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Papers In Press, published online ahead of print May 25, 2001
Oral Molecular biology, Oregon Health Sciences University, Portland, OR 97201
Corresponding Author: shearert{at}ohsu.edu
Calpains are calcium-dependent, intracellular, non-lysosomal proteases believed to hydrolyze specific substrates important in calcium regulated signaling pathways. Recently, an atypical member of the calpain family, calpain 10, was described, and genetic variation in this gene was associated with an increased risk of type II diabetes mellitis in humans. In the present report, a polyclonal antibody directed against rat calpain 10 was developed. This antibody was used to monitor the expression of calpain10 protein in tissues from rats, mice and humans. Calpain 10 protein was found to be present in all tissues examined by western blotting including lens, retina, brain, heart and skeletal muscle. While some calpain 10 was detectable in the water soluble protein fraction of these tissues, it was preferentially found in the water insoluble fraction. In the lens, immunohistochemistry revealed that calpain 10 was predominately located in the cytoplasm of epithelial and newly differentiating lens fibers at the transition zone. However, calpain 10 was found associated with the plasma membrane of differentiated lens fiber cells and with the sarcolemma of skeletal muscle. In the lens epithelium-derived cell line aTN4-1, calpain 10 protein was found in a punctate distribution in the cell nucleus as well as the cytoplasm. Following elevation of intracellular calcium levels with ionomycin, calpain 10 protein levels in the nucleus of aTN4-1 cells increased markedly while those in the cytoplasm decreased. In the lens, elevation of intracellular calcium levels following selenite administration resulted in increased levels of calpain 10 RNA within one day and a loss of calpain 10 protein from the lens nucleus coincident with the onset of selenite cataract. In conclusion, calpain 10 appears to be a ubiquitous calpain whose expression level and subcellular distribution is dynamically influenced by calcium.
J. Biol. Chem, 10.1074/jbc.M100603200
Submitted on January 23, 2001
Revised on May 24, 2001
Accepted on May 25, 2001
Characterization and expression of calpain 10: a novel ubiquitous calpain with nuclear localization
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