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Actin‐associated cell‐surface glycoprotein from ascites cell microvilli: A disulfide‐linked multimer

1985; Wiley; Volume: 28; Issue: 4 Linguagem: Inglês

10.1002/jcb.240280402

1097-4644

Goeh Jung, David Andrews, Kermit L. Carraway, Coralie A. Carothers Carraway,

Barrier Structure and Function Studies

Abstract Isolated microvilli of the MAT‐Cl subline of the 13762 rat mammary adenocarcinoma contain a transmembrane complex composed of a cell surface, cytoskeleton‐associated glycoprotein (CAG), actin, and a 58,000‐dalton polypeptide (58K). The behavior of CAG has been studied by differential centrifugation and velocity sedimentation gradient centrifugation of detergent extracts of microvilli. CAG can be pelleted along with a fraction of the microvillar actin even in the presence of ionic detergents and under microfilament‐depolymerizing conditions. By velocity sedimentation analysis CAG in Triton/PBS extracts sediments as a large, hetero‐geneous species (sedimentation coefficient > 25S). In Sarkosyl and sodium dodecyl sulfate (SDS) the size and heterogeneity are somewhat reduced. In SDS CAG sediments as a 20S species in the absence of mercaptoethanol and as a 5S species in the presence of mercaptoethanol. These results indicate that CAG is a disulfide‐linked multimer in the microvillus membrane. We suggest that the stable multimeric structure of CAG permits it to act as the membrane association site for several microfilaments and plays an important role in the formation and stabilization of the microvillus structure.