The relationship of rat liver overt carnitine palmitoyltransferase to the mitochondrial malonyl-CoA binding entity and to the latent palmitoyltransferase

Ghadiminejad, Iraj; Saggerson, E D

doi:10.1042/bj2700787

Cited by 28 publications

(20 citation statements)

References 36 publications

(42 reference statements)

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“…Isolation of liver mitochondrial outer membranes This was as described previously [24] except that the final outer membrane pellet was resuspended in potassium phosphate/ glycerol medium as for microsomes.…”

Section: Isolation Of Liver Microsomesmentioning

confidence: 99%

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Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme

Broadway

Saggerson

1995

Biochemical Journal

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Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltransferase activity can be separated into malonyl-CoA-sensitive and -insensitive activities either by gel filtration on Superdex 200 or by anion-exchange chromatography on Resource Q. On gel filtration the apparent molecular masses of the malonyl-CoA-sensitive and -insensitive activities are approx. 300 kDa and 60 kDa respectively. The malonyl-CoA-sensitive and -insensitive activities have different fatty-acyl-chain-length specificities and different stabilities in the detergent octyl glucoside. Together these findings indicate that the malonyl-CoA-sensitive and -insensitive activities are due to different enzymes. The malonyl-CoA sensitivity of the inhibitable enzyme is markedly increased on reconstitution into soybean L-alpha-lecithin liposomes, demonstrating that phospholipids play a crucial role in the inhibition by this metabolite. Evidence is also provided that the malonyl-CoA-sensitive microsomal carnitine acyltransferase is a different enzyme from the malonyl-CoA-sensitive carnitine palmitoyltransferase found in the mitochondrial outer membrane. The possible physiological role of the two microsomal acyltransferases is discussed.

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Section: Isolation Of Liver Microsomesmentioning

confidence: 99%

“…Marker enzyme assays NADPH cytochrome c reductase and succinate dehydrogenase were assayed as described previously [24]. Monoamine oxidase was assayed as described previously [4].…”

Section: Inhibition Of Microsomal Carnitine Acyltransferase By Etomoxmentioning

confidence: 99%

Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme

Broadway

Saggerson

1995

Biochemical Journal

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“…The purified outer membranes obtained from the discontinuous gradient is similar to this fraction obtained by other investigators (21,22). The purified outer membrane fraction is further enriched in outer membrane enzymes and is depleted of inner membrane enzymes ( Table 2).…”

Section: Preparation and Characterization Of Mitochondrial Membranesmentioning

confidence: 77%

Isolation of Hepatic Mitochondrial Contact Sites: Previously Unrecognized Inner Membrane Components

Hoppel

Kerner

Turkaly

et al. 2002

Analytical Biochemistry

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“…Liver mitochondria were isolated from 200 mg of liver tissue and the activity of CPT‐1a was measured using a spectrophotometric method . The assay measured the rate of formation of coenzyme A (CoA) from the reaction of palmitoyl CoA and L‐carnitine catalyzed by CPT‐1a.…”

Section: Methodsmentioning

confidence: 99%

Decreased liver triglyceride content in adult rats exposed to protein restriction during gestation and lactation: Role of hepatic triglyceride utilization

Qasem

Tang

et al. 2015

Clin Exp Pharma Physio

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We have previously demonstrated that protein restriction throughout gestation and lactation reduced liver triglyceride content in adult rat offspring. The mechanism(s) mediating the decrease in liver triglyceride content are not understood. The objective of the current study was to use a new group of pregnant animals and their offspring and determine the contribution of increased triglyceride utilization via the hepatic fatty acid oxidation and triglyceride secretory pathways to the reduction in liver triglyceride content. Pregnant Sprague-Dawley rats received either a control or a low protein diet throughout pregnancy and lactation. Pups were weaned onto laboratory chow on day 28 and sacrificed on day 65. Liver triglyceride content was reduced in male, but not female, low protein offspring both in the fed and fasted states. The reduction was accompanied by a trend towards higher liver carnitine palmitoyltransferase-1a activity suggesting increased fatty acid transport into the mitochondrial matrix. However, medium chain acyl CoA dehydrogenase activity within the mitochondrial matrix, expression of nuclear peroxisome proliferator activated receptor-α, and plasma levels of β-hydroxybutyrate were similar between low protein and control offspring indicating a lack of change in fatty acid oxidation. Hepatic triglyceride secretion, assessed by blocking peripheral triglyceride utilization and measuring serum triglyceride accumulation rate, and the activity of microsomal transfer protein were similar between low protein and control offspring. Since enhanced triglyceride utilization is not a significant contributor, the decrease in liver triglyceride content in male low protein offspring is likely due to alterations in liver fatty acid transport or triglyceride biosynthesis.

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The relationship of rat liver overt carnitine palmitoyltransferase to the mitochondrial malonyl-CoA binding entity and to the latent palmitoyltransferase

Cited by 28 publications

References 36 publications

Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme

Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme

Isolation of Hepatic Mitochondrial Contact Sites: Previously Unrecognized Inner Membrane Components

Decreased liver triglyceride content in adult rats exposed to protein restriction during gestation and lactation: Role of hepatic triglyceride utilization

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