Characterization of the porcine carboxypeptidase E cDNA: comparative analysis and investigation of a non-synonymous SNP
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Characterization of the porcine carboxypeptidase E cDNA : comparative analysis and investigation of a non-synonymous SNP. / Hreidarsdôttir, G.E.; Cirera, Susanna; Fredholm, Merete.
In: Animal Biotechnology (Print Edition), Vol. 18, No. 1, 2007, p. 61-64.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Characterization of the porcine carboxypeptidase E cDNA
T2 - comparative analysis and investigation of a non-synonymous SNP
AU - Hreidarsdôttir, G.E.
AU - Cirera, Susanna
AU - Fredholm, Merete
PY - 2007
Y1 - 2007
N2 - Carboxypeptidase E (CPE) is an important enzyme responsible for the proteolytic processing of prohormone intermediates. A naturally occurring point mutation, leading to an accumulation of many neuroendocrine peptides has been characterized within exon 5 of the CPE gene in mice. In the present study the sequence of the cDNA for the porcine CPE gene including all the coding region and the 3'-UTR region was generated. Comparisons with bovine, human, mouse, and rat CPE cDNA sequences showed that the coding regions of the gene are highly conserved both at the nucleotide and at the amino acid level. A very low nonsynonymousl/synonymous substitution ratios between the proteins was found indicating that purifying selection os acting on the CPE gene. A nonsynonymous SNP identified at position 1272 in the transcript resulting in a codon change from TCA (Serine) to TTA (Leucine) was genotyped in the Danish pig populations. However, the mutated allele was only identified in one particular family. Exon 5 was sequenced in 45 unrelated pigs. No evidence of variation was found in this region. In accordance with previous results and in accordance with comparative mapping information the gene was accurately mapped to porcine chromosome 8 using the ImpRH panel.
AB - Carboxypeptidase E (CPE) is an important enzyme responsible for the proteolytic processing of prohormone intermediates. A naturally occurring point mutation, leading to an accumulation of many neuroendocrine peptides has been characterized within exon 5 of the CPE gene in mice. In the present study the sequence of the cDNA for the porcine CPE gene including all the coding region and the 3'-UTR region was generated. Comparisons with bovine, human, mouse, and rat CPE cDNA sequences showed that the coding regions of the gene are highly conserved both at the nucleotide and at the amino acid level. A very low nonsynonymousl/synonymous substitution ratios between the proteins was found indicating that purifying selection os acting on the CPE gene. A nonsynonymous SNP identified at position 1272 in the transcript resulting in a codon change from TCA (Serine) to TTA (Leucine) was genotyped in the Danish pig populations. However, the mutated allele was only identified in one particular family. Exon 5 was sequenced in 45 unrelated pigs. No evidence of variation was found in this region. In accordance with previous results and in accordance with comparative mapping information the gene was accurately mapped to porcine chromosome 8 using the ImpRH panel.
KW - Former LIFE faculty
KW - Carboxypeptidase E
KW - Conservation
KW - SNP
KW - Substitution ratio
U2 - 10.1080/10495390600846139
DO - 10.1080/10495390600846139
M3 - Journal article
C2 - 17364445
VL - 18
SP - 61
EP - 64
JO - Animal Biotechnology
JF - Animal Biotechnology
SN - 1049-5398
IS - 1
ER -
ID: 8067487