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Research article

Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues within the N-terminus of the muscle isoform influence the kinetic properties of the enzyme

Nigel T. PRICE, Vicky N. JACKSON, Feike R. van der LEIJ, Jacqueline M. CAMERON, Maureen T. TRAVERS, Beatrijs BARTELDS, Nicolette C. HUIJKMAN, Victor A. ZAMMIT
Biochemical Journal Jun 15, 2003, 372 (3) 871-879; DOI: 10.1042/bj20030086
Nigel T. PRICE
Hannah Research Institute, Ayr KA6 5HL, U.K.
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Vicky N. JACKSON
Hannah Research Institute, Ayr KA6 5HL, U.K.
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Feike R. van der LEIJ
University Hospital, Department of Pediatrics, University of Groningen, P.O. Box 30 001, NL-9700 RB Groningen, The Netherlands
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Jacqueline M. CAMERON
Hannah Research Institute, Ayr KA6 5HL, U.K.
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Maureen T. TRAVERS
Hannah Research Institute, Ayr KA6 5HL, U.K.
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Beatrijs BARTELDS
University Hospital, Department of Pediatrics, University of Groningen, P.O. Box 30 001, NL-9700 RB Groningen, The Netherlands
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Nicolette C. HUIJKMAN
University Hospital, Department of Pediatrics, University of Groningen, P.O. Box 30 001, NL-9700 RB Groningen, The Netherlands
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Victor A. ZAMMIT
Hannah Research Institute, Ayr KA6 5HL, U.K.
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Abstract

Fatty acid and ketone body metabolism differ considerably between monogastric and ruminant species. The regulation of the key enzymes involved may differ accordingly. Carnitine palmitoyltransferase 1 (CPT 1) is the key locus for the control of long-chain fatty acid β-oxidation and liver ketogenesis. Previously we showed that CPT 1 kinetics in sheep and rat liver mitochondria differ. We cloned cDNAs for both isoforms [liver- (L-) and muscle- (M-)] of ovine CPT 1 in order to elucidate the structural features of these proteins and their genes (CPT1A and CPT1B). Their deduced amino acid sequences show a high degree of conservation compared with orthologues from other mammalian species, with the notable exception of the N-terminus of ovine M-CPT 1. These differences were also present in bovine M-CPT 1, whose N-terminal sequence we determined. In addition, the 5′-end of the sheep CPT1B cDNA suggested a different promoter architecture when compared with previously characterized CPT1B genes. Northern blotting revealed differences in tissue distribution for both CPT1A and CPT1B transcripts compared with other species. In particular, ovine CPT1B mRNA was less tissue restricted, and the predominant transcript in the pancreas was CPT1B. Expression in yeast allowed kinetic characterization of the two native enzymes, and of a chimaera in which the distinctive N-terminal segment of ovine M-CPT 1 was replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimaera, relative to the parental ovine M-CPT 1.

  • acyltransferase
  • fatty acid metabolism
  • malonyl-CoA

Footnotes

  • The nucleotide sequence data reported will appear in DDBJ, EMBL, GenBank® and GSDB Nucleotide Sequence Databases; the sequences of ovine CPT1A and CPT1B cDNAs have the accession numbers Y18387 and AJ272435 respectively and the partial adipose tissue and liver CPT1A clones have the accession numbers Y18830 and Y18829 respectively.

  • Abbreviations used: CPT 1, carnitine palmitoyltransferase 1 (the prefixes L- and M- refer to the liver and muscle isoforms respectively); COT, carnitine octanoyltransferase; EST, expressed sequence tag; RACE, rapid amplification of cDNA ends; UTR, untranslated region.

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June 2003

Volume: 372 Issue: 3

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Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues within the N-terminus of the muscle isoform influence the kinetic properties of the enzyme
Nigel T. PRICE, Vicky N. JACKSON, Feike R. van der LEIJ, Jacqueline M. CAMERON, Maureen T. TRAVERS, Beatrijs BARTELDS, Nicolette C. HUIJKMAN, Victor A. ZAMMIT
Biochemical Journal Jun 2003, 372 (3) 871-879; DOI: 10.1042/bj20030086
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Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues within the N-terminus of the muscle isoform influence the kinetic properties of the enzyme
Nigel T. PRICE, Vicky N. JACKSON, Feike R. van der LEIJ, Jacqueline M. CAMERON, Maureen T. TRAVERS, Beatrijs BARTELDS, Nicolette C. HUIJKMAN, Victor A. ZAMMIT
Biochemical Journal Jun 2003, 372 (3) 871-879; DOI: 10.1042/bj20030086

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Keywords

acyltransferase
fatty acid metabolism
malonyl-CoA

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