A study of the structure, function and distribution of β5 integrins using novel anti-β5 monoclonal antibodies

R. Pasqualini, J. Bodorova, S. Ye, M. E. Hemler

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Here, we have utilized six new anti-human β5 monoclonal antibodies to perform a detailed investigation of the structure, function and distribution of β5 integrins. Monoclonal anti-β5 specificity was confirmed by reactivity with β5-transfected CHO cells, by direct binding to the β5 subunit (immunoblotting), and by immunodepletion experiments using polyclonal anti-β5 serum. The β5 subunit was predominantly associated with the α(v) subunit, although on some cell lines, the level of β5 exceeded that of α(v) for unknown reasons. Cell adhesion studies showed that the adhesive function of β5 could be stimulated, inhibited or unaltered by different anti-β5 monoclonal antibodies. The β5 subunit was involved in adhesion to both vitronectin and fibronectin and, at least for K562 cells, fibronectin appeared to be the preferred ligand. Flow-cytometry studies showed that the β5 subunit was expressed at moderate to high levels on all adherent cell lines examined, was absent from all lymphoid cell lines, and was only weakly expressed on myeloid cell lines. Staining of thymic sections showed the distribution of β5 on blood vessels, Hassal's corpuscles, cortical and medullary stromal cells, and basement membranes. Skin sections showed β5 on the basal layer of the epidermis and on some dermal blood vessel walls, and kidney sections showed staining of glomerular regions, juxta glomerular apparatus, proximal convoluted tubules and collecting tubules, and at least one anti-β5 antibody also stained epithelial cells of proximal tubules.

Original languageEnglish (US)
Pages (from-to)101-111
Number of pages11
JournalJournal of cell science
Issue number1
StatePublished - 1993

All Science Journal Classification (ASJC) codes

  • Cell Biology


  • Anti-β monoclonal antibodies
  • Cell adhesion
  • β integrin

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