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Receptors for Maleylated Proteins Regulate Secretion of Neutral Proteases by Murine Macrophages
William J. Johnson, Salvatore V. Pizzo, Michael J. Imber and Dolph O. Adams
New Series, Vol. 218, No. 4572 (Nov. 5, 1982), pp. 574-576
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/1688672
Page Count: 3
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Receptors for maleylated or acetylated proteins as well as for α -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 α -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.
Science © 1982 American Association for the Advancement of Science