To gain insight into the function and regulation of malonyl-CoA decarboxylase (MCD) we have cloned rat MCD cDNA from a differentiated insulin-secreting pancreatic β-cell-line cDNA library. The full-length cDNA sequence shows 69% identity with the cDNA cloned previously from the goose uropygial gland, and predicts a 492 amino acid protein of 54.7 kDa. The open reading frame contains an N-terminal mitochondrial targeting sequence and the C-terminal part of the enzyme ends with a peroxisomal (Ser-Lys-Leu) targeting motif. Since the sequence does not reveal hydrophobic domains, MCD is most likely expressed in the mitochondrial matrix and inside the peroxisomes. A second methionine residue, located 3ʹ of the mitochondrial presequence, might be the first amino acid of a putative cytosolic MCD, since the nucleotide sequence around it fits fairly well with a consensus Kozak site for translation initiation. However, primer extension detects the presence of only one transcript initiating upstream of the first ATG, indicating that the major, if not exclusive, transcript expressed in the pancreatic β-cell encodes MCD with its mitochondrial presequence. The sequence also shows multiple possible sites of phosphorylation by casein kinase II and protein kinase C. mRNA tissue-distribution analysis indicates a transcript of 2.2 kb, and that the MCD gene is expressed over a wide range of rat tissues. The distribution of the enzyme shows a broad range of activities from very low in the brain to elevated in the liver and heart. The results provide the foundations for further studies of the role of MCD in lipid metabolism and metabolic signalling in various tissues.
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May 1999
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Research Article|
May 10 1999
Cloning and expression of rat pancreatic β-cell malonyl-CoA decarboxylase
Nicolas VOILLEY;
Nicolas VOILLEY
*Molecular Nutrition Unit, Department of Nutrition, University of Montreal and the CR Centre Hospitalier de l'Université de Montréal and Institut du Cancer, 1560 Sherbrooke Est, Montreal, Quebec H2L 4M1, Canada
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Raphaël RODUIT;
Raphaël RODUIT
*Molecular Nutrition Unit, Department of Nutrition, University of Montreal and the CR Centre Hospitalier de l'Université de Montréal and Institut du Cancer, 1560 Sherbrooke Est, Montreal, Quebec H2L 4M1, Canada
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Raffaela VICARETTI;
Raffaela VICARETTI
*Molecular Nutrition Unit, Department of Nutrition, University of Montreal and the CR Centre Hospitalier de l'Université de Montréal and Institut du Cancer, 1560 Sherbrooke Est, Montreal, Quebec H2L 4M1, Canada
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Christophe BONNY;
Christophe BONNY
†Department of Internal Medicine B, University Hospital, CHUV-1011 Lausanne, Switzerland
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Gérard WAEBER;
Gérard WAEBER
†Department of Internal Medicine B, University Hospital, CHUV-1011 Lausanne, Switzerland
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Jason R. B. DYCK;
Jason R. B. DYCK
‡The Cardiovascular Research Group, University of Alberta, Edmonton, Alberta T6G 2S2, Canada
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Gary D. LOPASCHUK;
Gary D. LOPASCHUK
‡The Cardiovascular Research Group, University of Alberta, Edmonton, Alberta T6G 2S2, Canada
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Marc PRENTKI
Marc PRENTKI
1
*Molecular Nutrition Unit, Department of Nutrition, University of Montreal and the CR Centre Hospitalier de l'Université de Montréal and Institut du Cancer, 1560 Sherbrooke Est, Montreal, Quebec H2L 4M1, Canada
1To whom correspondence should be addressed at Molecular Nutrition Unit, CR Centre Hospitalier de l'Universiteée Montréal, Pavillon de Sève4e, 1560 Sherbrooke Est, Montreal, Quebec H2L 4M1, Canada (e-mail : prentkim@ere.umontreal.ca).
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1999
1999
Biochem J (1999) 340 (1): 213–217.
Citation
Nicolas VOILLEY, Raphaël RODUIT, Raffaela VICARETTI, Christophe BONNY, Gérard WAEBER, Jason R. B. DYCK, Gary D. LOPASCHUK, Marc PRENTKI; Cloning and expression of rat pancreatic β-cell malonyl-CoA decarboxylase. Biochem J 15 May 1999; 340 (1): 213–217. doi: https://doi.org/10.1042/bj3400213
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