Linked Life Data

9703953

Source:http://linkedlifedata.com/resource/pubmed/id/9703953

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-9-8
pubmed:abstractText
The present work was performed to identify the possible roles of acetyl-CoA carboxylase isoforms (ACC-alpha and ACC-beta). Two forms show 70% amino acid identity, but N-terminal regions share no homology, indicating that these may be uniquely related to the specific role of each ACC form. Thus, we investigated whether introduction of the exogenous ACC N-terminus into H9c2 cardiomyocytes that express both ACC forms causes a noticeable change in a specific pathway of fatty acid metabolism. The effect of ACC-alpha N-terminus overexpression was specific to the fatty acid synthesis rate resulting in an 80% induction, whereas overexpression of the ACC-beta N-terminus increased fatty acid oxidation rate 50% without affecting the fatty acid synthesis rate. These results suggest that ACC-alpha and beta are involved in the regulation of fatty acid synthesis and oxidation, respectively, and that the N-terminus plays an important role in the process. We further demonstrated that novel proteins specifically bound to the ACC N-terminus. This interaction may mediate the involvement of each ACC form in different cellular activities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
248
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
490-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Evidence that acetyl-CoA carboxylase isoforms play different biological roles in H9c2 cardiomyocyte.
pubmed:affiliation
Department of Chemistry, Hanyang University, Seoul, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't