Syndecans as receptors and organizers of the extracellular matrix

被引:207
作者
Xian, Xiaojie [1 ]
Gopal, Sandeep [1 ]
Couchman, John R. [1 ]
机构
[1] Univ Copenhagen, Dept Biomed Sci, Bioctr, Ole Maaloes Vej 5, DK-2200 Copenhagen, Denmark
基金
英国医学研究理事会;
关键词
Proteoglycan; Heparan sulphate; Signalling; Extracellular matrix assembly; LAMININ ALPHA-1 CHAIN; HEPARAN-SULFATE PROTEOGLYCANS; FOCAL ADHESION FORMATION; CELL-ADHESION; TENASCIN-C; BINDING-SITES; G-DOMAIN; CYTOPLASMIC DOMAIN; DIRECTIONAL MIGRATION; DERMAL FIBROBLASTS;
D O I
10.1007/s00441-009-0829-3
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Syndecans are type I transmembrane proteins having a core protein modified with glycosaminoglycan chains, most commonly heparan sulphate. They are an ancient group of molecules, present in invertebrates and vertebrates. Among the plethora of molecules that can interact with heparan sulphate, the collagens and glycoproteins of the extracellular matrix are prominent. Frequently, they do so in conjunction with other receptors, most notably the integrins. For this reason, they are often referred to as "co-receptors". However, just as with integrins, syndecans can interact with actin-associated proteins and signalling molecules, such as protein kinases. Some aspects of syndecan signalling are understood but much remains to be learned. The functions of syndecans in regulating cell adhesion and extracellular matrix assembly are described here. Evidence from null mice suggests that syndecans have roles in postnatal tissue repair, inflammation and tumour progression. Developmental deficits in lower vertebrates in which syndecans are eliminated are also informative and suggest that, in mammals, redundancy is a key issue.
引用
收藏
页码:31 / 46
页数:16
相关论文
共 124 条
[1]   A role for syndecan-1 in coupling fascin spike formation by thrombospondin-1 [J].
Adams, JC ;
Kureishy, N ;
Tayor, AL .
JOURNAL OF CELL BIOLOGY, 2001, 152 (06) :1169-1182
[2]   Syndecans in wound healing, inflammation and vascular biology [J].
Alexopoulou, Annika N. ;
Multhaupt, Hinke A. B. ;
Couchman, John R. .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2007, 39 (03) :505-528
[3]   Analysis of heparin, α-dystroglycan and sulfatide binding to the G domain of the laminin α1 chain by site-directed mutagenesis [J].
Andac, Z ;
Sasaki, T ;
Mann, K ;
Brancaccio, A ;
Deutzmann, R ;
Timpl, R .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 287 (02) :253-264
[4]   Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration [J].
Bachy, Sophie ;
Letourneur, Francois ;
Rousselle, Patricia .
JOURNAL OF CELLULAR PHYSIOLOGY, 2008, 214 (01) :238-249
[5]  
BARKALOW FJB, 1991, J BIOL CHEM, V266, P7812
[6]   p190RhoGAP is the convergence point of adhesion signals from α5β1 integrin and syndecan-4 [J].
Bass, Mark D. ;
Morgan, Mark R. ;
Roach, Kirsty A. ;
Settleman, Jeffrey ;
Goryachev, Andrew B. ;
Humphries, Martin J. .
JOURNAL OF CELL BIOLOGY, 2008, 181 (06) :1013-1026
[7]   Sndecan-4-dependent Rac1 regulation determines directional migration in response to the extracellular matrix [J].
Bass, Mark D. ;
Roach, Kirsty A. ;
Morgan, Mark R. ;
Mostafavi-Pour, Zohreh ;
Schoen, Tobias ;
Muramatsu, Takashi ;
Mayer, Ulrike ;
Ballestrem, Christoph ;
Spatz, Joachim P. ;
Humphries, Martin J. .
JOURNAL OF CELL BIOLOGY, 2007, 177 (03) :527-538
[8]   Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation [J].
Bax, Daniel V. ;
Mahalingam, Yashithra ;
Cain, Stuart ;
Mellody, Kieran ;
Freeman, Lyle ;
Younger, Kerri ;
Shuttleworth, C. Adrian ;
Humphries, Martin J. ;
Couchman, John R. ;
Kielty, Cay M. .
JOURNAL OF CELL SCIENCE, 2007, 120 (08) :1383-1392
[9]   Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by α5β1 and αvβ3 integrins [J].
Bax, DV ;
Bernard, SE ;
Lomas, A ;
Morgan, A ;
Humphries, J ;
Shuttleworth, CA ;
Humphries, MJ ;
Kielty, CM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (36) :34605-34616
[10]   Syndecan-1 regulates αvβ3 and αvβ5 integrin activation during angiogenesis and is blocked by synstatin, a novel peptide inhibitor [J].
Beauvais, DeannaLee M. ;
Ell, Brian J. ;
McWhorter, Andrea R. ;
Rapraeger, Alan C. .
JOURNAL OF EXPERIMENTAL MEDICINE, 2009, 206 (03) :691-705