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Journal of Lipid Research, Vol 26, 451-456, Copyright © 1985 by Lipid Research, Inc.
SK Karathanasis, VI Zannis and JL Breslow
We have recently reported that the human apolipoprotein A-I (apoA-I) and
apolipoprotein C-III (apoC-III) genes are physically linked and that the
presence of a DNA insertion in the apoA-I gene is correlated with
apoA-I-apoC-III deficiency in patients with premature atherosclerosis. In
addition, the presence of a polymorphic restriction endonuclease site
(SacI) in the 3' noncoding region of apoC-III mRNA has been correlated with
hypertriglyceridemia in humans. In this study, we report the isolation and
characterization of cDNA clones containing the entire apoC-III mRNA coding
sequence. The nucleotide-derived apoC- III amino acid sequence indicates
that the apoC-III primary translational product contains a 20 amino acid
N-terminal extension, which conforms with the general properties of known
signal peptides, and is highly homologous to the recently reported rat
apoC-III signal peptide. The DNA-derived apoC-III amino acid sequence
differs from the previously reported apoC-III amino acid sequence at four
amino acid residues. More specifically, at positions +32, +33, +37, +39,
the DNA sequence predicts Glu, Ser, Gln, Ala, respectively, while the
previously reported sequence specifies Ser, Gln, Ala, Gln, respectively.
Finally, isolation and characterization of apoC-III cDNA clones, with or
without the polymorphic SacI restriction site, indicated that the apoC-III
nucleotide sequence corresponding to the Sac+ and Sac- clones differs at
three nucleotide sites; however, the amino acid sequence specified by the
Sac+ and Sac- alleles is identical.
ARTICLES
Isolation and characterization of cDNA clones corresponding to two different human apoC-III alleles
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