text:
Lost in Your Eyes
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"Lost in Your Eyes"
Single by Debbie Gibson
from the album Electric Youth
B-side
"Silence Speaks (A Thousand Words)"
Released
January 6, 1989
Format
7" vinyl
cassette single
Recorded
July–August 1988[citation needed]
Genre
Pop
Length
3:34
Label
Atlantic
Songwriter(s)
Deborah Gibson
Producer(s)
Deborah Gibson
Debbie Gibson singles chronology
"Red Hot"
(1988) "Lost in Your Eyes"
(1989) "Electric Youth"
(1989)
"Red Hot"
(1988) "Lost in Your Eyes"
(1989) "Electric Youth"
(1989)
"Lost in Your Eyes" is the sixth single from American singer-songwriter, Debbie Gibson, and the first from her second album, Electric Youth. First released in January 1989,[1] the ballad climbed to number one on the U.S. Billboard Hot 100 singles chart and remained there for three weeks, becoming her most successful single. Additionally, it reached number three on the Billboard Adult Contemporary chart.
The song was written by Gibson in late 1987[citation needed] and published by Creative Bloc Music, Ltd. and Deborah Ann's Music in early 1988,[citation needed] with the rights eventually administered by the Music Sales Corporation (ASCAP). A beta arrangement had been performed on the Out of the Blue Tour.[citation needed]
One variant mixed from the original multitrack, "Lost in Your Eyes" (Piano and Vocal Mix/3:34), was only available in Europe as Track 3 of the CD3 release #A8970CD. The song is mentioned by name in Kimya Dawson's, "Caving in," as the singer's preferred alternative to "Unchained Melody".
Contents
1 Re-recordings
2 Covers
3 Charts and certifications
3.1 Weekly charts
3.2 Year-end charts
3.3 Certifications
4 See also
5 References
Re-recordings[edit]
In 2006, Gibson rearranged the song with Tim and Ryan O'Neill for the O'Neill Brothers album Someone You Love. In 2010, Gibson re-recorded the song in both English and Japanese as extra tracks for the Japan-exclusive album Ms. Vocalist.
Covers[edit]
Filipino acoustic band Nyoy Volante & The Mannos covered the song on their 2006 self-titled album.
Filipina singer Sarah Geronimo did a cover of this song for her album Music and Me in 2009.
Japanese singer Nana Mizuki did an acoustic rendition of this song in MTV Unplugged, aired January 29, 2017. Mizuki's version is pretty much true to the original arrangement. Nana Mizuki's version (MusicPlayOn)
Charts and certifications[edit]
Weekly charts[edit]
Chart (1988-1989)
Peak
position
Australia (ARIA)[2] 7
Canada (RPM)[3] 1
Belgium (Ultratop 50 Flanders)[4] 34
Ireland (IRMA)[5] 18
Netherlands (Dutch Top 40)[6] 45
New Zealand (Recorded Music NZ)[7] 44
Spain (Spain Top 40 Radio)[8] 34
UK Singles (Official Charts Company)[9] 34
US Billboard Hot 100[10] 1
US Adult Contemporary (Billboard)[11] 3
Year-end charts[edit]
Chart (1989)
Position
Canada Top Singles (RPM)[12] 7
US Billboard Hot 100[13] 13
Certifications[edit]
Region
Certification
Certified units/Sales
Australia (ARIA)[14]
Gold 35,000^
United States (RIAA)[15]
Gold 500,000^
^shipments figures based on certification alone
See also[edit]
Stewie Kills Lois and Lois Kills Stewie
References[edit]
Jump up ^ "Gold & Patinum > Debbie Gibson: 'Lost in Your Eyes'". Recording Industry Association of America. Retrieved September 18, 2017. Release Date: January 6, 1989. Previous Certification(s) Date(s): Gold, March 9, 1989 (Click on "More Details")
Jump up ^ "Australian-charts.com – Debbie Gibson – Lost in Your Eyes". ARIA Top 50 Singles. Retrieved October 26, 2013.
Jump up ^ "Item Display - RPM - Library and Archives Canada (Top Singles - Volume 50, No. 1 May 01, 1989)". RPM. www.collectionscanada.gc.ca. Archived from the original on March 4, 2016. Retrieved 2012-04-30.
Jump up ^ "Ultratop.be – Debbie Gibson – Lost in Your Eyes" (in Dutch). Ultratop 50. Retrieved October 26, 2013.
Jump up ^ "The Irish Charts – Search Results – Lost in Your Eyes". Irish Singles Chart. Retrieved October 26, 2013.
Jump up ^ "Nederlandse Top 40 – Debbie Gibson" (in Dutch). Dutch Top 40. Retrieved October 26, 2013.
Jump up ^ "Charts.nz – Debbie Gibson – Lost in Your Eyes". Top 40 Singles. Retrieved October 26, 2013.
Jump up ^ Fernando Salaverri (September 2005). Sólo éxitos: año a año, 1959–2002 (1st ed.). Spain: Fundación Autor-SGAE. ISBN 84-8048-639-2.
Jump up ^ "Official Singles Chart Top 100". Official Charts Company. Retrieved October 26, 2013.
Jump up ^ "Debbie Gibson Chart History (Hot 100)". Billboard. Retrieved November 20, 2014.
Jump up ^ "Debbie Gibson Chart History (Adult Contemporary)". Billboard. Retrieved February 12, 2015.
Jump up ^ "Top Singles - Volume 51, No. 8, December 23, 1989". RPM. December 23, 1999. Retrieved November 22, 2017.
Jump up ^ "Billboard Top 100 - 1989". Retrieved 2010-12-27.
Jump up ^ "1988 ARIA Singles Chart". ARIA. Retrieved 2016-05-17.
Jump up ^ "American single certifications – Debbie Gibson – Lost in Your Eyes". Recording Industry Association of America. If necessary, click Advanced, then click Format, then select Single, then click SEARCH.
hide
v
t
e
Debbie Gibson
Discography
Studio albums
Out of the Blue (1987)
Electric Youth (1989)
Anything Is Possible (1990)
Body, Mind, Soul (1993)
Think with Your Heart (1995)
Deborah (1997)
M.Y.O.B. (2001)
Colored Lights: The Broadway Album (2003)
Ms. Vocalist (2010/2011)
Compilation albums
Greatest Hits (1995)
Lost in Your Eyes and Other Hits (1999)
Memory Lane, Volume 1 (2005)
Memory Lane, Volume 2 (2005)
Singles
"Only in My Dreams" (1986)
"Shake Your Love" (1987)
"Out of the Blue" (1987)
"Foolish Beat" (1988)
"Staying Together" (1988)
"Red Hot" (1988)
"Lost in Your Eyes" (1989)
"Electric Youth" (1989)
"No More Rhyme" (1989)
"We Could Be Together" (1989)
"Without You" (1990)
"Anything Is Possible" (1990)
"(This So-Called) Miracle" (1991)
"One Hand, One Heart" (1991)
"One Step Ahead" (1991)
"Sure" (1991)
"In His Mind" (1992)
"Losin' Myself" (1993)
"Eyes of the Child" (1993)
"Shock Your Mama" (1993)
"How Can This Be?" (1993)
"Free Me" (1993)
"For Better or Worse" (1995)
"Only in My Dreams 1998" (1998)
"Naturally" (1998)
"What You Want" (2000)
Related articles
Electric Youth (fragrance)
"Debbie Gibson Is Pregnant with My Two-Headed Love Child"
Book
Category
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Extracellular matrix
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Extracellular matrix
Illustration depicting extracellular matrix (basement membrane and interstitial matrix) in relation to epithelium, endothelium and connective tissue
Details
Identifiers
Latin
Matrix Extracellularis
Acronym(s)
ECM
MeSH
D005109
TH
H2.00.03.0.02001
Anatomical terms of microanatomy
[edit on Wikidata]
In biology, the extracellular matrix (ECM) is a collection of extracellular molecules secreted by support cells that provides structural and biochemical support to the surrounding cells.[1][2] Because multicellularity evolved independently in different multicellular lineages, the composition of ECM varies between multicellular structures; however, cell adhesion, cell-to-cell communication and differentiation are common functions of the ECM.[3]
The animal extracellular matrix includes the interstitial matrix and the basement membrane.[4] Interstitial matrix is present between various animal cells (i.e., in the intercellular spaces). Gels of polysaccharides and fibrous proteins fill the interstitial space and act as a compression buffer against the stress placed on the ECM.[5] Basement membranes are sheet-like depositions of ECM on which various epithelial cells rest. Each type of connective tissue in animals has a type of ECM: collagen fibers and bone mineral comprise the ECM of bone tissue; reticular fibers and ground substance comprise the ECM of loose connective tissue; and blood plasma is the ECM of blood.
The plant ECM includes cell wall components, like cellulose, in addition to more complex signaling molecules.[6] Some single-celled organisms adopt multicellular biofilms in which the cells are embedded in an ECM composed primarily of extracellular polymeric substances (EPS).[7]
Contents
1 Structure
1.1 Proteoglycans
1.1.1 Heparan sulfate
1.1.2 Chondroitin sulfate
1.1.3 Keratan sulfate
1.2 Non-proteoglycan polysaccharide
1.2.1 Hyaluronic acid
1.3 Proteins
1.3.1 Collagen
1.3.2 Elastin
1.4 Extracellular vesicles
1.5 Other
1.5.1 Fibronectin
1.5.2 Laminin
2 Development
3 Physiology
3.1 Stiffness and elasticity
3.1.1 Effect on gene expression
3.1.2 Effect on differentiation
3.1.3 Durotaxis
4 Function
4.1 Cell adhesion
5 Clinical significance
6 In plants
7 In pluriformea + filozoa
8 History
9 See also
10 References
11 Further reading
Structure[edit]
Components of the ECM are produced intracellularly by resident cells and secreted into the ECM via exocytosis.[8] Once secreted, they then aggregate with the existing matrix. The ECM is composed of an interlocking mesh of fibrous proteins and glycosaminoglycans (GAGs).
Proteoglycans[edit]
Glycosaminoglycans (GAGs) are carbohydrate polymers and mostly attached to extracellular matrix proteins to form proteoglycans (hyaluronic acid is a notable exception, see below). Proteoglycans have a net negative charge that attracts positively charged sodium ions (Na+), which attracts water molecules via osmosis, keeping the ECM and resident cells hydrated. Proteoglycans may also help to trap and store growth factors within the ECM.
Described below are the different types of proteoglycan found within the extracellular matrix.
Heparan sulfate[edit]
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan (PG) in which two or three HS chains are attached in close proximity to cell surface or ECM proteins.[9][10] It is in this form that HS binds to a variety of protein ligands and regulates a wide variety of biological activities, including developmental processes, angiogenesis, blood coagulation, and tumour metastasis.
In the extracellular matrix, especially basement membranes, the multi-domain proteins perlecan, agrin, and collagen XVIII are the main proteins to which heparan sulfate is attached.
Chondroitin sulfate[edit]
Chondroitin sulfates contribute to the tensile strength of cartilage, tendons, ligaments, and walls of the aorta. They have also been known to affect neuroplasticity.[11]
Keratan sulfate[edit]
Keratan sulfates have a variable sulfate content and, unlike many other GAGs, do not contain uronic acid. They are present in the cornea, cartilage, bones, and the horns of animals.
Non-proteoglycan polysaccharide[edit]
Hyaluronic acid[edit]
Hyaluronic acid (or "hyaluronan") is a polysaccharide consisting of alternating residues of D-glucuronic acid and N-acetylglucosamine, and unlike other GAGs, is not found as a proteoglycan. Hyaluronic acid in the extracellular space confers upon tissues the ability to resist compression by providing a counteracting turgor (swelling) force by absorbing significant amounts of water. Hyaluronic acid is thus found in abundance in the ECM of load-bearing joints. It is also a chief component of the interstitial gel. Hyaluronic acid is found on the inner surface of the cell membrane and is translocated out of the cell during biosynthesis.[12]
Hyaluronic acid acts as an environmental cue that regulates cell behavior during embryonic development, healing processes, inflammation, and tumor development. It interacts with a specific transmembrane receptor, CD44.[13]
Proteins[edit]
Collagen[edit]
Collagens are the most abundant protein in the ECM. In fact, collagen is the most abundant protein in the human body[14][15] and accounts for 90% of bone matrix protein content.[16] Collagens are present in the ECM as fibrillar proteins and give structural support to resident cells. Collagen is exocytosed in precursor form (procollagen), which is then cleaved by procollagen proteases to allow extracellular assembly. Disorders such as Ehlers Danlos Syndrome, osteogenesis imperfecta, and epidermolysis bullosa are linked with genetic defects in collagen-encoding genes.[8] The collagen can be divided into several families according to the types of structure they form:
Fibrillar (Type I, II, III, V, XI)
Facit (Type IX, XII, XIV)
Short chain (Type VIII, X)
Basement membrane (Type IV)
Other (Type VI, VII, XIII)
Elastin[edit]
Elastins, in contrast to collagens, give elasticity to tissues, allowing them to stretch when needed and then return to their original state. This is useful in blood vessels, the lungs, in skin, and the ligamentum nuchae, and these tissues contain high amounts of elastins. Elastins are synthesized by fibroblasts and smooth muscle cells. Elastins are highly insoluble, and tropoelastins are secreted inside a chaperone molecule, which releases the precursor molecule upon contact with a fiber of mature elastin. Tropoelastins are then deaminated to become incorporated into the elastin strand. Disorders such as cutis laxa and Williams syndrome are associated with deficient or absent elastin fibers in the ECM.[8]
Extracellular vesicles[edit]
In 2016, Huleihel et al., reported the presence of DNA, RNA, and Matrix-bound nanovesicles (MBVs) within ECM bioscaffolds.[17] MBVs shape and size were found to be consistent with previously described exosomes. MBVs cargo includes different protein molecules, lipids, DNA, fragments, and miRNAs. Similar to ECM bioscaffolds, MBVs can modify the activation state of macrophages and alter different cellular properties such as; proliferation, migration and cell cycle. MBVs are now believed to be an integral and functional key component of ECM bioscaffolds.
Other[edit]
Fibronectin[edit]
Fibronectins are glycoproteins that connect cells with collagen fibers in the ECM, allowing cells to move through the ECM. Fibronectins bind collagen and cell-surface integrins, causing a reorganization of the cell's cytoskeleton to facilitate cell movement. Fibronectins are secreted by cells in an unfolded, inactive form. Binding to integrins unfolds fibronectin molecules, allowing them to form dimers so that they can function properly. Fibronectins also help at the site of tissue injury by binding to platelets during blood clotting and facilitating cell movement to the affected area during wound healing.[8]
Laminin[edit]
Laminins are proteins found in the basal laminae of virtually all animals. Rather than forming collagen-like fibers, laminins form networks of web-like structures that resist tensile forces in the basal lamina. They also assist in cell adhesion. Laminins bind other ECM components such as collagens and nidogens.[8]
Development[edit]
There are many cell types that contribute to the development of the various types of extracellular matrix found in plethora of tissue types. The local components of ECM determine the properties of the connective tissue.
Fibroblasts are the most common cell type in connective tissue ECM, in which they synthesize, maintain, and provide a structural framework; fibroblasts secrete the precursor components of the ECM, including the ground substance. Chondrocytes are found in cartilage and produce the cartilagenous matrix. Osteoblasts are responsible for bone formation.
Physiology[edit]
Stiffness and elasticity[edit]
The ECM can exist in varying degrees of stiffness and elasticity, from soft brain tissues to hard bone tissues. The elasticity of the ECM can differ by several orders of magnitude. This property is primarily dependent on collagen and elastin concentration,[18] and it has recently been shown to play an influential role in regulating numerous cell functions.
Cells can sense the mechanical properties of their environment by applying forces and measuring the resulting backlash.[19] This plays an important role because it helps regulate many important cellular processes including cellular contraction,[20] cell migration,[21] cell proliferation,[22] differentiation[23] and cell death (apoptosis).[24] Inhibition of nonmuscle myosin II blocks most of these effects,[23][21][20] indicating that they are indeed tied to sensing the mechanical properties of the ECM, which has become a new focus in research during the past decade.
Effect on gene expression[edit]
Differing mechanical properties in ECM exert effects on both cell behaviour and gene expression. Although the mechanism by which this is done has not been thoroughly explained, adhesion complexes and the actin-myosin cytoskeleton, whose contractile forces are transmitted through transcellular structures are thought to play key roles in the yet to be discovered molecular pathways.[20]
Effect on differentiation[edit]
ECM elasticity can direct cellular differentiation, the process by which a cell changes from one cell type to another. In particular, naive mesenchymal stem cells (MSCs) have been shown to specify lineage and commit to phenotypes with extreme sensitivity to tissue-level elasticity. MSCs placed on soft matrices that mimic brain differentiate into neuron-like cells, showing similar shape, RNAi profiles, cytoskeletal markers, and transcription factor levels. Similarly stiffer matrices that mimic muscle are myogenic, and matrices with stiffnesses that mimic collagenous bone are osteogenic.[23]
Durotaxis[edit]
Main article: Durotaxis
Stiffness and elasticity also guide cell migration, this process is called durotaxis. The term was coined by Lo CM and colleagues when they discovered the tendency of single cells to migrate up rigidity gradients (towards more stiff substrates)[21] and has been extensively studied since. The molecular mechanisms behind durotaxis are thought to exist primarily in the focal adhesion, a large protein complex that acts as the primary site of contact between the cell and the ECM.[25] This complex contains many proteins that are essential to durotaxis including structural anchoring proteins (integrins) and signaling proteins (adhesion kinase (FAK), talin, vinculin, paxillin, α-actinin, GTPases etc.) which cause changes in cell shape and actomyosin contractility.[26] These changes are thought to cause cytoskeletal rearrangements in order to facilitate directional migration.
Function[edit]
Due to its diverse nature and composition, the ECM can serve many functions, such as providing support, segregating tissues from one another, and regulating intercellular communication. The extracellular matrix regulates a cell's dynamic behavior. In addition, it sequesters a wide range of cellular growth factors and acts as a local store for them.[4] Changes in physiological conditions can trigger protease activities that cause local release of such stores. This allows the rapid and local growth factor-mediated activation of cellular functions without de novo synthesis. This effect has been explored in a modelling and theoretical study wherein VEGFC, MMP2, and collagen I were used as an example.[27]
Formation of the extracellular matrix is essential for processes like growth, wound healing, and fibrosis. An understanding of ECM structure and composition also helps in comprehending the complex dynamics of tumor invasion and metastasis in cancer biology as metastasis often involves the destruction of extracellular matrix by enzymes such as serine proteases, threonine proteases, and matrix metalloproteinases.[4][28]
The stiffness and elasticity of the ECM has important implications in cell migration, gene expression,[29] and differentiation.[23] Cells actively sense ECM rigidity and migrate preferentially towards stiffer surfaces in a phenomenon called durotaxis.[21] They also detect elasticity and adjust their gene expression accordingly which has increasingly become a subject of research because of its impact on differentiation and cancer progression.[30]
Cell adhesion[edit]
Many cells bind to components of the extracellular matrix. Cell adhesion can occur in two ways; by focal adhesions, connecting the ECM to actin filaments of the cell, and hemidesmosomes, connecting the ECM to intermediate filaments such as keratin. This cell-to-ECM adhesion is regulated by specific cell-surface cellular adhesion molecules (CAM) known as integrins. Integrins are cell-surface proteins that bind cells to ECM structures, such as fibronectin and laminin, and also to integrin proteins on the surface of other cells.
Fibronectins bind to ECM macromolecules and facilitate their binding to transmembrane integrins. The attachment of fibronectin to the extracellular domain initiates intracellular signalling pathways as well as association with the cellular cytoskeleton via a set of adaptor molecules such as actin.[5]
Clinical significance[edit]
See also: Regenerative medicine
Extracellular matrix has been found to cause regrowth and healing of tissue. Although the mechanism of action by which extracellular matrix promotes constructive remodeling of tissue is still unknown, researchers now believe that Matrix-bound nanovesicles (MBVs) are a key player in the healing process.[17][31] In human fetuses, for example, the extracellular matrix works with stem cells to grow and regrow all parts of the human body, and fetuses can regrow anything that gets damaged in the womb. Scientists have long believed that the matrix stops functioning after full development. It has been used in the past to help horses heal torn ligaments, but it is being researched further as a device for tissue regeneration in humans.[32]
In terms of injury repair and tissue engineering, the extracellular matrix serves two main purposes. First, it prevents the immune system from triggering from the injury and responding with inflammation and scar tissue. Next, it facilitates the surrounding cells to repair the tissue instead of forming scar tissue.[32]
For medical applications, the ECM required is usually extracted from pig bladders, an easily accessible and relatively unused source. It is currently being used regularly to treat ulcers by closing the hole in the tissue that lines the stomach, but further research is currently being done by many universities as well as the U.S. Government for wounded soldier applications. As of early 2007, testing was being carried out on a military base in Texas. Scientists are using a powdered form on Iraq War veterans whose hands were damaged in the war.[33]
Not all ECM devices come from the bladder. Extracellular matrix coming from pig small intestine submucosa are being used to repair "atrial septal defects" (ASD), "patent foramen ovale" (PFO) and inguinal hernia. After one year 95% of the collagen ECM in these patches is replaced by the normal soft tissue of the heart.[34]
Extracellular matrix proteins are commonly used in cell culture systems to maintain stem and precursor cells in an undifferentiated state during cell culture and function to induce differentiation of epithelial, endothelial and smooth muscle cells in vitro. Extracellular matrix proteins can also be used to support 3D cell culture in vitro for modelling tumor development.[35]
A class of biomaterials derived from processing human or animal tissues to retain portions of the extracellular matrix are called ECM Biomaterial.
In plants[edit]
Plant cells are tessellated to form tissues. The cell wall is the relatively rigid structure surrounding the plant cell. The cell wall provides lateral strength to resist osmotic turgor pressure, but it is flexible enough to allow cell growth when needed; it also serves as a medium for intercellular communication. The cell wall comprises multiple laminate layers of cellulose microfibrils embedded in a matrix of glycoproteins, including hemicellulose, pectin, and extensin. The components of the glycoprotein matrix help cell walls of adjacent plant cells to bind to each other. The selective permeability of the cell wall is chiefly governed by pectins in the glycoprotein matrix. Plasmodesmata (singular: plasmodesma) are pores that traverse the cell walls of adjacent plant cells. These channels are tightly regulated and selectively allow molecules of specific sizes to pass between cells.[12]
In pluriformea + filozoa[edit]
The extracellular matrix functionality of animals/metazoa developed in the common ancestor of the pluriformea and filozoa, after the Ichthyosporea diverged.
History[edit]
The importance of the extracellular matrix has long been recognized (Lewis, 1922), but the usage of the term is more recent (Gospodarowicz et al., 1979).[36][37][38][39]
See also[edit]
Perineuronal net
Interstitium
References[edit]
Jump up ^ Michel, Gurvan; Thierry Tonon; Delphine Scornet; J. Mark Cock; Bernard Kloareg (October 2010). "The cell wall polysaccharide metabolism of the brown alga Ectocarpus siliculosus. Insights into the evolution of extracellular matrix polysaccharides in Eukaryotes". New Phytologist. 188 (1): 82–97. doi:10.1111/j.1469-8137.2010.03374.x.
Jump up ^ Alberts, Bruce (2002). Molecular biology of the cell (4. ed.). New York [u.a.]: Garland. ISBN 0-8153-4072-9.
Jump up ^ Abedin, Monika; Nicole King (December 2010). "Diverse evolutionary paths to cell adhesion". Trends in Cell Biology. 20 (12): 734–742. doi:10.1016/j.tcb.2010.08.002. PMC 2991404  . PMID 20817460.
^ Jump up to: a b c Kumar; Abbas; Fausto. Robbins and Cotran: Pathologic Basis of Disease (7th ed.). Philadelphia: Elsevier. ISBN 0-7216-0187-1.
^ Jump up to: a b Alberts B, Bray D, Hopin K, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2004). "Tissues and Cancer". Essential cell biology. New York and London: Garland Science. ISBN 0-8153-3481-8.
Jump up ^ Brownlee, Colin (October 2002). "Role of the extracellular matrix in cell-cell signalling: paracrine paradigms". Current Opinion in Plant Biology. 5 (5): 396–401. doi:10.1016/S1369-5266(02)00286-8.
Jump up ^ Kostakioti, Maria (2013). "Bacterial Biofilms: Development, Dispersal, and Therapeutic Strategies in the Dawn of the Postantibiotic Era". Cold Spring Harbor Perspectives in Medicine.
^ Jump up to: a b c d e Plopper G (2007). The extracellular matrix and cell adhesion, in Cells (eds Lewin B, Cassimeris L, Lingappa V, Plopper G). Sudbury, MA: Jones and Bartlett. ISBN 0-7637-3905-7.
Jump up ^ Gallagher, J.T.; Lyon, M. (2000). "Molecular structure of Heparan Sulfate and interactions with growth factors and morphogens". In Iozzo, R. V. Proteoglycans: structure, biology and molecular interactions. Marcel Dekker Inc. New York, New York. pp. 27–59. ISBN 9780824703349.
Jump up ^ Iozzo, R. V. (1998). "Matrix proteoglycans: from molecular design to cellular function". Annu. Rev. Biochem. 67 (1): 609–652. doi:10.1146/annurev.biochem.67.1.609. PMID 9759499.
Jump up ^ Hensch TK (2005). "Critical period mechanisms in developing visual cortex". Curr. Top. Dev. Biol. 69: 215–237. doi:10.1016/S0070-2153(05)69008-4. PMID 16243601.
^ Jump up to: a b Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, Zipursky SL, Darnell J. "Integrating Cells Into Tissues". Molecular Cell Biology (5th ed.). New York: WH Freeman and Company. pp. 197–234.
Jump up ^ Peach RJ, Hollenbaugh D, Stamenkovic I, Aruffo A (July 1993). "Identification of hyaluronic acid binding sites in the extracellular domain of CD44". J. Cell Biol. 122 (1): 257–264. doi:10.1083/jcb.122.1.257. PMC 2119597  . PMID 8314845.
Jump up ^ Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (2002). "Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen". J. Biol. Chem. 277 (6): 4223–4231. doi:10.1074/jbc.M110709200. PMID 11704682.
Jump up ^ Karsenty G, Park RW (1995). "Regulation of type I collagen genes expression". Int. Rev. Immunol. 12 (2–4): 177–185. doi:10.3109/08830189509056711. PMID 7650420.
Jump up ^ Kern B, Shen J, Starbuck M, Karsenty G (2001). "Cbfa1 contributes to the osteoblast-specific expression of type I collagen genes". J. Biol. Chem. 276 (10): 7101–7107. doi:10.1074/jbc.M006215200. PMID 11106645.
^ Jump up to: a b Huleihel, Luai; Hussey, George S.; Naranjo, Juan Diego; Zhang, Li; Dziki, Jenna L.; Turner, Neill J.; Stolz, Donna B.; Badylak, Stephen F. (2016-06-01). "Matrix-bound nanovesicles within ECM bioscaffolds". Science Advances. 2 (6): e1600502. doi:10.1126/sciadv.1600502. ISSN 2375-2548. PMC 4928894  . PMID 27386584.
Jump up ^ Alberts, Bruce (2002). Molecular biology of the cell. Garland Science. ISBN 0-8153-3218-1.
Jump up ^ Plotnikov SV, Pasapera AM, Sabass B, Waterman CM (2012). "Force fluctuations within focal adhesions mediate ECM-rigidity sensing to guide directed cell migration". Cell. 151 (7): 1513–27. doi:10.1016/j.cell.2012.11.034. PMC 3821979  . PMID 23260139.
^ Jump up to: a b c Discher DE; Janmey P.; Wang YL (2005). "Tissue cells feel and respond to the stiffness of their substrate". Science. 310: 1139–1143. doi:10.1126/science.1116995. PMID 16293750.
^ Jump up to: a b c d Lo CM, Wang HB, Dembo M, Wang YL (2000). "Cell movement is guided by the rigidity of the substrate". Biophys J. 79 (1): 144–52. doi:10.1016/S0006-3495(00)76279-5. PMC 1300921  . PMID 10866943.
Jump up ^ Hadjipanayi E, Mudera V, Brown RA (2009). "Close dependence of fibroblast proliferation on collagen scaffold matrix stiffness". J. Tissue Eng. 3 (2): 77–84. doi:10.1002/term.136. PMID 19051218.
^ Jump up to: a b c d Engler AJ, Sen S, Sweeney HL, Discher DE (2006). "Matrix elasticity directs stem cell lineage specification". Cell. 126 (4): 677–89. doi:10.1016/j.cell.2006.06.044. PMID 16923388.
Jump up ^ Wang HB, Dembo M, Wang YL (2000). "Substrate flexibility regulates growth and apoptosis of normal but not transformed cells". Am J Physiol Cell Physiol. 279 (5): 1345–50. PMID 11029281.
Jump up ^ Allen JL, Cooke ME, Alliston T (25 July 2012). "ECM stiffness primes the TGF pathway to promote chondrocyte differentiation". Molecular Biology of the Cell. 23 (18): 3731–3742. doi:10.1091/mbc.E12-03-0172. PMC 3442419  . PMID 22833566. CS1 maint: Uses authors parameter (link)
Jump up ^ Kanchanawong P, Shtengel G, Pasapera AM, Ramko EB, Davidson MW, Hess HF, Waterman CM (25 November 2010). "Nanoscale architecture of integrin-based cell adhesions". Nature. 468 (7323): 580–584. doi:10.1038/nature09621. PMC 3046339  . PMID 21107430.
Jump up ^ Wertheim, Kenneth Y.; Roose, Tiina (2017-4). "A Mathematical Model of Lymphangiogenesis in a Zebrafish Embryo". Bulletin of Mathematical Biology. 79 (4): 693–737. doi:10.1007/s11538-017-0248-7. ISSN 1522-9602. PMC 5501200  . PMID 28233173. Check date values in: |date= (help)
Jump up ^ Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S (1980). "Metastatic potential correlates with enzymatic degradation of basement membrane collagen". Nature. 284 (5751): 67–68. doi:10.1038/284067a0. PMID 6243750.
Jump up ^ Wang JH, Thampatty BP, Lin JS, Im HJ (2007). "Mechanoregulation of gene expression in fibroblasts". Gene. 391: 1–15. doi:10.1016/j.gene.2007.01.014. PMC 2893340  . PMID 17331678.
Jump up ^ Provenzano PP; Inman DR; Eliceiri KW; Keely PJ (2009). "Matrix density-induced mechanoregulation of breast cell phenotype, signaling and gene expression through a FAK-ERK linkage". Oncogene. 28 (49): 4326–4343. doi:10.1038/onc.2009.299. PMC 2795025  . PMID 19826415.
Jump up ^ "Pitt researchers solve mystery on how regenerative medicine works". EurekAlert!. Retrieved 2017-03-01.
^ Jump up to: a b 'Pixie dust' helps man grow new finger
Jump up ^ HowStuffWorks, Humans Can Regrow Fingers? In 2009, the St. Francis Heart Center announced the use of the extracellular matrix technology in repair surgery. Archived March 10, 2007, at the Wayback Machine.
Jump up ^ "First Ever Implantation of Bioabsorbable Biostar Device at DHZB". DHZB NEWS. December 2007. Retrieved 2008-08-05. The almost transparent collagen matrix consists of medically purified pig intestine, which is broken down by the scavenger cells (macrophages) of the immune system. After about 1 year the collagen has been almost completely (90-95%) replaced by normal body tissue: only the tiny metal framework remains. An entirely absorbable implant is currently under development.
Jump up ^ Kleinman, H.K.; Luckenbill-Edds, L.; Cannon, F.W.; Sephel, G.C. (October 1987). "Use of extracellularmatrix components for cell culture". Analytical Biochemistry. 186 (1): 1–13. doi:10.1016/0003-2697(87)90538-0. Retrieved 2012-05-14.
Jump up ^ Lewis WH (1922). "The adhesive quality of cells". Anat Rec. 23: 387–392. doi:10.1002/ar.1090230708. CS1 maint: Uses authors parameter (link)
Jump up ^ Gospodarowicz, D., Vlodovsky, I., Greenburg, G., and Johnson, L. K. (1979). In: Hormones and Cell Culture (G. H. Sato and R. Ross, eds.), p. 561.
Jump up ^ Mecham, R. P. (ed.). The extracellular matrix: an overview. New York: Springer. 2011, [1].
Jump up ^ Rieger, R.; Michaelis, A.; Green, M.M. 1991. Glossary of Genetics. Classical and Molecular (Fifth edition). Springer-Verlag, Berlin, 553 pp., [2].
Further reading[edit]
[ ANAT3231 Lecture 08 Extracellular Matrix] - Lecture about extracellular matrix from UNSW Cell Biology website.
Extracellular matrix: review of its roles in acute and chronic wounds
Usage of Extracellular Matrix from pigs to regrow human extremities
"The Extracellular Matrix of Animals", from Chapter 19 of The Molecular Biology of the Cell, 4th edition, Alberts et al.
Biology, John W. Kimball. An online Biology textbook.
[3], The man who grew a finger, By Matthew Price, BBC news
Sound Medicine - Heart Tissue Regeneration - July 19 interview discussing ECM and its uses in cardiac tissue repair (requires MP3 playback) [broken link].
Growing Body Parts - A December 2009 report by 60 Minutes
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Connective tissue
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Protein: scleroproteins
Extracellular matrix
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type I
COL1A1
COL1A2
type II (COL2A1)
type III
type V
COL5A1
COL5A2
COL5A3
COL24A1
COL26A1
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COL9A1
COL9A2
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type XII (COL12A1)
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COL22A1
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COL4A1
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COL4A5
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type XVIII
COL18A1
Endostatin
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type VIII
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Priest (Latter Day Saints)
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Priest is a priesthood office in the Aaronic priesthood of denominations within the Latter Day Saint movement, including The Church of Jesus Christ of Latter-day Saints (LDS Church).
Contents
1 Priests in The Church of Jesus Christ of Latter-day Saints
2 Priests in the Community of Christ
3 Priest in The Church of Jesus Christ (Bickertonite)
4 References
Priests in The Church of Jesus Christ of Latter-day Saints[edit]
In the LDS Church, priest is the third of four offices of the Aaronic priesthood. Male members who reach the age of 16 and male converts 16 and over are eligible to become ordained priests.[1] An interview with and approval by the bishop is required before ordination.[1] Prior to ordination, the proposed ordination must also be accepted by common consent by the members of the ward.[1] With the approval of the bishop, a priest or a holder of the Melchizedek priesthood may ordain a person to the office of priest by the laying on of hands. All priests in a ward are members of a priests quourm. A priests quorum can have a maximum of 48 members.[2]
The president of the priests quorum is the bishop, who holds the keys of the priesthood for this quorum. The bishop typically chooses a first and second assistant and a secretary from among the members of the quorum. These officers may not be set apart until after they have been accepted by the common consent of the members of the quorum.[3]
According to the Doctrine and Covenants, the duty of a priest is to "preach, teach, expound, exhort, and baptize, and administer the sacrament".[4] Accordingly, priests bless the sacrament and are permitted to perform baptism. They can also ordain deacons, teachers, and priests and confer the Aaronic priesthood upon others. A priest must receive the approval of the bishop prior to performing any of these actions. Usually, a priest will be paired with a man (often their father) as a home teacher. Priests also have all the duties and authority of a teacher and a deacon.
The adult president of the local Young Men organization advises the priests quorum. Sometimes an assistant advisor is also selected.
As the church in North America sponsors troops of the Boy Scouts of America and Scouts Canada programs, many priests participate in scouting programs. The adult ward leaders of the Young Men organization are frequently also leaders in the Scout troop, but the priesthood quorums and the Scouts are not otherwise connected.
In 1908, Joseph F. Smith organized a committee to standardize and reform the Aaronic Priesthood quorums. This committee standardized the age requirements for young men to be ordained to the office of Teacher or Priest.[5] Before that time there were not set ages for ordination. A priest who turns 18 years old, or graduates from high school, depending on the situation, is integrated into the elders quorum. Those who are 18 years old and approved by the bishop and stake president may receive the Melchizedek priesthood and become an elder.
Priests usually spend much time preparing for future service as a missionary. All suitable young men in the church are asked to serve missions, with the option to do so at age 18 if they have graduated from high school.
Priests in the Community of Christ[edit]
Main article: Priesthood (Community of Christ)
In the Community of Christ, a priest is an adult, who is a congregation-focused[6] "Minister of Presence" in the Aaronic Priesthood.[7] Their stated purpose is to "express their ministry of presence and model Jesus as Friend by being a spiritual friend to families, congregations, and community."[8][9] Each congregation should have a designated bishop or stewardship commissioner who is responsible for Aaronic ministry in that congregation. A priest is to meet the needs of their congregation by following the annual Aaronic Ministry Plan in place for their specific congregation.[9]
Priest in The Church of Jesus Christ (Bickertonite)[edit]
The Church of Jesus Christ (Bickertonite) does not recognize priest as a specific office of the priesthood.[10]
References[edit]
Book: Priesthood (LDS Church)
LDS Church portal
Book of Mormon portal
^ Jump up to: a b c "Ordinance and Blessing Policies", Handbook 1: Stake Presidents and Bishops (Salt Lake City, Utah: LDS Church, 2010) § 16.
Jump up ^ Doctrine and Covenants, Section 107:87
Jump up ^ "Callings in the Church", Handbook 2: Administering the Church (Salt Lake City, Utah: LDS Church, 2010) § 19.
Jump up ^ Doctrine and Covenants, Section 20:46
Jump up ^ Hartley, William (1973). "The Priesthood Reform Movement, 1908-1922". Brigham Young University Studies. |access-date= requires |url= (help)
Jump up ^ "Archived copy". Archived from the original on 2012-07-22. Retrieved 2011-03-11.
Jump up ^ http://www.cofchrist.org/aaronic/aaronicministrybrochure.pdf[permanent dead link]
Jump up ^ "Archived copy". Archived from the original on 2012-07-29. Retrieved 2011-03-11.
^ Jump up to: a b http://www.cofchrist.org/aaronic/focusbrochure.pdf[permanent dead link]
Jump up ^ "Archived copy". Archived from the original on 2012-09-13. Retrieved 2011-03-11.
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Dancing with the Stars (Irish TV series)
From Wikipedia, the free encyclopedia
Jump to: navigation, search
For the upcoming second series, see Dancing with the Stars (Irish series 2).
Dancing with the Stars
Genre
Talent show
Created by
Fenia Vardanis
Richard Hopkins
Karen Smith
Presented by
Amanda Byram
Nicky Byrne
Judges
Julian Benson
Loraine Barry
Brian Redmond
Darren Bennett
Voices of
Jack Boylan
Country of origin
Republic of Ireland
Original language(s)
English
No. of series
1
No. of episodes
12 (as of 26 March 2017)
Production
Location(s)
Ardmore Studios
Running time
120 minutes
Production company(s)
ShinAwil
Release
Original network
RTÉ One
Picture format
720p (HDTV)
Original release
8 January 2017 (2017-01-08) – present
Chronology
Related shows
Strictly Come Dancing
Dancing with the Stars
Dancing with the Stars is an Irish reality television series, airing on RTÉ One that started on 8 January 2017,[1] hosted by Amanda Byram and Nicky Byrne.[2] The show is based on the original UK version, and is part of the Dancing with the Stars franchise.[3] The judging panel consists of Julian Benson, Loraine Barry and Brian Redmond.[4][5] On 16 June 2017, it was announced by RTÉ that it will be returning for a second series.[6]
Contents
[hide]
1 Production
2 Format
2.1 Judges and hosts
2.2 Professional dancers and their partners
3 Main series results
3.1 Series 1 (2017)
3.2 Series 2 (2018)
4 References
5 External links
Production[edit]
In August 2016, it was confirmed that RTÉ One would broadcast an Irish version of Dancing with the Stars, which would replace the successful The Voice of Ireland, which was cancelled in order for the broadcaster to order the new show.[7] A producer of the show commented, "We've got fantastic production people in Ireland who, I believe, deliver a show that's comparable with any of those shows on a fraction of the budget. So we're looking forward to the task of doing this equally the same way."[7]
Format[edit]
The format of the series follows celebrities being paired up with professional dancers, who perform predetermined dances each week for judges' scores and public votes, with the couple with the lowest amount of points being eliminated, until the winning couple remains.[3]
Judges and hosts[edit]
On 18 December 2016, RTÉ confirmed that Julian Benson, Loraine Barry and Brian Redmond would be the judges on the programme.[4][5] Creative producer Darren Bennett stood in for Benson, during week five, six, seven and eight, who was absent due to illness.
People in the running to be host of the show included former Westlife musician and 2012 Strictly Come Dancing contestant Nicky Byrne; as well as popular radio host Ray D'Arcy, though D'Arcy ruled himself out of the running in August 2016.[7] In October 2016, it was reported that Marty Whelan had auditioned to host the show. In November, it was reported that Amanda Byram had been selected as one of the hosts.[2][8] In December, it was confirmed that Byrne would host alongside Byram.[9] It was also confirmed that Bláthnaid Treacy would be hosting RTÉ Two spin-off show, Can't Stop Dancing, airing on Friday nights before the live shows.[10]
Professional dancers and their partners[edit]
[hide]Professional
Average
Series 1
Series 2
Curtis Pritchard
19.0 Thalia Heffernan
Emily Barker
16.0 Hughie Maughan
Giulia Dotta
22.0 Des Bishop
John Nolan
16.6 Teresa Mannion
Kai Widdrington
20.9 Katherine Lynch
Karen Byrne
16.4 Des Cahill
Ksenia Zsikhotska
24.4 Dayl Cronin
Robert Rowiński
N/A
Ryan McShane
26.3 Denise McCormack
Sean Smullen
14.3 Dr. Eva Orsmond N/A
Valeria Milova
22.6 Aidan O'Mahony
Vitali Kozmin
26.5 Aoibhín Garrihy
Key:
Winner of the series
Second place
Third place
First elimination of the series
Withdrew in the series
Participating in current series
It should be noted that Week 7 of Series 1 was 'Switch-Up Week' in which the celebrities danced with different pros for one week only. The table above reflects this as it excludes each pro's regular celebrity partner's Switch-Up Week score and includes their Switch-Up Week partner's score.
Main series results[edit]
Series
Premiere date
Finale date
Number
of couples
Number
of weeks
Winners
Runners-up
1
8 January 2017 26 March 2017 11 12 Aidan O'Mahony & Valeria Milova Denise McCormack & Ryan McShane
Aoibhín Garrihy & Vitali Kozmin
2
7 January 2018 25 March 2018 11 12
Series 1 (2017)[edit]
Main article: Dancing with the Stars (Irish series 1)
The first series of Dancing with the Stars started on 8 January 2017 and finished on 26 March 2017.
Series 2 (2018)[edit]
Main article: Dancing with the Stars (Irish series 2)
The second series will begin on 7 January 2018.[11][12]
References[edit]
Jump up ^ Curran, Sarah (October 21, 2016). "Marty Whelan Auditions to Host Dancing with the Stars!". RSVP Magazine. Retrieved November 4, 2016.
^ Jump up to: a b Entertainment.ie (18 November 2016). "Irish 'Dancing with the Stars' have reportedly chosen their host".
^ Jump up to: a b "Dancing with the Stars to take centre stage on RTÉ One". RTÉ.
^ Jump up to: a b O'Donnell, Áine (18 December 2016). "The judges for Dancing With The Stars have been REVEALED - Goss". goss.ie.
^ Jump up to: a b "RTE One on Twitter".
Jump up ^ One, R. T. E. "Delighted to announce that Dancing with the Stars has been re-commissioned & will return to RTÉ One in the new year! #DWTSIrl #Season2pic.twitter.com/allnd6UCVz".
^ Jump up to: a b c "RTÉ drops The Voice for Dancing with the Stars". RTÉ. Retrieved 3 August 2016.
Jump up ^ "The host of RTE's Dancing with the Stars has been CONFIRMED". 18 November 2016.
Jump up ^ "Byram, Byrne 'so excited' to host Irish Dancing with the Stars". RTÉ. 7 December 2016. Retrieved 7 December 2016.
Jump up ^ "Nicky Byrne and Amanda Byram confirm they're hosting Dancing With The Stars". Irish Independent. 6 December 2016. Retrieved 6 December 2016.
Jump up ^ "Dancing with the Stars cha chas to second series". RTÉ. 16 June 2017.
Jump up ^ "Deirdre O'Kane to waltz her way onto DWTS in January". RTÉ. 3 December 2017.
External links[edit]
Official website
[show]
v
t
e
Dancing with the Stars (Ireland)
Contestants
Series
1
2
Winners
Celebrities
Aidan O'Mahony
Professionals
Valeria Milova
Related
Strictly Come Dancing
[show]
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Dancing_with_the_Stars_(Irish_TV_series)&oldid=814709060"
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values: Featured content – the best of Wikipedia

values: Find background information on current events

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values: Dancing with the Stars (sraith theilifíse na hÉireann) – Irish

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