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Journal of Lipid Research, Vol 28, 1326-1334, Copyright © 1987 by Lipid Research, Inc.
MH Doolittle, H Wong, RC Davis and MC Schotz
Immunoprecipitations of hepatic lipase from pulse-labeled rat liver have
demonstrated that hepatic lipase is synthesized in two distinct molecular
weight forms, HL-I (Mr = 51,000) and HL-II (Mr = 53,000). Both forms are
immunologically related to purified hepatic lipase, but not to lipoprotein
lipase. HL-I and HL-II are also kinetically related and represent different
stages of intracellular processing. Glycosidase experiments suggest that
HL-I is the high mannose microsomal form of the mature, sialylated HL-II
enzyme. Hepatic lipase activity was detected in liver and adrenal gland but
was absent in brain, heart, kidney, testes, small intestine, lung, and
spleen. The adrenal and liver lipase activities were inhibited in a similar
dose-dependent manner by hepatic lipase antiserum. Immunoblot analysis of
partially purified adrenal lipase showed an immunoreactive band
co-migrating with HL-II at 53,000 daltons which was absent in a control
blot treated with preimmune serum. Adrenal lipase and authentic hepatic
lipase yielded similar peptide maps, confirming the presence of the lipase
in adrenal gland. However, incorporation of L-[35S]methionine into
immunoprecipitable hepatic lipase was not detected in this tissue. In
addition, Northern blot analysis showed the presence of hepatic lipase mRNA
in liver but not adrenal gland. The presence of hepatic lipase in adrenal
gland in the absence of detectable synthesis or messenger suggests that
hepatic lipase originates in liver and is transported to this extrahepatic
site.
ARTICLES
Synthesis of hepatic lipase in liver and extrahepatic tissues
Laboratory of Lipid Research, Veterans Administration, Wadsworth Medical Center, Los Angeles, CA 90073.
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