Carnitine palmitoyl transferase I: Conformational changes induced by long-chain fatty acyl CoA ligands

The effect of long-chain acyl-CoA on subcellular adenine nucleotide systems was studied in the intact liver cell. Long-chain acyl-CoA content was varied by varying the nutritional state (fed and starved states) or by addition of oleate. Starvation led to an increase in the mitochondrial and a decrease in the cytosolic ATP/ADP ratio in liver both in vivo and in the isolated perfused organ as compared with the fed state. The changes were reversed on re-feeding glucose in liver in vivo or on infusion of substrates (glucose, glycerol) in the perfused liver, respectively. Similar changes in mitochondrial and cytosolic ATP/ADP ratios occurred on addition of oleate, but, importantly, not with a short-chain fatty acid such as octanoate. It is concluded that long-chain acyl-CoA exerts an inhibitory effect on mitochondrial adenine nucleotide translocation in the intact cell, as was previously postulated in the literature from data obtained with isolated mitochondria. The physiological relevance with respect to pyruvate metabolism, i.e. regulation of pyruvate carboxylase and pyruvate dehydrogenase by the mitochondrial ATP/ADP ratio, is discussed.

Download Full-text

HDAC8 Catalyzes the Hydrolysis of Long Chain Fatty Acyl Lysine

ACS Chemical Biology ◽

10.1021/acschembio.6b00396 ◽

2016 ◽

Vol 11 (10) ◽

pp. 2685-2692 ◽

Cited By ~ 44

Author(s):

Pornpun Aramsangtienchai ◽

Nicole A. Spiegelman ◽

Bin He ◽

Seth P. Miller ◽

Lunzhi Dai ◽

...

Keyword(s):

Fatty Acyl ◽

Hydrolysis Of ◽

Long Chain

Download Full-text

Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane

The Journal of Lipid Research ◽

10.1016/s0022-2275(20)32123-4 ◽

1999 ◽

Vol 40 (5) ◽

pp. 881-892 ◽

Cited By ~ 8

Author(s):

Christina E. Gargiulo ◽

Sarah M. Stuhlsatz-Krouper ◽

Jean E. Schaffer

Keyword(s):

Plasma Membrane ◽

Fatty Acyl ◽

Long Chain

Download Full-text

Expression Profile of Acetyl CoA Carboxylase Beta (ACACB) Gene during the Pre and Post-hatch Period in Chicken

Indian Journal of Animal Research ◽

10.18805/ijar.b-4382 ◽

2021 ◽

Author(s):

Ch. Shiva Prasad ◽

R. Vinoo ◽

R.N. Chatterjee ◽

M. Muralidhar ◽

D. Narendranath ◽

...

Keyword(s):

Gene Expression ◽

Fatty Acid ◽

Expression Pattern ◽

Fatty Acyl ◽

Acid Oxidation ◽

Acetyl Coa Carboxylase ◽

Acetyl Coa ◽

Layer Chicken ◽

Differential Expression Pattern ◽

Long Chain

Background: Acetyl-CoA Carboxylase Beta (ACACB) plays a key role in fatty acid oxidation and was known to be involved in production of very-long-chain fatty acid and other compounds needed for proper development. This gene is mainly expressed in the tissues of heart, muscle, liver and colon. It chiefly involved in the production of malonyl-coA, a potent inhibitor of carnitine palmitoyl transferase I (CPT-I) enzyme needed in transport of long-chain fatty acyl-coAs to the mitochondria for β-oxidation.Methods: The present study was conducted to explore the expression pattern of the ACACB gene in breast muscle tissue during pre-hatch embryonic day (ED) 5th to 18th and post-hatch (18th, 22nd and 40th week of age) periods of White leghorn (IWI line) by using Quantitative real-time PCR (qPCR). Then, fold change of ACACB gene expression was calculated.Result: Our study showed that the ACACB gene expression was down-regulated during embryonic stages from ED6 to ED18. The gene expression was also down-regulated during adult stages i.e. on 22nd and 40th week of age. This result indicated that the initial expression of the ACACB gene is required for embryo development and during adult periods, low gene expression leads to the less fat deposition in muscle of layer chicken. Finally, it can be concluded that there was a differential expression pattern of the ACACB gene during the pre-hatch embryonic and post-hatch adult periods to mitigate varied requirements of lipids during different physiological stages in layer chicken.

Download Full-text

III. Peroxisomal β-oxidation, PPARα, and steatohepatitis

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.2001.281.6.g1333 ◽

2001 ◽

Vol 281 (6) ◽

pp. G1333-G1339 ◽

Cited By ~ 142

Author(s):

Janardan K. Reddy

Keyword(s):

Fatty Acids ◽

Dicarboxylic Acids ◽

Fatty Acyl ◽

Branched Chain Fatty Acids ◽

Oxidation Chain ◽

Branched Chain ◽

Cytochrome P 450 ◽

Oxidation System ◽

Long Chain ◽

Chain Fatty Acids

Peroxisomes are involved in the β-oxidation chain shortening of long-chain and very-long-chain fatty acyl-CoAs, long-chain dicarboxylyl-CoAs, the CoA esters of eicosanoids, 2-methyl-branched fatty acyl-CoAs, and the CoA esters of the bile acid intermediates, and in the process, they generate H2O2. There are two complete sets of β-oxidation enzymes present in peroxisomes, with each set consisting of three distinct enzymes. The classic PPARα-regulated and inducible set participates in the β-oxidation of straight-chain fatty acids, whereas the second noninducible set acts on branched-chain fatty acids. Long-chain and very-long-chain fatty acids are also metabolized by the cytochrome P-450 CYP4A ω-oxidation system to dicarboxylic acids that serve as substrates for peroxisomal β-oxidation. Evidence derived from mouse models of PPARα and peroxisomal β-oxidation deficiency highlights the critical importance of the defects in PPARα-inducible β-oxidation in energy metabolism and in the development of steatohepatitis.

Download Full-text