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J. Biol. Chem., Vol. 256, Issue 14, 7105-7108, 07, 1981
JC Khoo, EM Mahoney and JL Witztum
Cultured macrophages were shown to synthesize and constitutively secrete a
triglyceride lipase identified as lipoprotein lipase on the basis of the
following criteria: 1) it required apolipoprotein C-II for optimal
activity; 2) it exhibited maximal activity at pH 8.2; 3) it was inhibited
by 1 M NaCl; 4) it bound tightly to a heparin-Sepharose affinity gel and
was eluted with buffer containing 1.5 M NaCl; and 5) the quantity of enzyme
released from macrophages was enhanced by heparin. Cycloheximide treatment
of macrophage cultures blocked the spontaneous secretion of lipoprotein
lipase. Macrophage secretion of lipoprotein lipase may be relevant to the
role of this cell in atherogenesis.
Secretion of lipoprotein lipase by macrophages in culture
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