Abstract

Using a monoclonal antibody that rounds and detaches chick myoblast and certain chick fibroblasts from their substratum, we have identified a cell surface glycoprotein involved in cell-substratum adhesion. These glycoproteins are integral cell surface constituents, which are extracted from the cell with non-ionic detergents. The glycoproteins are purified by monoclonal antibody affinity chromatography. Sedimentation studies suggest that these glycoproteins exist as a bi- or tri-molecular complex. Fluorescent microscopy indicates that these glycoproteins are found along actin-containing stress fibers and co-localize with fibronectin around, but not within, adhesive plaques. Our working hypothesis is that these glycoproteins exist in the surface membrane as a complex serving as transmembrane linkers between molecules of the extracellular matrix and the cytoskeleton. They appear to be enriched in close contact adhesion sights. (A)

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA019144-13
Application #
3165110
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1979-06-01
Project End
1989-02-28
Budget Start
1987-03-01
Budget End
1988-02-29
Support Year
13
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Wistar Institute
Department
Type
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Yi, Yijun; Shepard, Anne; Kittrell, Frances et al. (2004) p19ARF determines the balance between normal cell proliferation rate and apoptosis during mammary gland development. Mol Biol Cell 15:2302-11
Schachtner, S; Buck, C; Bergelson, J et al. (1999) Temporally regulated expression patterns following in utero adenovirus-mediated gene transfer. Gene Ther 6:1249-57
Baldwin, H S; Mickanin, C; Buck, C (1997) Adenovirus-mediated gene transfer during initial organogenesis in the mammalian embryo is promoter-dependent and tissue-specific. Gene Ther 4:1142-9
Shih, D T; Boettiger, D; Buck, C A (1997) Epitopes of adhesion-perturbing monoclonal antibodies map within a predicted alpha-helical domain of the integrin beta 1 subunit. J Cell Sci 110 ( Pt 20):2619-28
Buck, C A; Edelman, J M; Buck, C E et al. (1996) Expression patterns of adhesion receptors in the developing mouse lung: functional implications. Cell Adhes Commun 4:69-87
Yan, H C; Pilewski, J M; Zhang, Q et al. (1995) Localization of multiple functional domains on human PECAM-1 (CD31) by monoclonal antibody epitope mapping. Cell Adhes Commun 3:45-66
Bazzoni, G; Shih, D T; Buck, C A et al. (1995) Monoclonal antibody 9EG7 defines a novel beta 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J Biol Chem 270:25570-7
Edelman, J M; Chan, B M; Uniyal, S et al. (1994) The mouse VLA-2 homologue supports collagen and laminin adhesion but not virus binding. Cell Adhes Commun 2:131-43
Mette, S A; Pilewski, J; Buck, C A et al. (1993) Distribution of integrin cell adhesion receptors on normal bronchial epithelial cells and lung cancer cells in vitro and in vivo. Am J Respir Cell Mol Biol 8:562-72
Damjanovich, L; Albelda, S M; Mette, S A et al. (1992) Distribution of integrin cell adhesion receptors in normal and malignant lung tissue. Am J Respir Cell Mol Biol 6:197-206

Showing the most recent 10 out of 27 publications