CHICK LAMININ - ISOLATION BY MONOCLONAL-ANTIBODIES AND DIFFERENTIAL DISTRIBUTION OF VARIANTS IN THE EMBRYO

被引:13
作者
BRUBACHER, D [1 ]
WEHRLEHALLER, B [1 ]
CHIQUET, M [1 ]
机构
[1] UNIV BASEL,BIOCTR,DEPT BIOPHYS CHEM,KLINGELBERGSTR 70,CH-4056 BASEL,SWITZERLAND
关键词
D O I
10.1016/0014-4827(91)90435-W
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
In order to study the expression and function of laminin variants during chick embryonic development, we have generated monoclonal antibodies against chick heart laminin. One monoclonal antibody (mAb), called 9/F-10, could be used to purify chick laminin to homogeneity. By rotary shadowing, cross-shaped and T-shaped laminin particles as well as aggregates of two laminin molecules crosslinked via their short arms could be observed in this preparation. Purified chick laminin was very potent in mediating neurite growth by chick embryonic neurons. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of reduced chick heart laminin revealed a complex pattern of polypeptides which are immunologically related to several mammalian laminin chains. The two mAbs, 9/F-10 and 3/E-8, recognize two different types of chick laminin subunits. By immunofluorescence, antibody 3/E-8 labels basement membranes, aortic smooth muscle, and mesenchyme of 6-day-old chick embryos. In contrast, staining by mAb 9/F-10 is confined to basement membranes. Therefore, the two antibodies seem to distinguish between two different chick laminin isoforms. © 1991.
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页码:290 / 299
页数:10
相关论文
共 41 条
  • [21] KLEIN G, 1990, DEVELOPMENT, V110, P823
  • [22] KUCHEREREHRET S, 1990, DEVELOPMENT, V110, P1285
  • [23] CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4
    LAEMMLI, UK
    [J]. NATURE, 1970, 227 (5259) : 680 - +
  • [24] PATHWAY SELECTION BY EMBRYONIC CHICK MOTO-NEURONS IN AN EXPERIMENTALLY ALTERED ENVIRONMENT
    LANCEJONES, C
    LANDMESSER, L
    [J]. PROCEEDINGS OF THE ROYAL SOCIETY SERIES B-BIOLOGICAL SCIENCES, 1981, 214 (1194): : 19 - 52
  • [25] ENDOTHELIAL-CELLS USE ALPHA-2-BETA-1 INTEGRIN AS A LAMININ RECEPTOR
    LANGUINO, LR
    GEHLSEN, KR
    WAYNER, E
    CARTER, WG
    ENGVALL, E
    RUOSLAHTI, E
    [J]. JOURNAL OF CELL BIOLOGY, 1989, 109 (05) : 2455 - 2462
  • [26] LAMININ AND OTHER BASEMENT-MEMBRANE COMPONENTS
    MARTIN, GR
    TIMPL, R
    [J]. ANNUAL REVIEW OF CELL BIOLOGY, 1987, 3 : 57 - 85
  • [27] THE HIGH-AFFINITY BINDING OF LAMININ TO CELLS - ASSIGNATION OF A MAJOR CELL-BINDING SITE TO THE LONG ARM OF LAMININ AND OF A LATENT CELL-BINDING SITE TO ITS SHORT ARMS
    NURCOMBE, V
    AUMAILLEY, M
    TIMPL, R
    EDGAR, D
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 180 (01): : 9 - 14
  • [28] LAMININ ALTERS CELL-SHAPE AND STIMULATES MOTILITY AND PROLIFERATION OF MURINE SKELETAL MYOBLASTS
    OCALAN, M
    GOODMAN, SL
    KUHL, U
    HAUSCHKA, SD
    VONDERMARK, K
    [J]. DEVELOPMENTAL BIOLOGY, 1988, 125 (01) : 158 - 167
  • [29] PAULSSON M, 1989, J BIOL CHEM, V264, P18726
  • [30] BINDING OF CA-2+ INFLUENCES SUSCEPTIBILITY OF LAMININ TO PROTEOLYTIC DIGESTION AND INTERACTIONS BETWEEN DOMAIN-SPECIFIC LAMININ FRAGMENTS
    PAULSSON, M
    SALADIN, K
    LANDWEHR, R
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 177 (03): : 477 - 481