The role of laminins in basement membrane function

被引:225
作者
Aumailley, M [1 ]
Smyth, N [1 ]
机构
[1] Fac Med, Inst Biochem 2, D-50931 Cologne, Germany
关键词
extracellular matrix; congenital muscular dystrophy; epidermolysis bullosa;
D O I
10.1046/j.1469-7580.1998.19310001.x
中图分类号
R602 [外科病理学、解剖学]; R32 [人体形态学];
学科分类号
100101 ;
摘要
Laminins are a family of multifunctional macromolecules, ubiquitous in basement membranes, and represent the most abundant structural noncollagenous glycoproteins of these highly specialised extracellular matrices. Their discovery started with the difficult task of isolating molecules produced by cultivated cells or extracted from tissues. The development of molecular biology techniques has facilitated and accelerated the identification and the characterisation of new laminin variants making it feasible to identify full-length polypeptides which have not been purified. Further, genetically engineered laminin fragments can be generated for studies of their structure-function relationship, permitting the demonstration that laminins are involved in multiple interactions with themselves, with other components of the basal lamina, and with cells. It endows laminins with a central role in the formation, the architecture, and the stability of basement membranes. In addition, laminins may both separate and connect different tissues, i.e. the parenchymal and the interstitial connective tissues. Laminins also provide adjacent cells with a mechanical scaffold and biological information either directly by interacting with cell surface components, or indirectly by trapping growth factors. In doing so they trigger and control cellular functions. Recently, the structural and biological diversity of the laminins has started to be elucidated by gene targeting and by the identification of laminin defects in acquired or inherited human diseases. The consequent phenotypes highlight the pivotal role of laminins in determining heterogeneity in basement membrane functions.
引用
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页码:1 / 21
页数:21
相关论文
共 199 条
[51]   NONMUSCLE ALPHA-DYSTROGLYCAN IS INVOLVED IN EPITHELIAL DEVELOPMENT [J].
DURBEEJ, M ;
LARSSON, E ;
IBRAGHIMOVBESKROVNAYA, O ;
ROBERDS, SL ;
CAMPBELL, KP ;
EKBLOM, P .
JOURNAL OF CELL BIOLOGY, 1995, 130 (01) :79-91
[52]   Dystroglycan and laminins: Glycoconjugates involved in branching epithelial morphogenesis [J].
Durbeej, M ;
Ekblom, P .
EXPERIMENTAL LUNG RESEARCH, 1997, 23 (02) :109-118
[53]   EXPRESSION OF NIDOGEN AND LAMININ IN BASEMENT-MEMBRANES DURING MOUSE EMBRYOGENESIS AND IN TERATOCARCINOMA CELLS [J].
DZIADEK, M ;
TIMPL, R .
DEVELOPMENTAL BIOLOGY, 1985, 111 (02) :372-382
[54]  
EADY RAJ, 1986, CLIN EXPT DERMATOLOG, V12, P161
[55]   MEROSIN, A TISSUE-SPECIFIC BASEMENT-MEMBRANE PROTEIN, IS A LAMININ-LIKE PROTEIN [J].
EHRIG, K ;
LEIVO, I ;
ARGRAVES, WS ;
RUOSLAHTI, E ;
ENGVALL, E .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (09) :3264-3268
[56]   Receptors for laminins during epithelial morphogenesis [J].
Ekblom, P .
CURRENT OPINION IN CELL BIOLOGY, 1996, 8 (05) :700-706
[57]   LAMININ ISOFORMS AND THEIR RECEPTORS IN THE DEVELOPING KIDNEY [J].
EKBLOM, P ;
KLEIN, G ;
EKBLOM, M ;
SOROKIN, L .
AMERICAN JOURNAL OF KIDNEY DISEASES, 1991, 17 (06) :603-605
[58]  
EKBLOM P, 1996, LAMININS, P321
[59]   Common structural motifs in proteins of the extracellular matrix [J].
Engel, Juergen .
CURRENT OPINION IN CELL BIOLOGY, 1991, 3 (05) :779-785
[60]   DISTRIBUTION AND ISOLATION OF 4 LAMININ VARIANTS - TISSUE RESTRICTED DISTRIBUTION OF HETEROTRIMERS ASSEMBLED FROM 5 DIFFERENT SUBUNITS [J].
ENGVALL, E ;
EARWICKER, D ;
HAAPARANTA, T ;
RUOSLAHTI, E ;
SANES, JR .
CELL REGULATION, 1990, 1 (10) :731-740