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Science 5 November 1982:
Vol. 218. no. 4572, pp. 574 - 576
DOI: 10.1126/science.6289443
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Articles

Science, Vol 218, Issue 4572, 574-576
Copyright © 1982 by American Association for the Advancement of Science

articles

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

WJ Johnson, SV Pizzo, MJ Imber, and DO Adams

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.


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