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

Biological Chemistry

Volumn 379, Issue 2, 1998, Pages 175-183

  Lee, Hahn Jun ^a   Sorimachi, Hiroyuki ^a   Jeong, Seon Yong ^a   Ishiura, Shoichi ^a   Suzuki, Koichi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Calpain; Chromosome 1; Cysteine protease; Digestive tract; EF hand; nCL 4

Indexed keywords

CALCIUM BINDING PROTEIN; CALPAIN; COMPLEMENTARY DNA;

ARTICLE; CHROMOSOME 1; DIGESTIVE SYSTEM; ENZYME SUBUNIT; EXON; HUMAN; MOLECULAR CLONING; MOUSE; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; TISSUE SPECIFICITY;

MAMMALIA; RODENTIA;

EID: 0031883959     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.2.175     Document Type: Article

References (33)

1. Andresen, K., Tom, T.D., and Strand, M. (1991). Characterization of cDNA clones encoding a novel calcium-activated neutral protease from Schistosome mansoni. J. Biol. Chem. 265, 15085-15090.
2. Ausubel, F.M., Brent, R., Kingstone, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (1987). Current Protocols in Molecular Biology, (New York: Grenee Publishing Associates and Wiley-Interscience).
3. 2+-induced conformational changes. Nature Structural Biology 4, 532-538.
4. Chu, G., Hayagawa, H., and Berg, R (1987). Electroporation for the efficient mammalian cells with DNA. Nucleic Acids Res. 75, 1311-1326.
5. Crawford, C. (1990). Protein and peptide inhibitors of calpains. In: Intracellular Calcium Dependent Proteolysis, R.L. Mellgren and T. Murachi, eds. (Boca Raton, FL, USA: CRC Press).
6. Croall, D.E., and DeMartino, G.N. (1991). Calcium-activated neutral protease (calpain) system; structure, function, and regulation. Physiol. Rev. 71, 813-847.
7. Delany, S.J., Hayward, D.C., Barleben, F., Fischbach, K.F., and Miklos, G.L.G. (1991). Molecular cloning and analysis of small obtic lobes, a structural brain gene of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 88, 7214-7218.
8. Denison, S.H., Orejas, M., and Arst, H.N. (1995). Signaling of ambient pH in aspergillus involves a cysteine protease. J. Biol. Chem. 270, 28519-28522.
9. Emori, Y, Ohno, S., Tobita, M., and Suzuki, K. (1986). Gene structure of calcium-dependent protease retains the ancestral organization of the calcium-binding protein gene. FEBS Lett. 794, 249-252.
10. Emori, Y., and Saigo, K. (1994). Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. J. Biol. Chem. 269, 25137-25142.
11. 2+-dependent proteinase system. In: Intracellular Calcium-dependent Proteolysis, R.L. Mellgren and T. Murachi, eds. (Boca Raton, FL, USA: CRC Press), pp. 3-24.
12. Kozak, M. (1984). Compilation and analysis of sequences from the translational start site in eukaryotic mRNAs. Nucleic Acid Res. 12, 857-872.
13. Lerner, R.A., Green, N., Alexander, H., Liu, F.-T., Sutcliffe, J.G., and Shinnick, T.M. (1981). Chemically synthesized peptides prepared from the nucleotide sequence of the hepatitis B virus genome elicit antibodies reactive with the native envelope protein of dane particle. Proc. Natl. Acad. Sci. USA 78, 3403-3407.
14. Lin, G.-D., Chattopadhyay, D., Maki, M., Wang, K.K.W., Carson, M., Jin, L., Yuen, P.-W., Takano, E., Hatanaka, M., Delucas, L.J., and Narayana, S.V.L. (1997). Crystal structure of calcium bound domain VI of calpain at 1.9 A. U. resolution and its role in enzyme resembly, regulation, and inhibitor binding Nature Structural Biology 4, 539-547.
15. Maki, M., Hatanaka, M., Takano, E., and Murachi, T. (1990). Structure-function relationship of calpastatins. In: Intracellular Calcium Dependent Proteolysis (R.L. Mellgren and T. Murachi, eds. (Boca Raton, FL, USA: CRC Press), pp. 37-54.
16. Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M., and Suzuki, K. (1984). Evolutionary orign of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium binding-protein?, Nature 312, 566-570.
17. 2+-activated thiol protease from Drosophila melanogaster. Biochemistry 31, 8201-8206.
18. Richard, I., Broux, O., Allamand, V., Fougerousse, F., Chiannilkulchai, N., Bourg, N., Brenguier, L., Devaud, C., Pasturaud, P., Roudaut, C., Hillare, D., Passos-Bueno, M.-R., Zata, M., Tischfield, J.A., Fardeau, M., Jackson, C.E., Cohen, D., and Beckman, J.S. (1995). Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 81, 27-40.
19. Saido, T.C., Sorimachi, H., and Suzuki, K. (1994). Calpain: new perspective in molecular diversity and physiological-pathological involvement, FASEB J. 8, 814-821.
20. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed. (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press).
21. Sorimachi, H., and Suzuki, K. (1992). Sequence comparison among muscle specific calpain, p94, and calpain subunit. Biochim. Biophys. Acta. 1160, 55-62.
22. Sorimachi, H., Imajoh-Ohmi, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y., and Suzuki, K. (1989). Molecular cloning of a novel mammalian calcium-dependent protease distinct from both μ- and m-types. J. Biol. Chem. 264, 20106-20111.
23. Sorimachi, H., Tsukahara, T., Kawasaki, H., Ishiura, S., Emori, Y., Sugita, H., and Suzuki, K. (1990). Molecular cloning of cDNAs for two subunits of rat multicatalytic proteinase; existence of N-terminal conserved and C-terminal diverged sequence. Eur. J. Biochem. 193, 775-781.
24. Sorimachi, H., Toyama-Sorimachi, N., Saido, T.C., Kawasaki, H., Sugita, H., Miyasaka, M., Arahata, K., Ishiura, S., and Suzuki, K. (1993a). Muscle specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J. Biol. Chem. 268, 10593-10605.
25. 2+-binding domain. J. Biol. Chem. 268, 19476-19482.
26. Sorimachi, H., Saido, T.C., and Suzuki, K. (1994). New era of calpain research, FEBS Lett. 343, 1-5.
27. Sorimachi, H., Kinbara, K., Kimura, S., Takahashi, M., Ishiura, S., Sasagawa, N., Shimada, H., Tagawa, K., Maruyama, K., and Suzuki, K. (1995). Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94 specific sequence. J. Biol. Chem. 270, 31158-31162.
28. Sorimachi, H., Forsberg, N.E., Lee, H.-J., Jeong, S.-Y., Richard, I., Beckmann, J.S., Ishiura, S., and Suzuki, K. (1996). Highly conserved structure in the promoter region of the gene for muscle-specific calpain. Biol. Chem. Hoppe-Seyler 377, 859-864.
29. Suzuki, K., Sorimachi, H., Yosizawa, T., Kinbara, K., and Ishiura, S. (1995). Calpain; novel family members, activation, and physiological function, Biol. Chem. Hoppe-Seyler 376, 523-529.
30. Theopold, U., Pinter, M., Daffre, S., Tryselius, Y., Friedrich, P., Naessl, D.R., and Hultmark, D. (1995). CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. Mol. Cell. Biol. 15, 824-834.
31. Tufty, R.H., and Kretsinger, R.H. (1975). Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 187, 167-169.
32. Waterston, R., Martini, C., Craxton, M., Huynh, C., Coulson, A., Hillier, L., Durbin, R., Green, P., Shownkeen, R., Halloran, N., Metzstein, M., Hawkins, T., Wilson, R., Berks, M., Du, Z., Thomas, K., Thierry-Mieg, J., and Sulston, J. (1992). A survey of expressed genes in Caenorhabditis elegans. Nature Genetics 1, 114-123.
33. Wilson, R., Ainscough, R., et al. (1994). 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 360, 32-38.