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  • Title: Distinct structural and functional epitopes of the alpha E beta 7 integrin.
    Author: Russell GJ, Parker CM, Cepek KL, Mandelbrot DA, Sood A, Mizoguchi E, Ebert EC, Brenner MB, Bhan AK.
    Journal: Eur J Immunol; 1994 Nov; 24(11):2832-41. PubMed ID: 7525307.
    Abstract:
    Intestinal intraepithelial lymphocytes (iIEL) are predominantly CD3+, CD8+ T lymphocytes located above or adjacent to the mucosal basement membrane. Although they are positioned to interact with intercellular luminal antigen or with enterocytes, the function of iIEL remains unknown. Most (> 85%) of the iIEL express the alpha E beta 7 integrin which appears to be involved in the adhesion of lymphocytes to epithelial cells. We report the characterization of three monoclonal antibodies (mAb) termed alpha E7-1, alpha E7-2, and alpha E7-3, that react with the alpha E beta 7 integrin recognized by the previously described mAb HML-1 as demonstrated by identical sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility and charge. Flow cytometric analysis of antibody cross-blocking indicated that these mAb recognize distinct epitopes of alpha E beta 7. While all of the mAb were capable of blocking the adhesion of cultured iIEL to a breast epithelial cell line, only HML-1 and alpha E7-1 (which recognize an identical or closely related epitope) were co-stimulatory with suboptimal concentrations of anti-CD3 mAb in inducing proliferation of cultured iIEL. Thus, these mAb appear to recognize functionally distinct epitopes of alpha E beta 7 and will be useful to study relationships between the structure and function of this integrin.
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