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Related Experiment Videos

Microsomal malonyl-CoA-sensitive carnitine acyltransferase.

N M Broadway1, R J Pease, G Birdsey

  • 1Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K.

Biochemical Society Transactions
|May 18, 2001
PubMed
Summary

Researchers investigated carnitine palmitoyltransferase-1 (CPT-1) in liver microsomes. Despite cross-reactivity suggesting dual localization, experiments failed to confirm CPT-1

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Metabolism

Background:

  • Liver microsomes possess carnitine acyltransferase activities.
  • One activity mirrors mitochondrial carnitine palmitoyltransferase-1 (CPT-1) at 88 kDa.
  • Antibodies to CPT-1 react with an 88 kDa microsomal protein.

Purpose of the Study:

  • To determine if carnitine palmitoyltransferase-1 (CPT-1) is present in both mitochondrial and microsomal membranes.
  • To investigate the localization of CPT-1 using molecular biology techniques.

Main Methods:

  • Immunological cross-reactivity assays using antisera against CPT-1.
  • In vitro translation experiments with microsomes.
  • In vivo transfection studies using COS-1 cells with CPT-1 cDNAs.

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Main Results:

  • Antisera against CPT-1 showed cross-reactivity with an 88 kDa microsomal protein.
  • Experiments involving CPT-1 cDNAs, in vitro translation, and COS-1 cell transfection did not provide evidence for microsomal CPT-1.
  • The hypothesis of CPT-1 targeting to both membrane types was not supported by experimental data.

Conclusions:

  • While immunological data suggested potential dual localization, molecular experiments failed to confirm the presence of carnitine palmitoyltransferase-1 (CPT-1) in liver microsomes.
  • Further investigation is needed to elucidate the identity and function of the microsomal carnitine acyltransferase activity.