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Journal of Lipid Research, Vol 28, 1405-1409, Copyright © 1987 by Lipid Research, Inc.

ARTICLES

Molecular cloning of a human apoC-III variant: Thr 74----Ala 74 mutation prevents O-glycosylation

H Maeda, RK Hashimoto, T Ogura, S Hiraga and H Uzawa
Department of Molecular Genetics, Kumamoto University Medical School, Japan.

Apolipoprotein C-III (apoC-III) is a major protein of very low density lipoprotein (VLDL). The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74. We have cloned the apoC-III gene from a subject whose serum contained unusually high amounts of apoC-III lacking the carbohydrate moiety (C-III-0). DNA sequence analysis of the cloned gene revealed a single nucleotide substitution (A----G) that encodes an alanine at position 74 instead of the normal threonine. As a result of this amino acid replacement, the mutant apoC-III polypeptide is not glycosylated. The mutation in the apoC-III gene creates a novel AluI site that permits diagnosis of the change by Southern blotting of genomic DNA.
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