Receptors for maleylated proteins regulate secretion of neutral proteases by murine macrophages.

Journal Article

Receptors for maleylated or acetylated proteins as well as for alpha-2-macroglobulin-protease complexes on macrophages serve as scavengers by mediating the uptake of macromolecules from the extracellular compartment. Described in this report is a novel function of these receptors on macrophages: regulation of neutral protease secretion. The binding of maleylated bovine serum albumin to macrophages triggered secretion of three neutral proteases: neutral caseinases, plasminogen activator, and cytolytic proteinase. Release of acid phosphatase, however, was not induced. An important biological consequence of protease secretion by macrophages, tumor-cytolysis, was also triggered by engagement of the receptor for maleylated bovine serum albumin. By contrast, the binding of alpha-2-macroglobulin-protease complexes to the macrophages suppressed secretion of all three proteases. Thus two receptors heretofore believed to serve principally as scavengers also regulate secretory functions of macrophages.

Full Text

Duke Authors

Cited Authors

  • Johnson, WJ; Pizzo, SV; Imber, MJ; Adams, DO

Published Date

  • November 5, 1982

Published In

Volume / Issue

  • 218 / 4572

Start / End Page

  • 574 - 576

PubMed ID

  • 6289443

International Standard Serial Number (ISSN)

  • 0036-8075

Language

  • eng

Conference Location

  • United States