The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CalpA  -  Calpain-A

Drosophila melanogaster

Synonyms: CANP A, CG18152, CG7563, Calcium-activated neutral proteinase A, Dmel\CG7563, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CalpA

  • The analysis of the mechanism of activation in Drosophila calpains seems to corroborate the autolysis model of calpain activation [1].
  • Drosophila calpains. Purification of a calpain-like enzyme from fruit flies, and expression in Escherichia coli [2].

High impact information on CalpA


Biological context of CalpA

  • The sequencing of the fly genome has been recently completed and a novel calpain homologue has been identified in the CG3692 gene product [7].
  • Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila [8].
  • Drosophila calpain has an amino acid sequence highly homologous to those of mammalian calpains and exhibits a distinct domain structure consisting of cysteine protease and calcium-binding domains [8].
  • These results suggest that domain III might be the primary lipid binding site of calpain and may play a decisive role in orchestrating Ca2+- and lipid activation of the enzyme [9].
  • In similar assays, DUK114 was ineffective with Drosophila calpain A or calpain B. To test for its chaperone activity in vivo, DUK114 was transfected into Schneider (S2) cells; after heat shock, the number of viable non-transfected cells started to increase after a lag time; in the presence of DUK114, cell proliferation started at once [10].

Anatomical context of CalpA

  • In the blood cell line mbn-2, calpain is associated with a granular component in the cytoplasm [6].
  • These results indicate that calpain is involved in the dynamic changes in the embryonic cytoskeleton, especially actin-related structures, during early embryogenesis prior to cellularization [8].
  • Co-staining experiments with anti-actin antibody revealed that calpain condenses specifically at the edge of and between actin caps that underlie the plasma membrane immediately above each nucleus [8].

Associations of CalpA with chemical compounds

  • To the various orthologues diverse functions have been ascribed, such as translation inhibition, regulation of purine repressor or calpain activation [10].
  • The decay of protein kinase C activity can be prevented by leupeptin or a crude calpastatin preparation isolated from fly heads, indicating the presence of the Ca2+-dependent neutral protease, calpain, in larval brains [11].
  • Moreover, we show that the genes encoding three other esterase phenotypes also map to the same region; these phenotypes involve allozymic differences in EST 9 (formerly EST C), ali-esterase activity, defined by the hydrolysis of methyl butyrate, and malathion carboxylesterase activity, defined by hydrolysis of the organophosphate malathion [12].

Regulatory relationships of CalpA

  • However, we suggest that single chain, non-heterodimeric calpains may be insensitive to calpastatin and that Drosophila cystatin-like molecules may play a role in negatively regulating Drosophila calpain [13].

Other interactions of CalpA


Analytical, diagnostic and therapeutic context of CalpA


  1. Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB. Jékely, G., Friedrich, P. J. Biol. Chem. (1999) [Pubmed]
  2. Drosophila calpains. Purification of a calpain-like enzyme from fruit flies, and expression in Escherichia coli. Jékely, G., Pintér, M., Friedrich, P. Methods Mol. Biol. (2000) [Pubmed]
  3. Kettin, a large modular protein in the Z-disc of insect muscles. Lakey, A., Labeit, S., Gautel, M., Ferguson, C., Barlow, D.P., Leonard, K., Bullard, B. EMBO J. (1993) [Pubmed]
  4. Signal convergence on protein kinase A as a molecular correlate of learning. Aszódi, A., Müller, U., Friedrich, P., Spatz, H.C. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster. Delaney, S.J., Hayward, D.C., Barleben, F., Fischbach, K.F., Miklos, G.L. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  6. CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. Theopold, U., Pintér, M., Daffre, S., Tryselius, Y., Friedrich, P., Nässel, D.R., Hultmark, D. Mol. Cell. Biol. (1995) [Pubmed]
  7. Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C. Spadoni, C., Farkas, A., Sinka, R., Tompa, P., Friedrich, P. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  8. Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila. Emori, Y., Saigo, K. J. Biol. Chem. (1994) [Pubmed]
  9. Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Tompa, P., Emori, Y., Sorimachi, H., Suzuki, K., Friedrich, P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  10. DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. Farkas, A., Nardai, G., Csermely, P., Tompa, P., Friedrich, P. Biochem. J. (2004) [Pubmed]
  11. Protein kinase C in larval brain of wild-type and dunce memory-mutant Drosophila. Dévay, P., Pintér, M., Kiss, I., Faragó, A., Friedrich, P. J. Neurogenet. (1989) [Pubmed]
  12. A cluster of esterase genes on chromosome 3R of Drosophila melanogaster includes homologues of esterase genes conferring insecticide resistance in Lucilia cuprina. Spackman, M.E., Oakeshott, J.G., Smyth, K.A., Medveczky, K.M., Russell, R.J. Biochem. Genet. (1994) [Pubmed]
  13. A calpain-like activity insensitive to calpastatin in Drosophila melanogaster. Laval, M., Pascal, M. Biochim. Biophys. Acta (2002) [Pubmed]
  14. The calpain-system of Drosophila melanogaster: coming of age. Friedrich, P., Tompa, P., Farkas, A. Bioessays (2004) [Pubmed]
  15. Troponin of asynchronous flight muscle. Bullard, B., Leonard, K., Larkins, A., Butcher, G., Karlik, C., Fyrberg, E. J. Mol. Biol. (1988) [Pubmed]
  16. Assembly of the giant protein projectin during myofibrillogenesis in Drosophila indirect flight muscles. Ayme-Southgate, A., Bounaix, C., Riebe, T.E., Southgate, R. BMC Cell Biol. (2004) [Pubmed]
  17. On the sequential determinants of calpain cleavage. Tompa, P., Buzder-Lantos, P., Tantos, A., Farkas, A., Szilágyi, A., Bánóczi, Z., Hudecz, F., Friedrich, P. J. Biol. Chem. (2004) [Pubmed]
WikiGenes - Universities