Identification of human acetyl-CoA carboxylase isozymes in tissue and in breast cancer cells |
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Authors: | LA Witters J Widmer AN King K Fassihi F Kuhajda |
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Affiliation: | Department of Medicine, Dartmouth Medical School, Hanover, NH 03755-3833. |
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Abstract: | 1. In the rat, acetyl-CoA carboxylase (ACC), a rate-limiting enzyme in fatty acid metabolism, exists as at least two different isozymes (M(r) 265,000 and 280,000) that display distinct tissue-specific distribution and regulation. 2. Based on the study of human tissue and human-derived breast cancer cell lines by enzyme isolation and protein blotting techniques, we have now identified two human isoforms of M(r) 265,000 (HACC 265) and 275,000 (HACC 275), each of which is homologous to one of the rat isozymes. 3. Human breast carcinoma cell lines show variable expression of these two isoforms, mirrored in the estimation of ACC acetyl-CoA kinetics. |
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