Characterization of the IgA receptor from human polymorphonuclear leucocytes

Immunology. 1988 Jun;64(2):201-5.

Abstract

Human polymorphonuclear leucocytes (PMNs) will phagocytose yeasts opsonized with specific affinity-purified human serum IgA. PMNs also bind to Sepharose beads coated with IgA or IgG, but not to beads coated with bovine serum albumin (BSA) or horseradish peroxidase (HRP). Binding to IgA-Sepharose stimulates the cells to release lysozyme. Affinity chromatography of 125I-labelled PMN membrane proteins on IgA-Sepharose results in isolation of a polypeptide of apparent 60,000 MW. The protein, which is not bound to IgG-Sepharose under the same conditions, appears as a diffuse band on SDS-PAGE, suggesting it is heavily glycosylated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD*
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoglobulin A / immunology
  • Immunoglobulin A / isolation & purification
  • Neutrophils / immunology*
  • Neutrophils / metabolism
  • Phagocytosis
  • Receptors, Fc / isolation & purification*
  • Saccharomyces cerevisiae / immunology
  • Sepharose / metabolism

Substances

  • Antigens, CD
  • Fc(alpha) receptor
  • Immunoglobulin A
  • Receptors, Fc
  • Sepharose