Dissociation of Madin-Darby canine kidney epithelial cells by the monoclonal antibody anti-arc-1: mechanistic aspects and identification of the antigen as a component related to uvomorulin.

作者: J Behrens , W Birchmeier , S L Goodman , B A Imhof

DOI: 10.1083/JCB.101.4.1307

关键词: Cell cultureCytochalasinAntibodyTight junctionBiologyAntigenCell adhesionMolecular biologyCell adhesion moleculeCell junction

摘要: It has previously been shown that the monoclonal antibody anti-Arc-1 dissociates Madin-Darby canine kidney (MDCK) epithelial cells and changes their morphology in vitro (Imhof, B.A., H.P. Vollmers, S.L. Goodman, W. Birchmeier, 1983, Cell, 35:667-675). In this article we demonstrate recognizes an uvomorulin-like molecule on MDCK cells, i.e., it immunoprecipitates 84-kD protein fragment from a tryptic digest of cell surfaces presence Ca2+ (as does anti-uvomorulin antiserum). Furthermore, antiserum prevents binding to cells. The distribution Arc-1 antigen is also quite similar uvomorulin: enriched at cell-cell contacts both various tissues. intestinal epithelium could be further localized region junctional complex. To study mechanism action dissociating antibody, grown Nuclepore filters Boyden chambers were exposed either upper or lower compartment. interfered with adhesion only basolateral but not apical surface. Antibody was inhibited colchicine cytochalasin B. dissociation prevented when cellular cAMP level raised. These findings indicate acts target below tight junctions (possibly located complex), they confirm cytoskeleton metabolic factors are actively involved maintenance integrity.

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