Expression of three calpain isoform genes in human skeletal muscles

Journal of the Neurological Sciences

Volumn 155, Issue 2, 1998, Pages 163-169

  Ueyama, Hidetsugu ^a   Kumamoto, Toshihide ^a   Fujimoto, Shin ^a   Murakami, Tatsufumi ^b   Tsuda, Tomiyasu ^a  

^a OITA UNIVERSITY   (Japan)

^b KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

Author keywords

Amyotrophic lateral sclerosis; Calpain; Human muscle; Isoform; mRNA; Progressive muscular dystrophy; RT PCR

Indexed keywords

CALPAIN;

ADOLESCENT; ADULT; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; GENE EXPRESSION; GENETIC TRANSCRIPTION; HUMAN; MALE; MUSCLE BIOPSY; OLIGONUCLEOTIDE PROBE; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA TRANSLATION; SCHOOL CHILD; SKELETAL MUSCLE;

ADOLESCENT; ADULT; AGED; AMYOTROPHIC LATERAL SCLEROSIS; CALPAIN; CHILD; DNA PRIMERS; FEMALE; HUMANS; ISOENZYMES; MALE; MIDDLE AGED; MUSCLE, SKELETAL; MUSCULAR DYSTROPHIES; POLYMERASE CHAIN REACTION; RNA, MESSENGER; UP-REGULATION;

EID: 0032485455     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-510X(97)00309-2     Document Type: Article

References (35)

1. Adachi Y., Ozawa A.K., Sugamura K.et al. Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. J. Biol. Chem. 267:1992;19373-19378.
2. Amemiya Y., Miyahara J. Imaging plate illuminates many fields. Nature. 336:1988;89-90.
3. 2+-activated neutral protease (mCANP) deduced from its cDNA sequence. FEBS Lett. 205:1986;313-317.
4. Bodensteiner J.B., Engel A.G. Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: a study of 567 000 muscle fibers in 114 biopsies. Neurology. 28:1978;439-446.
5. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
6. 2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme. Biochemistry. 15:1976;2159-2167.
7. Deshpande R.V., Goust J.M., Chakrabarti A.K., Barbosa E., Hogan E.L., Banik N.L. Calpain expression in lymphoid cells. Increased mRNA and protein levels after cell activation. J. Biol. Chem. 270:1995;2497-2505.
8. Goll D.E., Dayton W.R., Singh I., Robson R.M. Studies of the α-actinin/actin interaction in the Z-disk by using calpain. J. Biol. Chem. 266:1991;8501-8510.
9. Goll D.E., Thompson V.F., Taylor R.G., Zalewska T. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssays. 14:1992;549-556.
10. Hata A., Ohno S., Akita Y., Suzuki K. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. J. Biol. Chem. 264:1989;6404-6411.
11. Hata A., Ohno S., Suzuki K. Transcriptional activation of the gene for the large subunit of human m-calpain by 12-o-tetradecanoyl-phorbol-13-acetate. FEBS Lett. 304:1992;241-244.
12. Hoffman E.P., Brown R.H., Kunkel L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell. 51:1987;919-928.
13. Iijima N.S., Hamada H., Reddy P., Kakunaga T. Molecular structure of the human cytoplasmic β-actin gene: Interspecies homology of sequences in the introns. Proc. Natl. Acad. Sci. USA. 82:1985;6133-6137.
14. Ilian M.A., Forsberg N.E. Gene expression of calpains and their specific endogeneous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits. Biochem. J. 287:1992;163-171.
15. 2+-activated neutral protease. Biochemistry. 27:1988;8122-8128.
16. Kar N.C., Pearson C.M. A calcium-activated neutral protease in normal and dystrophic human muscle. Clin. Chim. Acta. 73:1976;293-297.
17. Kinoshita T., Imamura J., Nagai H., Shimotohno K. Quantification of gene expression over a wide range by the polymerase chain reaction. Anal. Biochem. 206:1992;231-235.
18. 2+-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle. Anat. Rec. 232:1992;60-77.
19. Kumamoto T., Ueyama H., Watanabe S., Kominami E., Ando M. Muscle fiber degradation in distal myopathy with rimmed vacuoles. Acta Neuropathol. 87:1994;143-148.
20. Kumamoto T., Ueyama H., Watanabe S.et al. Immunohistochemical study of calpain and its endogenous inhibitor in the skeletal muscle of muscular dystrophy. Acta Neuropathol. 89:1995;399-403.
21. Kumamoto T., Ueyama H., Sugihara R., Kominami E., Goll D.E., Tsuda T. Calpain and cathepsins in the skeletal muscle of inflammatory myopathies. Eur. Neurol. 37:1997;176-181.
22. 2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients. Proc. Natl. Acad. Sci. USA. 93:1996;2714-2718.
23. Mellgren R.L. Calcium-dependent proteases: an enzyme system active at cellular membranes? FASEB J. 1:1987;110-115.
24. Parr T., Bardsley R.G., Gilmour R.S., Buttery P.J. Changes in calpain and calpastatin mRNA induced by β-adrenergic stimulation of bovine skeletal muscle. Eur. J. Biochem. 208:1992;333-339.
25. Poussard S., Cottin P., Brustis J.J., Talmat S., Elamrani N., Ducastaing A. Quantitative measurement of calpain I and II mRNAs in differentiating rat muscle cells using a competitive polymerase chain reaction method. Biochimie. 75:1993;885-890.
26. Reddy P.A., Anandavalli T.E., Anandaraj M.P.J.S. Calcium activated neutral proteases (milli- and micro-CANP) and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD). Clin. Chim. Acta. 160:1986;281-288.
27. Richard I., Broux O., Allamand V.et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 81:1995;27-40.
28. Saido T.C., Sorimachi H., Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:1994;814-822.
29. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
30. Sorimachi H., Ohmi S.I., Emori Y.et al. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and m-types: Specific expression of the mRNA in skeletal muscle. J. Biol. Chem. 264:1989;20106-20111.
31. Spencer M.J., Croall D.E., Tidball J.G. Calpains are activated in necrotic fibers from mdx dystrophic mice. J. Biol. Chem. 270:1995;10909-10914.
32. 2+ ions. J. Biochem. 90:1981;275-278.
33. Suzuki K., Imajoh S., Emori Y., Kawasaki H., Minami Y., Ohno S. Calcium-activated neutral protease and its endogenous inhibitor. Activation at the cell membrane and biological function. FEBS Lett. 220:1987;271-277.
34. Tsujinaka T., Fujita J., Ebisui C.et al. Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice. J. Clin. Invest. 97:1996;244-249.
35. Ueyama H., Kumamoto T., Mizobe T., Mita S., Ando M., Tsuda T. Abnormal distribution of myofibrillar proteins and proteases in cytoplasmic body myopathy. Acta Cardiomiol. 7:1995;67-71.