The Collagen Family

被引:1488
作者
Ricard-Blum, Sylvie [1 ]
机构
[1] Univ Lyon 1, CNRS, Inst Biol & Chim Prot, UMR 5086, F-69367 Lyon, France
关键词
DYSTROPHIC EPIDERMOLYSIS-BULLOSA; DOMAIN RECEPTOR 2; CRYSTAL-STRUCTURE; EXTRACELLULAR-MATRIX; I COLLAGEN; BASEMENT-MEMBRANES; TRIPLE-HELIX; CROSS-LINK; FIBRILLAR COLLAGENS; ENDOTHELIAL-CELLS;
D O I
10.1101/cshperspect.a004978
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. Four collagens are type II membrane proteins that also exist in a soluble form released from the cell surface by shedding. Collagens play structural roles and contribute to mechanical properties, organization, and shape of tissues. They interact with cells via several receptor families and regulate their proliferation, migration, and differentiation. Some collagens have a restricted tissue distribution and hence specific biological functions.
引用
收藏
页码:1 / 19
页数:19
相关论文
共 132 条
[1]   Proteoglycan-collagen XV in human tissues is seen linking banded collagen fibers subjacent to the basement membrane [J].
Amenta, PS ;
Scivoletti, NA ;
Newman, MD ;
Sciancalepore, JP ;
Li, DQ ;
Myers, JC .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 2005, 53 (02) :165-176
[2]   Type XIV Collagen Regulates Fibrillogenesis PREMATURE COLLAGEN FIBRIL GROWTH AND TISSUE DYSFUNCTION IN NULL MICE [J].
Ansorge, Heather L. ;
Meng, Xianmin ;
Zhang, Guiyun ;
Veit, Guido ;
Sun, Mei ;
Klement, John F. ;
Beason, David P. ;
Soslowsky, Louis J. ;
Koch, Manuel ;
Birk, David E. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (13) :8427-8438
[3]   The effects of the Maillard reaction on the physical properties and cell interactions of collagen [J].
Avery, N. C. ;
Bailey, A. J. .
PATHOLOGIE BIOLOGIE, 2006, 54 (07) :387-395
[4]   Zebrafish collagen XII is present in embryonic connective tissue sheaths (fascia) and basement membranes [J].
Bader, Hannah L. ;
Keene, Douglas R. ;
Charvet, Benjamin ;
Veit, Guido ;
Driever, Wolfgang ;
Koch, Manuel ;
Ruggiero, Florence .
MATRIX BIOLOGY, 2009, 28 (01) :32-43
[5]  
Banos Charles C., 2008, Birth Defects Research, V84, P228, DOI 10.1002/bdrc.20130
[6]   Collagen XXIII expression is associated with prostate cancer recurrence and distant metastases [J].
Banyard, Jacqueline ;
Bao, Lere ;
Hofer, Matthias D. ;
Zurakowski, David ;
Spivey, Kristin A. ;
Feldman, Adam S. ;
Hutchinson, Lloyd M. ;
Kuefer, Rainer ;
Rubin, Mark A. ;
Zetter, Bruce R. .
CLINICAL CANCER RESEARCH, 2007, 13 (09) :2634-2642
[7]   Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations [J].
Bateman, John F. ;
Boot-Handford, Raymond P. ;
Lamande, Shireen R. .
NATURE REVIEWS GENETICS, 2009, 10 (03) :173-183
[8]   Conformational effects of Gly-X-Gly interruptions in the collagen triple helix [J].
Bella, Jordi ;
Liu, Jingsong ;
Kramer, Rachel ;
Brodsky, Barbara ;
Berman, Helen M. .
JOURNAL OF MOLECULAR BIOLOGY, 2006, 362 (02) :298-311
[9]   COLdb, a Database Linking Genetic Data to Molecular Function in Fibrillar Collagens [J].
Bodian, Dale L. ;
Klein, Teri E. .
HUMAN MUTATION, 2009, 30 (06) :946-951
[10]   Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer [J].
Bogin, O ;
Kvansakul, M ;
Rom, E ;
Singer, J ;
Yayon, A ;
Hohenester, E .
STRUCTURE, 2002, 10 (02) :165-173