| First Author | Lee HJ | Year | 1998 |
| Journal | Biol Chem | Volume | 379 |
| Issue | 2 | Pages | 175-83 |
| PubMed ID | 9524069 | Mgi Jnum | J:73503 |
| Mgi Id | MGI:2155572 | Doi | 10.1515/bchm.1998.379.2.175 |
| Citation | Lee HJ, et al. (1998) Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract. Biol Chem 379(2):175-83 |
| abstractText | 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. |
