Laminins of the dermo-epidermal junction

被引:107
作者
Aumailley, M
Rousselle, P
机构
[1] Fac Med, Inst Biochem 2, D-50931 Cologne, Germany
[2] CNRS, Inst Biol & Chim Prot, F-69367 Lyon, France
关键词
laminins; non-collagenous glycoproteins; basement membranes;
D O I
10.1016/S0945-053X(98)00004-3
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
Laminins are the most abundant structural non-collagenous glycoproteins ubiquitously present in basement membranes. They are multidomain molecules constituting a family of possibly more than 50 members. Some members such as laminins 5, 6 and 10 are specific of the basal lamina present under stratified epithelia. Although only few intact laminin isoforms have been purified from cultivated cells or tissues, genetic engineering has opened the way for a rapid development of laminin structural biology. Moreover, the phenotypes resulting from gene targeting in mouse or from laminin defects in acquired or inherited human diseases highlight the pivotal role of laminins in morphogenesis, development, and physiology. Indeed, the laminins display a remarkable repertoire of functions, most importantly as structural elements forming a network throughout the basement membrane to which other collagenous or non-collagenous glycoproteins and proteoglycans attach. Furthermore, they are signaling molecules providing adjacent cells with diverse information by interacting with cell surface components. (C) 1999 Elsevier Science B.V./International Society of Matrix Biology. All rights reserved.
引用
收藏
页码:19 / 28
页数:10
相关论文
共 97 条
  • [1] DEVELOPMENTAL EXPRESSION OF NICEIN ADHESION PROTEIN (LAMININ-5) SUBUNITS SUGGESTS MULTIPLE MORPHOGENIC ROLES
    ABERDAM, D
    AGUZZI, A
    BAUDOIN, C
    GALLIANO, MF
    ORTONNE, JP
    MENEGUZZI, G
    [J]. CELL ADHESION AND COMMUNICATION, 1994, 2 (02) : 115 - 129
  • [2] Laminin-alpha 2 but not -alpha 1-mediated adhesion of human (Duchenne) and murine (mdx) dystrophic myotubes is seriously defective
    Angoli, D
    Corona, P
    Baresi, R
    Mora, M
    Wanke, E
    [J]. FEBS LETTERS, 1997, 408 (03) : 341 - 344
  • [3] NIDOGEN MEDIATES THE FORMATION OF TERNARY COMPLEXES OF BASEMENT-MEMBRANE COMPONENTS
    AUMAILLEY, M
    BATTAGLIA, C
    MAYER, U
    REINHARDT, D
    NISCHT, R
    TIMPL, R
    FOX, JW
    [J]. KIDNEY INTERNATIONAL, 1993, 43 (01) : 7 - 12
  • [4] Laminins: A family of diverse multifunctional molecules of basement membranes
    Aumailley, M
    Krieg, T
    [J]. JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1996, 106 (02) : 209 - 214
  • [5] Structure and biological activity of the extracellular matrix
    Aumailley, M
    Gayraud, B
    [J]. JOURNAL OF MOLECULAR MEDICINE-JMM, 1998, 76 (3-4): : 253 - 265
  • [6] AUMAILLEY M, 1996, LAMININS, P127
  • [7] BALDING SD, 1997, BIOCHEMISTRY-US, V36, P5821
  • [8] Structure of the nidogen binding LE module of the laminin gamma 1 chain in solution
    Baumgartner, R
    Czisch, M
    Mayer, U
    Poschl, E
    Huber, R
    Timpl, R
    Holak, TA
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 257 (03) : 658 - 668
  • [9] IONIC INTERACTIONS IN THE COILED-COIL DOMAIN OF LAMININ DETERMINE THE SPECIFICITY OF CHAIN ASSEMBLY
    BECK, K
    DIXON, TW
    ENGEL, J
    PARRY, DAD
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1993, 231 (02) : 311 - 323
  • [10] Bullous pemphigoid and cicatricial pemphigoid autoantibodies react with ultrastructurally separable epitopes on the BP180 ectodomain: Evidence that BP180 spans the lamina lucida
    Bedane, C
    McMillan, JR
    Balding, SD
    Bernard, P
    Prost, C
    Bonnetblanc, JM
    Diaz, LA
    Eady, RAJ
    Giudice, GJ
    [J]. JOURNAL OF INVESTIGATIVE DERMATOLOGY, 1997, 108 (06) : 901 - 907