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Journal of Lipid Research, Vol 37, 1616-1622, Copyright © 1996 by Lipid Research, Inc.
Y Murata, E Maeda, G Yoshino and M Kasuga
Structure of rabbit lecithin:cholesterol acyltransferase (LCAT) and
molecular basis for the effects of cholesterol feeding on LCAT expression
were investigated by cloning and sequencing LCAT cDNA from rabbit. The
rabbit and human sequences are 91% identical at the nucleotide level and
93% identical at the amino acid level. The interfacial substrate active
site, asparagine-linked glycosylation sites, and sites at which rare
mutations cause human familial LCAT deficiency are all highly conserved in
the rabbit protein. The apparent molecular mass of rabbit LCAT, as
determined by immunoblot analysis, was approximately equal to that of human
LCAT. Rabbits showed 2.6- and 5.5-fold increases in serum LCAT activity 3
and 6 weeks, respectively, after switching to a cholesterol-enriched diet.
Northern blot analysis revealed that the abundance of LCAT mRNA in liver
increased 1.6- and 2.8-fold after 3 and 6 weeks, respectively, of
cholesterol feeding. The marked temporal relation between the increase in
serum LCAT activity and the liver LCAT mRNA abundance suggest that the
regulation of LCAT activity in vivo may be primarily determined by changes
in the amount of LCAT mRNA.
ARTICLES
Cloning of rabbit LCAT cDNA: increase in LCAT mRNA abundance in the liver of cholesterol-fed rabbits
Second Department of Internal Medicine, Kobe University School of Medicine, Japan.
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