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Alpha 2 beta 1 integrins from different cell types show different binding specificities.

Authors
  • Kirchhofer, D
  • Languino, L R
  • Ruoslahti, E
  • Pierschbacher, M D
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Jan 15, 1990
Volume
265
Issue
2
Pages
615–618
Identifiers
PMID: 2153105
Source
Medline
License
Unknown

Abstract

Purified alpha 2 beta 1 integrin from human platelets was compared in its function and immunoreactivity to alpha 2 beta 1 from endothelial cells. Both alpha 2 beta 1 integrins bound to type I collagen-Sepharose and had indistinguishable immunoreactivities when analyzed by a panel of monoclonal and polyclonal alpha 2-specific antibodies. However, functional analysis using rechromatography of purified receptors on laminin and collagen-Sepharose showed that endothelial alpha 2 beta 1 was able to bind to laminin, whereas its counterpart from platelets did not. Moreover, a receptor binding assay indicated that, in contrast to platelets, endothelial cells might also use alpha 2 beta 1 to bind to fibronectin. These results suggest that the alpha 2 beta 1 binding specificity may be modulated by cell-type specific factors.

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