter, 1971; Anders Aukland, 2004; Jørgen Aukland, 2008 and 2013; John Kristian Dahl, 2014, 2016 and 2017; and Petter Eliassen, 2015. Two countries have produced two winners: Finland (Pekka Kuvaja, 1954; Pauli Siitonen, 1973) and Austria (Walter Mayer, 1980; Mikhail Botvinov, 1997). Five countries have produced one winner: East Germany (Gert-Dietmar Klause, 1975), the Soviet Union (Ivan Garanin, 1977), France (Jean-Paul Pierrat, 1978), Switzerland (Konrad Hallenbarter, 1983), and Estonia (Raul Olle, 2000).
Sweden won every race until 1954, when Pekka Kuvaja of Finland won the race. The next non-Swede to win was Ole Ellefsæter of Norway (1971), who kicked off a decade in which Sweden won just five titles and racers from five other countries won the five other titles. Sweden won 8 of the titles in the 1980s (Austria [Mayer, 1980] and Switzerland [Hallenbarter, 1983] each won one title in that decade), and 8 more in the 1990s (Austria won one more title in that decade [Botvinov, 1997], and the race was canceled once [1990]). In the 2000s, Sweden won seven races, Norway won twice (Anders Aukland, 2004; Jørgen Aukland, 2008), and Estonia won once (Olle, 2000).
Winners[edit]
Men[edit]
Year
Name
Club/Nation
Time
1922 Ernst Alm IFK Norsjö, Sweden 7:32:49
1923 Oskar Lindberg IFK Norsjö, Sweden 6:32:41
1924 John Lindgren IFK Umeå, Sweden 6:53:26
1925 Sven Utterström Bodens BK, Sweden 6:03:55
1926 Per-Erik Hedlund Malungs IF, Sweden 5:36:07
1927 Konrad Pettersson Luleå SK, Sweden 6:19:32
1928 Per-Erik Hedlund and
Sven Utterström (tie) Särna SK, Sweden
Bodens BK, Sweden 5:33:23
1929 Johan Abram Persson Arjeplogs SK, Sweden 6:38:22
1930 Verner Lundström Arvidsjaurs IF, Sweden 6:56:30
1931 Anders Ström IFK Mora, Sweden 6:37:47
1932 Cancelled
1933 Arthur Häggblad IFK Umeå, Sweden 5:57:09
1934 Cancelled
1935 Arthur Häggblad IFK Umeå, Sweden 6:08:55
1936 Sven Hansson Lima IF, Sweden 6:31:55
1937 Arthur Häggblad IFK Umeå, Sweden 6:05:56
1938 Elias Nilsson Östersunds SK, Sweden 5:48:28
1939 Alfred Lif Orsa IF, Sweden 5:35:59
1940 Arthur Häggblad IFK Umeå, Sweden 6:23:57
1941 Mauritz Brännström IFK Norsjö, Sweden 6:51:12
1942 Olle Wiklund IFK Bergvik, Sweden 5:31:50
1943 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:47:10
1944 Gösta Andersson IFK Umeå, Sweden 5:18:43
1945 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 6:27:59
1946 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 6:08:42
1947 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:59:35
1948 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:35:13
1949 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:44:09
1950 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 6:08:25
1951 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:27:20
1952 Sigfrid Mattsson Skarpnäcks IF, Sweden 5:09:45
1953 Nils 'Mora-Nisse' Karlsson IFK Mora, Sweden 5:01:55
1954 Pekka Kuvaja Finland 6:22:51
1955 Sixten Jernberg Lima IF, Sweden 5:27:28
1956 Sigvard Jonsson Rossöns IK, Sweden 5:23:36
1957 Gunnar Larsson Oxbergs IF, Sweden 6:23:40
1958 Gunnar Larsson Oxbergs IF, Sweden 5:31:50
1959 Sune Larsson Oxbergs IF, Sweden 5:13:28
1960 Sixten Jernberg Lima IF, Sweden 5:13:26
1961 David Johansson Delsbo IF, Sweden 4:45:10
1962 Janne Stefansson Sälens IF, Sweden 5:07:46
1963 Janne Stefansson Sälens IF, Sweden 4:56:25
1964 Janne Stefansson Sälens IF, Sweden 5:32:07
1965 Janne Stefansson Sälens IF, Sweden 4:35:03
1966 Janne Stefansson Sälens IF, Sweden 5:52:38
1967 Assar Rönnlund IFK Umeå, Sweden 5:20:22
1968 Janne Stefansson Sälens IF, Sweden 4:39:49
1969 Janne Stefansson Sälens IF, Sweden 4:50:07
1970 Lars-Arne Bölling IFK Mora, Sweden 5:08:38
1971 Ole Ellefsæter Norway 5:12:56
1972 Lars-Arne Bölling IFK Mora, Sweden 5:35:19
1973 Pauli Siitonen Finland 4:42:11
1974 Matti Kuosku Högbo IF, Sweden 5:06:23
1975 Gert-Dietmar Klause East Germany 4:20:29
1976 Matti Kuosku Högbo IF, Sweden 4:09:07
1977 Ivan Garanin Soviet Union 4:30:34
1978 Jean-Paul Pierrat France 5:20:12
1979 Ola Hassis Orsa IF, Sweden 4:05:58
1980 Walter Mayer Austria 4:08:02
1981 Sven-Åke Lundbäck IFK Råneå, Sweden 4:29:32
1982 Lasse Frykberg IFK Mora, Sweden 4:28:50
1983 Konrad Hallenbarter Switzerland 3:58:08
1984 Hans Persson Åsarna IK, Sweden 4:14:14
1985 Bengt Hassis Orsa IF, Sweden 4:45:43
1986 Bengt Hassis Orsa IF, Sweden 3:48:55
1987 Anders Larsson Bondsjöhöjden, Sweden 4:20:20
1988 Anders Blomquist and
Örjan Blomquist (tie) IFK Lidingö, Sweden
IFK Lidingö, Sweden 4:47:04
1989 Jan Ottosson Åsarna IK, Sweden 5:09:33
1990 Cancelled
1991 Jan Ottosson Åsarna IK, Sweden 5:07:11
1992 Jan Ottosson Åsarna IK, Sweden 3:57:04
1993 Håkan Westin Graningealliansen, Sweden 4:02:10
1994 Jan Ottosson Åsarna IK, Sweden 4:06:19
1995 Sven-Erik Danielsson Dala-Järna IK, Sweden 4:11:09
1996 Håkan Westin Graningealliansen, Sweden 4:01:15
1997 Michail Botvinov Austria 4:11:41
1998 Peter Göransson Åsarna IK, Sweden 3:38:57
1999 Staffan Larsson IFK Mora, Sweden 4:31:37
2000 Raul Olle Estonia 4:14:38
2001 Henrik Eriksson IFK Mora, Sweden 4:01:22
2002 Daniel Tynell Falun/Borlänge SK, Sweden 3:58:52
2003 Oskar Svärd Sollefteå SK, Sweden 3:58:23
2004 Anders Aukland Norway 3:48:42
2005 Oskar Svärd Ulricehamns IF, Sweden 3:51:47
2006 Daniel Tynell Grycksbo IF, Sweden 4:34:09
2007 Oskar Svärd Ulricehamns IF, Sweden 4:43:40
2008 Jørgen Aukland Team Xtra Personnel, Norway 4:13:45
2009 Daniel Tynell Grycksbo IF, Sweden 4:10:56
2010 Jörgen Brink Hudiksvalls IF, Sweden 4:02:59
2011 Jörgen Brink Hudiksvalls IF, Sweden 3:51:51
2012 Jörgen Brink Team United Bakeries, Sweden 3:38:41
2013 Jørgen Aukland Team Xtra Personnel, Norway 3:50:49
2014 John Kristian Dahl Team United Bakeries, Norway 4:14:33
2015 Petter Eliassen Team LeasePlan Go, Norway 4:01:48
2016 John Kristian Dahl Team United Bakeries, Norway 4:08:00
2017 John Kristian Dahl Team United Bakeries, Norway 3:57:18
2018 Andreas Nygaard Norway 4:24:36
Women[edit]
Year
Name
Club/Nation
Time
1997 Sofia Lind Åsarna IK, Sweden 5:06:35
1998 Kerrin Petty IFK Mora, citizen of United States 4:17:02
1999 Sofia Lind Åsarna IK, Sweden 5:04:50
2000 Svetlana Nageykina Russia 4:52:35
2001 Ulrica Persson SK Bore, Sweden 4:31:05
2002 Svetlana Nageykina Belarus 4:38:47
2003 Ulrica Persson SK Bore, Sweden 4:32:57
2004 Sofia Lind Åsarna IK, Sweden 4:20:28
2005 Sofia Lind Åsarna IK, Sweden 4:24:09
2006 Cristina Paluselli Italy 4:59:24
2007 Elin Ek IFK Mora, Sweden 4:48:29
2008 Sandra Hansson Uddevalla IS, Sweden 4:47:16
2009 Sandra Hansson Uddevalla IS, Sweden 4:43:13
2010 Susanne Nyström IFK Mora, Sweden 4:33:07
2011 Jenny Hansson Östersunds SK, Sweden 4:25:30
2012 Vibeke Skofterud Slitu IF, Norway 4:08:24
2013 Laila Kveli Lierne IL, Norway 4:22:22
2014 Laila Kveli Lierne IL, Norway 4:31:57
2015 Justyna Kowalczyk Poland 4:41:02
2016 Katerina Smutna Austria 4:17:56
2017 Britta Johansson Norgren Sollefteå SK, Sweden 4:19:43
2018 Lina Korsgren Åre Längdskidklubb Sweden 4:41:50
Sister races[edit]
Vasaloppet USA, held annually on the second Saturday of February in Mora, Minnesota, USA (prior to 2015, the race occurred annually on the second Sunday of February)
Vasaloppet Japan, held in Asahikawa, Hokkaido, since 1981
Chinese Vasaloppet, held in Changchun since 2003
Botniavasan, Finland, since 2006
Vasaloppet de la Sergerie, Jonquière, Quebec, Canada, since 2007
Notable participants[edit]
Prince Frederik of Denmark, 2012
Vasaloppet has been called a rite of passage for Swedes.[24] Aside from the winners, some of the noted people who have completed the race are:
Carl XVI Gustaf, King of Sweden (3 times)[25]
Carl Philip, Prince of Sweden[26]
Peter Forsberg, ice hockey player[27]
Frederik, Crown Prince of Denmark[27]
Marcus Grönholm, rally driver[28]
Mark Levengood, journalist, writer[29]
Ueli Maurer, Swiss defence minister[27]
Pippa Middleton, socialite[30]
James William Middleton, businessman[30]
Arild Monsen, cross-country skier[27]
Rickard Olsson, television and radio presenter[28]
Anja Pärson, alpine skier[28]
Åsa Romson, politician[27]
Olaf Tufte, competition rower[28]
Frida Wallberg, boxer[27]
Måns Zelmerlöw, Eurovision winner[31]
See also[edit]
Finlandia-hiihto
List of Swedish sportspeople
Skiing
Tjejvasan
Tourism in Sweden
References[edit]
^ Jump up to: a b c d e f g "Så började allt" [How it all began]. www.vasaloppet.se. Vasaloppet. Retrieved 4 March 2016.
^ Jump up to: a b "Anta utmaningen i världens största skidtävling" [Accept the challenge in the world's largest ski competition]. www.vasaloppet.se. Vasaloppet. Retrieved 4 March 2016.
Jump up ^ "Vasaloppets betydelse för regionen" [Vasaloppet's significance for the region]. www.mora.se. Mora Municipality, Sweden. Retrieved 4 March 2016.
^ Jump up to: a b TT (25 February 2013). "Vasaloppet en lönsam affär" [Vasaloppet profitable business]. www.gp.se. Göteborgs-Posten. Retrieved 4 March 2016.
Jump up ^ "Sponsorer" [Sponsors]. www.vasaloppet.se. Vasaloppet. Retrieved 4 March 2016.
Jump up ^ Larsson, Lars-Gunnar (4 March 2016). "Vasaloppet nära ställas in efter Palmemordet" [Vadsaloppet almost cancelled after murder of Palme]. www.svt.se. Sveriges Television. Retrieved 5 March 2016.
^ Jump up to: a b Svensson, Jan (7 March 2015). "Vasaloppet och kvinnor har inte alltid gått bra ihop" [Vasaloppet and women have not always seen eye to eye]. www.dt.se. Dalarnas Tidningar. Retrieved 4 March 2016.
Jump up ^ Modin, Jenny (6 March 2015). "Birgitta åkte Vasaloppet 1978 – utklädd till man" [She did the Vasaloppet race in 1978 - disguised as a man]. www.svt.se. Sveriges Television. Retrieved 6 March 2016.
Jump up ^ "Målgången i Mora" [The finish line in Mora]. www.svt.se. Sveriges Television. 2 February 2011. Retrieved 4 March 2016.
Jump up ^ "Kranskulla och kransmas". www.vasaloppet.se. Vasaloppet. Retrieved 4 March 2016.
Jump up ^ Björnbom, Jonna (28 November 2014). "Här är nästa års kranskulla och kransmas" [Here is next year's karnskulla and kransmas]. www.svt.se. Sveriges Television. Retrieved 4 March 2016.
Jump up ^ "Vasaloppsföreningen Sälen-Mora" (in Swedish). allabolag.se. Archived from the original on 2016-05-18. Retrieved 2016-05-18.
Jump up ^ "A non-profit organization owned by IFK Mora and Sälens IF". Vasaloppet. Archived from the original on 2015-09-09. Retrieved 2016-05-18.
Jump up ^ "Ekströms & Vasaloppet". www.ekströms.se. Ekströms. Retrieved 5 March 2016.
Jump up ^ Micu, Patrik (29 February 2016). "Fina förhållanden i Vasaloppsspåret" [Good conditions in the Vasaloppet track]. www.expressen.se. Expressen. Retrieved 5 March 2016.
Jump up ^ Falk, Anna (28 February 2002). "Ur spår, ditt blåbär!" [Make way, rookie!]. www.sn.se. Södermanlands Nyheter. Retrieved 6 March 2016.
Jump up ^ Johansson, Carolina (2013). "Bättre ett blåbär i Vasaloppet än ett torkat russin i TV-soffan" [Better a rookie in Vasaloppet than a rasin on the TV couch] (PDF). www.uu.se. Uppsala University. Retrieved 6 March 2016.
Jump up ^ Blomqvist, Anna (26 January 2016). "Nytt Vasalopp för blåbär och funktionärer" [A new Vasalopp for rookies and officials]. www.svt.se. Sveriges Television. Retrieved 6 March 2016.
^ Jump up to: a b "Karta". www.ibm.com. IBM. Retrieved 6 March 2016.
Jump up ^ Hedlund, Johan. "Snart dras repet för allt tuffare Tjurrus" [Soon The Rope will be drawn for a tougher Tjurrus]. www.vf.se. Värmlands Folkblad. Retrieved 6 March 2016.
Jump up ^ "Grattis till målgång! Vad händer nu?" [Congrats on reaching the finish line! What happens next?]. www.vasaloppet.se. Vasaloppet. Retrieved 6 March 2016.
Jump up ^ Jutéus, Sten (1 March 2014). "Han är långsammast någonsin i vasaloppet" [He is the slowest ever in Vasaloppet]. www.expressen.se. Expressen. Retrieved 6 March 2016.
Jump up ^ "Vasaloppet". Worldloppet. Retrieved 4 March 2015.
Jump up ^ Pettersson, Kjell (9 March 2010). "Mandomsprovet. Tolvtaggaren. Vasaloppet. Numera öppet även för kvinnor!" [Rite of passage. Crown jewel. Vasaloppet. Now open to women.]. www.internationalen.se. Internationalen. Retrieved 5 March 2016.
Jump up ^ "Kung Carl den sextonde Gustaf". www.kungahuset.se. Monarchy of Sweden. Retrieved 5 March 2016.
Jump up ^ "Prins Carl Philip". www.kungahuset.se. Monarchy of Sweden. Retrieved 5 March 2016.
^ Jump up to: a b c d e f Banck, Stina (28 February 2014). "Kändistätt i Vasaloppsspåren" [Celebs in Vasaloppet]. www.svt.se. Sveriges Television. Retrieved 5 March 2016.
^ Jump up to: a b c d Bloodworth, Callum (3 March 2015). "Här följer du kändisarna i Vasaloppet" [Celebs in Vasaloppet]. www.expressen.se. Expressen. Retrieved 5 March 2016.
Jump up ^ Ståhlspets, Sofia (2 February 2012). "Kändisarna som diggar längdskidor" [Celebs who like cross-country skiing]. www.expressen.se. Expressen. Retrieved 5 March 2016.
^ Jump up to: a b "Pippa Middleton in Vasaloppet 2012". www.mynewsdesk.com. MyNewsDesk. 4 March 2012. Retrieved 5 March 2016.
Jump up ^ Åberg, Erik (6 March 2016). "Måns Zelmerlöw i mål – klarade Vasaloppet" [Måns Zelmerlöv at the finish line - made Vasaloppet]. www.aftonbladet.se. Aftonbladet. Retrieved 24 March 2016.
External links[edit]
Wikimedia Commons has media related to Vasaloppet.
Vasa That! – A participant's story
Vasaloppet USA Website
3D animation of race – Google Earth software required
Vasaloppet 2013 photos
The event at SVT's Open Archive (in Swedish)
En svensk klassiker
Vasaloppet | Vätternrundan | Vansbrosimningen | Lidingöloppet
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text:
The Only One I Know
From Wikipedia, the free encyclopedia
Jump to: navigation, search
"The Only One I Know"
Single by The Charlatans
from the album Some Friendly
Released
14 May 1990
Format
7" vinyl
12" vinyl
CD maxi
Recorded
The Winding Studios, Wrexham, Wales, 1990
Genre
Madchester[1]
Length
4:00
Label
Situation Two (UK)
RCA (US)
Songwriter(s)
Martin Blunt
Jon Brookes
Tim Burgess
Mark Collins
Jon Day
Producer(s)
Chris Nagle
The Charlatans singles chronology
"Indian Rope"
(1990) "The Only One I Know"
(1990) "Then"
(1990)
"Indian Rope"
(1990) "The Only One I Know"
(1990) "Then"
(1990)
"The Only One I Know" is the second single by the English rock band The Charlatans. It was their first top-ten hit, reaching no. 9 on the UK Singles Chart.[2] In the UK it was the highest-charting single from the Some Friendly album. Its best showing in the US was on the Modern Rock Chart, where it reached no. 5 in September 1990.[3][4] The song contained lines directly lifted from The Byrds' 1967 song "Everybody’s Been Burned,"[1] while the melody prominently features an organ riff lifted from the Deep Purple rendition of the song "Hush".[5]
The song was included as a track on the influential compilation album Happy Daze. A funk-styled cover version with vocals by Robbie Williams appeared on Mark Ronson's 2007 album Version. In 2010, the song was used in a TV advert for Cadbury's chocolate. In 2012 the song featured in the film California Solo.
Tim Burgess, in his memoir Telling Stories, says the single went on to sell 250,000 copies.
Track listing[edit]
All tracks written by Brookes, Day, Collins, Blunt and Burgess
7"
"The Only One I Know" – 4:00
"Everything Changed" – 3:23
12"
"The Only One I Know" – 4:00
"Imperial 109 (Edit)" – 3:44
"Everything Changed" – 3:23
CD
"The Only One I Know" – 4:00
"Imperial 109 (Edit)" – 3:44
"Everything Changed" – 3:23
"You Can Talk to Me" – 4:48
"You Can Talk to Me" was recorded 20 March 1990 for the John Peel Show, BBC Radio 1. First broadcast 9 April 1990.
Charts[edit]
Chart (1990)
Peak
position
Australia (ARIA)[6] 75
Ireland (IRMA)[7] 11
Netherlands (Single Top 100)[8] 56
UK Singles (Official Charts Company)[2] 9
US Billboard Mainstream Rock Tracks[3] 37
US Billboard Modern Rock Tracks[3] 5
References[edit]
^ Jump up to: a b "BBC – Music TV – Pop on trial – 1950s-1990s". BBC Online. Retrieved 5 October 2014.
^ Jump up to: a b "Official Singles Chart Top 100". Official Charts Company. Retrieved 5 October 2014.
^ Jump up to: a b c "Some Friendly – Awards". AllMusic. All Media Network. Retrieved 5 October 2014.
Jump up ^ "September 15, 1990 – Alternative Songs". Billboard. 15 September 1990. Retrieved 5 October 2013.
Jump up ^ Raggett, Ned. "The Charlatans UK – Only One I Know". AllMusic. All Media Network. Retrieved 22 March 2014.
Jump up ^ Ryan, Gavin (2011). Australia's Music Charts 1988–2010. Mt. Martha, VIC, Australia: Moonlight Publishing.
Jump up ^ "The Irish Charts – Search Results – The Only One I Know". Irish Singles Chart. Retrieved 5 October 2014.
Jump up ^ "Dutchcharts.nl – The Charlatans – The Only One I Know" (in Dutch). Single Top 100. Retrieved 5 October 2014.
[hide]
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The Charlatans
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Jon Day
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Studio albums
Some Friendly (1990)
Between 10th and 11th (1992)
Up to Our Hips (1994)
The Charlatans (1995)
Tellin' Stories (1997)
Us and Us Only (1999)
Wonderland (2001)
Up at the Lake (2004)
Simpatico (2006)
You Cross My Path (2008)
Who We Touch (2010)
Modern Nature (2015)
Different Days (2017)
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Heart of palm
From Wikipedia, the free encyclopedia
Jump to: navigation, search
Fresh heart of palm
Heart of palm is a vegetable harvested from the inner core and growing bud of certain palm trees (notably the coconut (Cocos nucifera), palmito juçara (Euterpe edulis), Açaí palm (Euterpe oleracea), sabal (Sabal spp.), pupunha and pejibaye (Bactris gasipaes) palms). Harvesting of many non-cultivated or wild single-stemmed palms results in palm tree death (e.g. Geonoma edulis).[1] However, other palm species are clonal or multi-stemmed plants (e.g. Prestoea acuminata, Euterpe oleracea) and moderate harvesting will not kill the entire clonal palm. Heart of palm may be eaten on its own, and often it is eaten in a salad.
An alternative to wild heart of palm are palm varieties which have undergone a process of adaptation to become a domesticated farm species. The main variety that has been domesticated is the botanical species Bactris gasipaes, known in Ecuador as chontaduro, in Brazil and Costa Rica as palmito, and in English as the peach palm.[2] This variety is the most widely used for canning. Peach palms are self-suckering and produce multiple stems,[3] up to 40 on one plant, so harvesting several stems from a plant is not so expensive because the plant can live on. Another advantage it has over other palms is that it has been selectively bred to eliminate the vicious thorns of its wild cousins. Since harvesting is still a labor-intensive task, palm hearts are regarded as a delicacy.
As of 2008, Costa Rica is the primary source of fresh palm hearts in the US. The Edible Palm Company located in Orlando, Florida has been the largest importer of sustainably farmed Fresh Hearts of Palm from Costa Rica to the United States since 2002. Peach palm is also cultivated in Hawaii,[3] and now has limited distribution on the mainland, primarily to the restaurant trade. Florida's wild Sabal palmetto or cabbage palm was once a source of hearts of palm but is now protected by conservation law.[2]
Contents
[hide]
1 Harvesting
2 Nutrition
3 See also
4 References
Harvesting[edit]
Heart of palm being prepared in Brazil for sale
When harvesting the cultivated young palm, the tree is cut down and the bark is removed leaving layers of white fibers around the center core. During processing the fibers are removed leaving the center core or heart of palm. The center core is attached to a slightly more fibrous cylindrical base with a larger diameter. The entire cylindrical center core and the attached base are edible. The center core is considered more of a delicacy because of its lower fiber content.
Nutrition[edit]
Heart of Palm
Nutritional value per 100 g (3.5 oz)
Energy
79.5 kJ (19.0 kcal)
Carbohydrates
3.1 g
Sugars
0.0 g
Dietary fiber
1.6 g
Fat
0.39 g
Protein
1.55 g
Vitamins
Vitamin A equiv.
(3%)
23.4 μg
Vitamin C
(2%)
1.9 mg
Minerals
Calcium
(5%)
47 mg
Iron
(16%)
2.09 mg
Sodium
(23%)
349 mg
Link to USDA Database entry
Units
μg = micrograms • mg = milligrams
IU = International units
Percentages are roughly approximated using US recommendations for adults.
Source: USDA Nutrient Database
Hearts of palm is rich in fibers, potassium, iron, zinc, phosphorus, copper, vitamins B2, B6, and C.[1]
See also[edit]
Deckenia nobilis
References[edit]
Wikimedia Commons has media related to heart of palm.
Jump up ^ Sylvester, O.; Avalos, G. (2009). Illegal palm heart (Geonoma edulis) harvest in Costa Rican national parks: patterns of consumption and extraction. Economic Botany. 63(2): 179-189.
^ Jump up to: a b Zeldes, Leah A. (2010-11-17). "Eat this! Heart of palm, an exotic taste of the tropics". Dining Chicago. Chicago's Restaurant & Entertainment Guide, Inc. Retrieved 2011-05-18.
^ Jump up to: a b Rose Kahele (August–September 2007). "Big Island Hearts". Hana Hou! Vol. 10, No. 4.
Retrieved from "https://en.wikipedia.org/w/index.php?title=Heart_of_palm&oldid=814257635"
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