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J. Biol. Chem., Vol. 276, Issue 30, 28525-28531, July 27, 2001
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From the Calpains are
calcium-dependent intracellular nonlysosomal proteases that
are 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 mellitus 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 calpain 10 protein in
tissues from rats, mice, and humans. Calpain 10 protein was found to be
present in all tissues examined by Western blotting including the lens,
retina, brain, heart, and skeletal muscle. Although 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 to be
associated with the plasma membrane of differentiated lens fiber cells
and the sarcolemma of skeletal muscle. In the lens epithelium-derived
cell line, Departments of Oral Molecular Biology,
Biochemistry and Molecular Biology, and Ophthalmology, Oregon Health & Science University, Portland, Oregon 97201, the § Laboratory
of Biology, Senju Pharmaceutical Company, Ltd., 1-5-4 Murotani,
Nishi-ku, Kobe 651-22, Japan, the ¶ Department of Animal Sciences,
Oregon State University, Corvallis, Oregon 97331, and the
Department of Biological Sciences, Division of Molecular Biology
and Genetics, University of Delaware, Newark, Delaware 19716-2590
TN4-1, the calpain 10 protein was found in a punctate
distribution in the cell nucleus as well as the cytoplasm. After the
elevation of intracellular calcium levels with ionomycin, calpain 10 protein levels in the nucleus of TN4-1 cells increased markedly,
whereas those in the cytoplasm decreased. In the lens, the elevation of intracellular calcium levels after selenite administration resulted in
increased levels of calpain 10 RNA within 1 day and a loss of calpain
10 protein from the lens nucleus coincident with the onset of selenite
cataract. In conclusion, calpain 10 seems to be a ubiquitous calpain,
the expression level and subcellular distribution of which are
dynamically influenced by calcium.
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