Monoclonal antibodies against a glycoprotein localized in coated pits and endocytic vesicles inhibit α2-macroglobulin binding and uptake

J. A. Hanover, P. D'Souza, T. August, I. Pastan, M. C. Willingham

Research output: Contribution to journalArticle

Abstract

Eight monoclonal antibodies, all IgG(2a), which recognize a 180/90-kDa glycoprotein similar in properties to the receptor for α2-macroglobulin of mouse embryo 3T3 cell plasma membranes, have been tested for their effect on the binding and uptake of α2-macroglobulin by live cells. One antibody directly inhibited binding of 125I-α2-macroglobulin under conditions in which 125I-transferrin binding to the transferrin receptor was unaffected. Another monoclonal antibody decreased α2-macroglobulin binding when preincubated with cells at 37°C. This antibody was also capable of specifically binding to ligand-receptor complexes formed by preincubating 125I-α2-macroglobulin with detergent extracts of Swiss 3T3 cells. Immunoelectron microscopy showed that the 180/90-kDa glycoprotein was localized in coated pits of the cell surface and in intracellular endocytic vesicles (receptosomes/endosomes). The data suggest that the 180/90-kDa glycoprotein is a component of the receptor for α2-macroglobulin.

Original languageEnglish (US)
Pages (from-to)16732-16737
Number of pages6
JournalJournal of Biological Chemistry
Volume261
Issue number35
StatePublished - Dec 1 1986

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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