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Macrophage proteases can modify low density lipoproteins to increase their uptake by macrophages
Author(s) -
Leake David S.,
Rankin Sara M.,
Collard Jane
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81156-i
Subject(s) - pepstatin , proteases , leupeptin , chemistry , proteolysis , cathepsin , macrophage , protease , biochemistry , low density lipoprotein , microbiology and biotechnology , cholesterol , enzyme , biology , in vitro
When low density lipoprotein (LDL) was incubated with sonicated macrophages at acidic pH, its protein moiety was partially degraded by cathepsins B and D. The reisolated LDL was taken up by intact macrophages up to about 20 times as fast as control LDL. LDL proteolysis and its enhanced uptake could be inhibited almost entirely by the selective protease inhibitors leupeptin and pepstatin. If macrophages in atherosclerotic lesions were to release acidic proteases (either by exocytosis or following cell death) and these were to modify LDL, this may help to explain why so much cholesteryl ester accumulates in these cells.