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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract.

In the course of the genomic cloning of nCL-2, a stomach-specific calpain, we identified a genomic clone encoding a novel member of the calpain large subunit family and designated it ' nCL-4'. First, using exon sequences, we cloned the cDNA for mouse nCL-4. Based on this sequence, we also cloned the cDNAs for rat and human nCL-4. In the case of human nCL-4, the longest open reading frame encodes 690 amino acid residues (Mr 79095) with equal sequence similarities (50-55%) to both ubiquitous and organ-specific calpain large subunits from mammals. The deduced amino acid sequence revealed that nCL-4 is highly conserved among mammals. nCL-4 can be aligned without significant deletions or insertions, and, thus, like other calpains, can be divided into four domains (I-IV). The significant similarity of domains II and IV to those in conventional calpain large subunits suggests the potential protease activity and Ca2+- binding ability of nCL-4. Northern blot analysis revealed that the mRNA for nCL-4 is expressed predominantly in stomach and small intestine but not in uterus, suggesting specialized functions of nCL-4 in the digestive tract. When overexpressed in COS-7 cells, a specific band for nCL-4 was detected. In addition, the gene coding for nCL-4 was localized on human chromosome 1.[1]

References

  1. Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract. Lee, H.J., Sorimachi, H., Jeong, S.Y., Ishiura, S., Suzuki, K. Biol. Chem. (1998) [Pubmed]
 
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