Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-4-10
pubmed:abstractText
Calpains are calcium-regulated proteases involved in cellular functions that include muscle proteolysis both ante- and post-mortem. This study was designed to clone the complete coding sequence of the porcine calpain10 gene, CAPN10, to analyze its expression characteristics and to investigate its polymorphism. Two isoforms of the CAPN10 gene, CAPN10A and CAPN10B, were obtained by reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends methods combined with in silico cloning. RT-PCR results indicated that CAPN10 mRNA was ubiquitously expressed in all tissues examined and, with increasing age, the expression level increased in muscles at six different growth points. In the same tissues, the expression level of CAPN10A was higher than that of CAPN10B. In addition, three single nucleotide polymorphisms were detected by the PCR-single-stranded conformational polymorphism method and by comparing the sequences of Chinese Min pigs with those of Yorkshire pigs. C527T mutation was a missense mutation and led to transforming Pro into Leu at the 176 th amino acid. The results of the current study provided basic molecular information for further study of the function of the porcine CAPN10 gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1745-7270
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
356-63
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Cloning, expression, and polymorphism of the porcine calpain10 gene.
pubmed:affiliation
College of Animal Science and Technology, Northeast Agricultural University, Harbin 150030, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't