ANOTHER LOOK AT COLLAGEN-V AND COLLAGEN-XI MOLECULES

被引:123
作者
FICHARD, A [1 ]
KLEMAN, JP [1 ]
RUGGIERO, F [1 ]
机构
[1] INST BIOL & CHIM PROT,F-69367 LYON 07,FRANCE
关键词
D O I
10.1016/S0945-053X(05)80001-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The fibrillar collagens are the most abundant proteins of extracellular matrices. Among them, collagens V and XI are quantitatively minor components which participate in the formation of the fibrillar collagen network. Since these collagens were discovered, studies have demonstrated that they may play a fundamental role in the control of fibrillogenesis, probably by forming a core within the fibrils. Ano ther characteristic of these collagens is the partial retention of their N-propeptide extensions in tissue forms, an unusual observation in comparison to the other known fibrillar collagens. The tissue locations of collagens V and XI are different, but their structural and biological properties seem to be closely related. It has been shown that their primary structures are highly conserved at both the gene and protein levels, and that these conserved features are the bases of their similar biological properties. In particular, they are both resistant to mammalian collagenases, and surprisingly sensitive to trypsin treatment. Collagens V and XI are usually buried within the major collagen fibrils, although they have both cell adhesion and heparin binding sites which could be of crucial importance in physiological processes such as development and wound healing. It has became evident that several molecules are in fact heterotypic associations of chains from both collagens V and XI, demonstrating that these two collagens are not distinct types but a single type which can be called collagen V/XI.
引用
收藏
页码:515 / 531
页数:17
相关论文
共 150 条
[1]  
ADACHI E, 1985, COLLAGEN REL RES, V5, P225
[2]   IMMUNOELECTRON MICROSCOPICAL EVIDENCE THAT TYPE-V COLLAGEN IS A FIBRILLAR COLLAGEN - IMPORTANCE FOR AN AGGREGATING CAPABILITY OF THE PREPARATION FOR RECONSTITUTING BANDING FIBRILS [J].
ADACHI, E ;
HAYASHI, T ;
HASHIMOTO, PH .
MATRIX, 1989, 9 (03) :232-237
[3]   INVITRO FORMATION OF HYBRID FIBRILS OF TYPE-V COLLAGEN AND TYPE-I COLLAGEN - LIMITED GROWTH OF TYPE-I COLLAGEN INTO THICK FIBRILS BY TYPE-V COLLAGEN [J].
ADACHI, E ;
HAYASHI, T .
CONNECTIVE TISSUE RESEARCH, 1986, 14 (04) :257-266
[4]   EXTRACELLULAR-MATRIX - THE THROMBOSPONDIN FAMILY [J].
ADAMS, J ;
LAWLER, J .
CURRENT BIOLOGY, 1993, 3 (03) :188-190
[5]  
ALITALO K, 1982, J BIOL CHEM, V257, P9016
[6]   LOCALIZATION OF PRO-ALPHA-2(V) COLLAGEN TRANSCRIPTS IN THE TISSUES OF THE DEVELOPING MOUSE EMBRYO [J].
ANDRIKOPOULOS, K ;
SUZUKI, HR ;
SOLURSH, M ;
RAMIREZ, F .
DEVELOPMENTAL DYNAMICS, 1992, 195 (02) :113-120
[7]  
ANDRIKOPOULOS K, 1993, AUG MOUS MOL GEN M E
[8]  
BACHINGER HP, 1982, J BIOL CHEM, V257, P4590
[9]   PLATELET ACTIVATION BY BASEMENT-MEMBRANE COLLAGENS [J].
BALLEISEN, L ;
RAUTERBERG, J .
THROMBOSIS RESEARCH, 1980, 18 (05) :725-732
[10]   PLATELET-AGGREGATION BY BASEMENT-MEMBRANE - ASSOCIATED COLLAGENS [J].
BARNES, MJ ;
BAILEY, AJ ;
GORDON, JL ;
MACINTYRE, DE .
THROMBOSIS RESEARCH, 1980, 18 (3-4) :375-388