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

CAPN1  -  calpain 1, (mu/I) large subunit

Gallus gallus

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 CAPN1

  • Various lines of evidence suggest that calcium dependent protease (CANP, calpain) exists in the cytosol as an inactive proenzyme which is converted to an active form by autolysis [1].

High impact information on CAPN1


Biological context of CAPN1

  • The amino acid sequence shows 66% and 86% identity with the mouse and zebrafish Capn1, respectively [7].
  • The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined [4].
  • Fifteen hybridomas secreting antibodies against calcium-activated neutral protease (CANP), especially those for rabbit muscle mCANP with low calcium sensitivity, have been produced by the cell fusion technique [8].

Anatomical context of CAPN1

  • Localization of calcium-activated neutral protease (CANP) in the peripheral nerve [9].
  • This study shows that the loss of perifused chick pineal gland activity is a complex process which seems to involve the release of calcium from intracellular stores, calmodulin and calcium-activated neutral protease (CANP) [5].
  • Analyses of the autocatalytic activation of CANP in the presence of plasma membranes reveal that proCANP translocates to the membrane in the presence of microM Ca2+ and is activated at the membrane [1].
  • CANP was demonstrated in the axon, but not in the myelin sheath or endoneurium [9].
  • The amount of CANP bound to myofibrils was approximately 4 percent of that contained in the whole muscle homogenate [10].

Associations of CAPN1 with chemical compounds


Analytical, diagnostic and therapeutic context of CAPN1

  • Starvation of rainbow trout fingerlings (15-20 g) for 35 days stimulated the expression of Capn1 (2.2-fold increase, P < 0.01), Capn2 (6.0-fold increase, P < 0.01), and calpastatins (1.6-fold increase, P < 0.05) as measured by quantitative real-time RT-PCR [7].
  • Its specificity to CANP, as well as its cross-reactivity with rat CANP, were confirmed by the Ouchterlony immunodiffusion procedure and immunoreplica method [9].
  • To clarify the mechanism of activation of calcium activated neutral protease (CANP, or mCANP: active at mM Ca2+), the structure of mCANP was examined by measuring CD spectra and by titration of SH groups in the presence of Mn2+ [11].


  1. Regulation of activity of calcium activated neutral protease. Suzuki, K., Imajoh, S., Emori, Y., Kawasaki, H., Minami, Y., Ohno, S. Adv. Enzyme Regul. (1988) [Pubmed]
  2. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. Sorimachi, H., Imajoh-Ohmi, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y., Suzuki, K. J. Biol. Chem. (1989) [Pubmed]
  3. Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Imajoh, S., Aoki, K., Ohno, S., Emori, Y., Kawasaki, H., Sugihara, H., Suzuki, K. Biochemistry (1988) [Pubmed]
  4. Amino acid sequence around the active site cysteine residue of calcium-activated neutral protease (CANP). Suzuki, K., Hayashi, H., Hayashi, T., Iwai, K. FEBS Lett. (1983) [Pubmed]
  5. Effects of ethylene glycol tetraacetic acid, A23187 and calmodulin, calcium activated neutral proteinase antagonists on melatonin secretion in perifused chick pineal gland. Agapito, M.T., Pablos, M., Reiter, R.J., Recio, J.M., Gutierrez-Baraja, R. Neurosci. Lett. (1998) [Pubmed]
  6. Protease activity in brain, nerve, and muscle of hens given neuropathy-inducing organophosphates and a calcium channel blocker. el-Fawal, H.A., Correll, L., Gay, L., Ehrich, M. Toxicol. Appl. Pharmacol. (1990) [Pubmed]
  7. Identification and molecular characterization of the rainbow trout calpains (Capn1 and Capn2): their expression in muscle wasting during starvation. Salem, M., Nath, J., Rexroad, C.E., Killefer, J., Yao, J. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2005) [Pubmed]
  8. Isolation and characterization of monoclonal antibodies against calcium-activated neutral protease with low calcium sensitivity. Kasai, Y., Inomata, M., Hayashi, M., Imahori, K., Kawashima, S. J. Biochem. (1986) [Pubmed]
  9. Localization of calcium-activated neutral protease (CANP) in the peripheral nerve. Kamakura, K., Ishiura, S., Fujita, T., Nonaka, I., Sugita, H. Muscle Nerve (1985) [Pubmed]
  10. Calcium-activated neutral protease. Its localization in the myofibril, especially at the Z-band. Ishiura, S., Sugita, H., Nonaka, I., Imahori, K. J. Biochem. (1980) [Pubmed]
  11. Effect of metal ions on the structure and activity of calcium-activated neutral protease (CANP). Suzuki, K., Ishiura, S. J. Biochem. (1983) [Pubmed]
WikiGenes - Universities