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J. Biol. Chem., Vol. 265, Issue 3, 1502-1509, Jan, 1990
A Bianchi, JL Evans, AJ Iverson, AC Nordlund, TD Watts and LA Witters
Acetyl-CoA carboxylase (ACC) is a major rate-limiting enzyme of fatty acid
biosynthesis; its product, malonyl-CoA, also contributes to the regulation
of fatty acid oxidation and elongation. Using monospecific antibodies
directed against rat liver ACC and N- and C-terminal antipeptide antibodies
raised against predicted sequences of the cloned ACC of Mr 265,000, we have
identified a unique biotin-containing cytosolic protein of molecular mass
280,000 daltons that is distinct from this 265,000-dalton protein. This
protein is uniquely expressed in rat cardiac and skeletal muscle but is
co-expressed with the 265,000- dalton protein in rat liver, mammary gland,
and brown adipose tissue. In the fed rat, white adipose tissue contains
only the 265,000-dalton protein. Like the 265,000-dalton protein, the
280,000-dalton protein is present predominantly in the cytosolic fraction
of liver. In the liver, the content of both proteins is diminished on
fasting and increases on fasting/refeeding with a high carbohydrate diet.
In contrast, the cardiac and skeletal muscle 280,000-dalton protein content
is unaltered by nutritional manipulation. Avidin-Sepharose isolates of
citrate- dependent ACC from the heart reveal only the 280,000-dalton
protein, while white adipose tissue isolates show only the 265,000 form.
These species differ in the sensitivity to citrate activation and in the Km
for acetyl-CoA. Antibodies reactive with the 280,000-dalton protein on
immunoblotting precipitate ACC activity in heart isolates, while white
adipose ACC is precipitated only by antibodies specific for the 265,000-
dalton species. However, in ACC isolates where both proteins are present, a
heteroisozyme complex can be detected both by immunoprecipitation and by a
sandwich enzyme-linked immunosorbent assay. We conclude that the
280,000-dalton protein is an isozyme of ACC, distinct from the previously
cloned 265,000-dalton species. Its presence in cardiac and skeletal muscle,
where fatty acid synthesis rates are low, suggest that it might play
alternative roles in these tissues such as regulation of fatty acid
oxidation or microsomal fatty acid elongation.
Identification of an isozymic form of acetyl-CoA carboxylase
Department of Medicine, Dartmouth Medical School, Hanover, New Hampshire 03756.
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