Exp Mol Med.
1998 Jun;30(2):73-79.
Rapid increase of cytosolic content of acetyl-CoA carboxylase isoforms in H9c2
cells by short-term treatment with insulin and okadaic acid
- Affiliations
-
- 1Department of Molecular Biology, College of Medicine, Kyung Hee University,
Seoul, Korea.
Abstract
- Mammalian acetyl-CoA carboxylase (ACC) is present in two isoforms, alpha and
beta, both of which catalyze formation of malonyl-CoA by fixing CO2 into
acetyl-CoA. ACC-alpha is highly expressed in lipogenic tissues whereas ACC-beta
is a predominant form in heart and skeletal muscle tissues. Even though the
tissue-specific expression pattern of two ACC isoforms suggests that each form
may have a distinct function, existence of two isoforms catalyzing the identical
reaction in a same cell has been a puzzling question. As a first step to answer
this question and to identify the possible role of ACC isoforms in myogenic
differentiation, we have investigated in the present study whether the
expression and the subcellular distribution of ACC isoforms in H9c2 cardiac
myocyte change so that malonyl-CoA produced by each form may modulate fatty acid
oxidation. We have observed that the expression levels of both ACC forms were
correlated to the extent of myogenic differentiation and that they were present
not only in cytoplasm but also in other subcellular compartment. Among the
various tested compounds, short-term treatment of H9c2 myotubes with insulin or
okadaic acid rapidly increased the cytosolic content of both ACC isoforms up to
2 folds without affecting the total cellular ACC content. Taken together, these
observations
suggest that both ACC isoforms may play a pivotal role in muscle
differentiation and that they may translocate between cytoplasm and other
subcellular compartment to achieve its specific goal under the various
physiological conditions.