Laminin γ3 chain binds to nidogen and is located in murine basement membranes

被引:51
作者
Gersdorff, N
Kohfeldt, E
Sasaki, T
Timpl, R
Miosge, N [1 ]
机构
[1] Univ Gottingen, Dept Histol, D-37075 Gottingen, Germany
[2] Univ Gottingen, Dept Prosthodont, D-37075 Gottingen, Germany
[3] Max Planck Inst Biochem, Dept Prot Chem, D-82152 Martinsried, Germany
关键词
D O I
10.1074/jbc.M501875200
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
Recently a novel laminin gamma 3 chain was identified in mouse and human and shown to have the same modular structure as the laminin gamma 1 chain. We expressed two fragments of the gamma 3 chain in mammalian cells recombinantly. The first, domain VI/V, consisting of laminin N-terminal (domain VI) and four laminin-type epidermal growth factor-like (domain V) and laminin N-terminal modules, was shown to be essential for self-assembly of laminins. The other was domain III3-5, which consists of three laminin-type epidermal growth factor-like modules and is predicted to bind to nidogens. The gamma 3 VI/V fragment was a poor inhibitor for laminin-1 polymerization as was the gamma 2 VI/ V fragment. The gamma 3 III3-5 fragment bound to nidogen-1 and nidogen-2 with lower affinity than the gamma 1 III3-5 fragment. These data suggested that laminins containing the gamma 3 chain may assemble networks independent of other laminins. Polyclonal antibodies raised against gamma 3 VI/V and gamma 3 III3-5 showed no cross-reaction with homologous fragments from the gamma 1 and gamma 2 chains of laminin and allowed the establishment of gamma chain-specific radioimmunoassays and light and electron microscopic immunostaining of tissues. This demonstrated a 20-100-fold lower content of the gamma 3 chain compared with the gamma 1 chain in various tissue extracts of adult mice. The expression of gamma 3 chain was highly tissue-specific. In contrast to earlier assumptions, the antibodies against the gamma 3 chain showed light microscopic staining exclusively in basement membrane zones of adult and embryonic tissues, such as the brain, kidney, skin, muscle, and testis. Ultrastructural immunogold staining localized the gamma 3 chain to basement membranes of these tissues.
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页码:22146 / 22153
页数:8
相关论文
共 40 条
[1]   BINDING OF NIDOGEN AND THE LAMININ-NIDOGEN COMPLEX TO BASEMENT-MEMBRANE COLLAGEN TYPE-IV [J].
AUMAILLEY, M ;
WIEDEMANN, H ;
MANN, K ;
TIMPL, R .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 184 (01) :241-248
[2]   DISSECTION OF LAMININ BY CATHEPSIN-G INTO ITS LONG-ARM AND SHORT-ARM STRUCTURES AND LOCALIZATION OF REGIONS INVOLVED IN CALCIUM DEPENDENT STABILIZATION AND SELF-ASSOCIATION [J].
BRUCH, M ;
LANDWEHR, R ;
ENGEL, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 185 (02) :271-279
[3]   Self-assembly of laminin isoforms [J].
Cheng, YS ;
Champliaud, MF ;
Burgeson, RE ;
Marinkovich, MP ;
Yurchenco, PD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (50) :31525-31532
[4]  
Colognato H, 2000, DEV DYNAM, V218, P213, DOI 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO
[5]  
2-R
[6]   The N-terminal globular domain of the laminin α1 chain binds to α1β1 and α2β1 integrins and to the heparan sulfate-containing domains of perlecan [J].
Ettner, N ;
Göhring, W ;
Sasaki, T ;
Mann, K ;
Timpl, R .
FEBS LETTERS, 1998, 430 (03) :217-221
[7]   RECOMBINANT NIDOGEN CONSISTS OF 3 GLOBULAR DOMAINS AND MEDIATES BINDING OF LAMININ TO COLLAGEN TYPE-IV [J].
FOX, JW ;
MAYER, U ;
NISCHT, R ;
AUMAILLEY, M ;
REINHARDT, D ;
WIEDEMANN, H ;
MANN, K ;
TIMPL, R ;
KRIEG, T ;
ENGEL, J ;
CHU, ML .
EMBO JOURNAL, 1991, 10 (11) :3137-3146
[8]   Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin α3B and α5 chains [J].
Garbe, JHO ;
Göhring, W ;
Mann, K ;
Timpl, R ;
Sasaki, T .
BIOCHEMICAL JOURNAL, 2002, 362 :213-221
[9]   Molecular cloning and tissue-specific expression of a novel murine laminin γ3 chain [J].
Iivanainen, A ;
Morita, T ;
Tryggvason, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (20) :14107-14111
[10]   Characterization and expression of the laminin γ3 chain:: A novel, non-basement membrane-associated, laminin chain [J].
Koch, M ;
Olson, PF ;
Albus, A ;
Jin, W ;
Hunter, DD ;
Brunken, WJ ;
Burgeson, RE ;
Champliaud, MF .
JOURNAL OF CELL BIOLOGY, 1999, 145 (03) :605-617