Receptors for maleylated proteins regulate secretion of neutral proteases by murine macrophages.
Journal Article (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
Digital Object Identifier (DOI)
- 10.1126/science.6289443
Language
- eng
Conference Location
- United States