Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies with the rat monoclonal antibody KMI6 had localized its antigen in vivo to a discrete subpopulation of marrow stromal cells. The KMI6 antigen has now been identified as the murine homolog of integrin beta 1 by amino acid sequence analysis and by cross-reactivity with antiserum to the avian integrin beta 1. The relative tissue abundance of murine integrin beta 1 was determined by Western blot. Although immunoperoxidase staining of fixed murine hematopoietic tissues demonstrated an abundance of intracellular beta 1, few primary-derived cells of lymphohematopoietic origin were surface positive as assessed by immunofluorescence and flow cytometry. Fetal erythroblasts provided the only exception. In contrast, the antigen was readily detected on the surface of several cultured cell lines in association with a variety of alpha chains. The biochemical properties of the surface labeled murine integrin beta 1 were similar to those of its human counterpart, exhibiting an altered electrophoretic migration under reduced conditions or following N-glycanase treatment. The antibody recognition of the protein was insensitive to glycosylation state, presence of divalent cations, detergents, or transfer to a nitrocellulose membrane. However, on Western blot, the epitope was lost on reduction of the protein, suggesting that it is conformation dependent. These data indicate that although KMI6 epitope is widely distributed, its surface expression in vivo may be restricted within lymphohemopoietic tissues.
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PMID:Recognition of murine integrin beta 1 by a rat anti-stromal cell monoclonal antibody. 753 55

The expression of non-beta 2 integrins on polymorphonuclear neutrophils (PMNs) was analyzed by immunoprecipitation and flow cytometry using platelet-free PMN preparations and anti-Fc gamma R blocking mAbs. No beta 3 integrin was detected with six anti-beta 3 mAbs. Conversely, integrin beta 1 chain was present on PMNs, although at low level, and could be distinguished from platelet beta 1 by SDS-PAGE. The MW differences disappeared after N-glycanase treatment. PMNs express only 2500 molecules of beta 1 per cell and this expression is not modulated by agonists such as phorbol myristate acetate, formylmethionyl-leucyl-phenylalanine, granulocyte-macrophage colony-stimulating factor, or tumor necrosis factor alpha, which enhance CD11b expression, or by interferon-gamma or transforming growth factor beta. PMNs were found to express alpha 6 associated with beta 1, and no reactivity was observed with various anti-alpha 1, anti-alpha 2, anti-alpha 3, anti-alpha 4, anti-alpha 5 or anti-alpha V mAbs. In conclusion, although other leukocytes express various beta 1 integrins, which mediate cell interactions with ECM proteins, PMNs appear to express only the laminin receptor alpha 6 beta 1. PMN interactions with non-laminin ECM ligands thus seem to be mediated either exclusively by beta 2 integrins or by nonintegrin molecules.
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PMID:Evidence for integrins other than beta 2 on polymorphonuclear neutrophils: expression of alpha 6 beta 1 heterodimer. 809 16