Acyl-Coenzyme A Binding Protein Expression Alters Liver Fatty Acyl-Coenzyme A Metabolism†

Biochemistry ◽  
2005 ◽  
Vol 44 (30) ◽  
pp. 10282-10297 ◽  
Author(s):  
Huan Huang ◽  
Barbara P. Atshaves ◽  
Andrey Frolov ◽  
Ann B. Kier ◽  
Friedhelm Schroeder
Biochemistry ◽  
1994 ◽  
Vol 33 (11) ◽  
pp. 3327-3334 ◽  
Author(s):  
Timothy Hubbell ◽  
William D. Behnke ◽  
Judith K. Woodford ◽  
Friedhelm Schroeder

1996 ◽  
Vol 271 (50) ◽  
pp. 31878-31884 ◽  
Author(s):  
Andrey Frolov ◽  
Tae-Hyeon Cho ◽  
Jeffrey T. Billheimer ◽  
Friedhelm Schroeder

1996 ◽  
Vol 271 (40) ◽  
pp. 24698-24710 ◽  
Author(s):  
Chun-Yang Fan ◽  
Jie Pan ◽  
Ruiyin Chu ◽  
Denise Lee ◽  
Kimberly D. Kluckman ◽  
...  

2009 ◽  
Vol 29 (17) ◽  
pp. 4864-4872 ◽  
Author(s):  
Seung-Soon Im ◽  
Linda E. Hammond ◽  
Leyla Yousef ◽  
Cherryl Nugas-Selby ◽  
Dong-Ju Shin ◽  
...  

ABSTRACT We generated a line of mice in which sterol regulatory element binding protein 1a (SREBP-1a) was specifically inactivated by insertional mutagenesis. Homozygous mutant mice were completely viable despite expressing SREBP-1a mRNA below 5% of normal, and there were minimal effects on expression of either SREBP-1c or -2. Microarray expression studies in liver, where SREBP-1a mRNA is 1/10 the level of the highly similar SREBP-1c, demonstrated that only a few genes were affected. The only downregulated genes directly linked to lipid metabolism were Srebf1 (which encodes SREBP-1) and Acacb (which encodes acetyl coenzyme A [acetyl-CoA] carboxylase 2 [ACC2], a critical regulator of fatty acyl-CoA partitioning between cytosol and mitochondria). ACC2 regulation is particularly important during food restriction. Similar to Acacb knockout mice, SREBP-1a-deficient mice have lower hepatic triglycerides and higher serum ketones during fasting than wild-type mice. SREBP-1a and -1c have identical DNA binding and dimerization domains; thus, the failure of the more abundant SREBP-1c to substitute for activating hepatic ACC2 must relate to more efficient recruitment of transcriptional coactivators to the more potent SREBP-1a activation domain. Our chromatin immunoprecipitation results support this hypothesis.


Sign in / Sign up

Export Citation Format

Share Document