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

Homo sapiens

Synonyms: CANP, CANP 1, CANP1, CANPL1, Calcium-activated neutral proteinase 1, ...
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


Psychiatry related information on CAPN1


High impact information on CAPN1

  • We have cloned a human cDNA that encodes a factor that binds to the GC-rich sequences present in the epidermal growth factor receptor (EGFR), beta-actin, and calcium-dependent protease (CANP) promoters [7].
  • We used single sarcomeres from which the Z-lines, structures which anchor the thin filaments in the sarcomere, had been completely removed by calcium-activated neutral protease (CANP) and trypsin, and measured both the sliding velocity of single actin filaments along myosin filaments and the ATPase activity during sliding [8].
  • Glycoprotein (GP) Ib was purified from lysates of human platelets prepared in the presence or absence of inhibitors of the endogenous calcium-activated neutral protease (CANP) by immunoaffinity chromatography, employing the GPIb-specific murine monoclonal antibody, AP1, coupled to Sepharose CL4B [9].
  • Thus, proteases have been implicated in myelin protein degradation, and recent studies have demonstrated increased expression and activity of a calcium-activated neutral proteinase (calpain) in experimental allergic encephalomyelitis, the corresponding animal model of MS [10].
  • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration [11].

Chemical compound and disease context of CAPN1

  • Melanoma cells resistant to gamma-IFN excrete calcium activated neutral protease (CANP) and as a consequence, make L-tryptophan available by the hydrolysis of serum proteins in the culture medium [12].
  • Furthermore, the inhibitors against CANP, NCO-700 (2 and 20 micrograms/ml) that was demonstrated to permeate sarcolemma using 14C-labelled reagent, against CDP, mepacrine (1 and 10 micrograms/ml) or against cyclooxygenase, indomethacin (1 and 10 micrograms/ml) caused no effect on the Ca entry, nigrosin intake nor CPK release under hypoxia [13].

Biological context of CAPN1


Anatomical context of CAPN1


Associations of CAPN1 with chemical compounds


Enzymatic interactions of CAPN1


Regulatory relationships of CAPN1


Other interactions of CAPN1

  • However, our results do not allow conclusions on the function of CAPN1 and CAPN2 in BCCs and SCCs [1].
  • Mapping studies of the gene encoding mu-calpain (CAPN1) located CAPN1 to 11q13 and in the vicinity of the MEN1 locus [24].
  • The purified mu CANP is a thiol proteinase and requires calcium for activity [25].

Analytical, diagnostic and therapeutic context of CAPN1

  • Interestingly, CAPN1 immunoreactivity (streptavidin-peroxidase technique) was markedly reduced in BCCs compared to normal human skin or SCCs, while in contrast CAPN1 mRNA levels (determined by real-time PCR) were markedly elevated in BCCs and SCCs compared to normal human skin [1].
  • To resolve conflicting reports on the localization of mCANP based on activity measurements, we developed an immunoassay for CANP and compared the content and activity of the molecule in soluble and membrane fractions of mouse and human brain [18].
  • The major active form of CANP exhibited a molecular weight of 94-100 kilodaltons (Kd) by gel filtration on Sephacryl 300 and consisted of 78-Kd and 27-Kd subunits [4].
  • More than 95% of the total immunoreactive mCANP remained in the soluble fraction after 15,000 g centrifugation of the whole homogenate. mCANP activity was determined with [14C]azocasein as substrate after removing endogenous CANP inhibitor(s) by ion-exchange chromatography on DEAE-cellulose [18].
  • The cytotoxicity of an endogenous inhibitor of calcium-activated neutral proteinase (CANP-I) was evaluated using various mammalian tumor-derived cell lines and human cell cultures [26].


  1. Different expression patterns of calpain isozymes 1 and 2 (CAPN1 and 2) in squamous cell carcinomas (SCC) and basal cell carcinomas (BCC) of human skin. Reichrath, J., Welter, C., Mitschele, T., Classen, U., Meineke, V., Tilgen, W., Seifert, M. J. Pathol. (2003) [Pubmed]
  2. A 500-kb sequence-ready cosmid contig and transcript map of the MEN1 region on 11q13. Bergman, L., Silins, G., Grimmond, S., Hummerich, H., Stewart, C., Little, P., Hayward, N. Genomics (1999) [Pubmed]
  3. Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit. Vilei, E.M., Calderara, S., Anagli, J., Berardi, S., Hitomi, K., Maki, M., Carafoli, E. J. Biol. Chem. (1997) [Pubmed]
  4. Calcium-activated neutral proteinase of human brain: subunit structure and enzymatic properties of multiple molecular forms. Vitto, A., Nixon, R.A. J. Neurochem. (1986) [Pubmed]
  5. Hydrolytic and autolytic behavior of two forms of calcium-activated neutral protease (CANP). Inomata, M., Hayashi, M., Nakamura, M., Imahori, K., Kawashima, S. J. Biochem. (1985) [Pubmed]
  6. Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease. Nixon, R.A., Saito, K.I., Grynspan, F., Griffin, W.R., Katayama, S., Honda, T., Mohan, P.S., Shea, T.B., Beermann, M. Ann. N. Y. Acad. Sci. (1994) [Pubmed]
  7. Molecular cloning and characterization of a human DNA binding factor that represses transcription. Kageyama, R., Pastan, I. Cell (1989) [Pubmed]
  8. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Yanagida, T., Arata, T., Oosawa, F. Nature (1985) [Pubmed]
  9. On the association of glycoprotein Ib and actin-binding protein in human platelets. Okita, J.R., Pidard, D., Newman, P.J., Montgomery, R.R., Kunicki, T.J. J. Cell Biol. (1985) [Pubmed]
  10. A putative mechanism of demyelination in multiple sclerosis by a proteolytic enzyme, calpain. Shields, D.C., Schaecher, K.E., Saido, T.C., Banik, N.L. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  11. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Saito, K., Elce, J.S., Hamos, J.E., Nixon, R.A. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  12. Tryptophan protects human melanoma cells against gamma-interferon and tumour necrosis factor-alpha: a unifying mechanism of action. Wood, J.M., Ehrke, C., Schallreuter, K.U. Melanoma Res. (1991) [Pubmed]
  13. Ca overload and the action of calcium sensitive proteases, phospholipases and prostaglandin E2 in myocardial cell degradation. Toyo-oka, T., Hara, K., Nakamura, N., Kitahara, M., Masaki, T. Basic Res. Cardiol. (1985) [Pubmed]
  14. Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily. Matena, K., Boehm, T., Dear, N. Genomics (1998) [Pubmed]
  15. 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]
  16. Characterization of cDNA clones encoding a novel calcium-activated neutral proteinase from Schistosoma mansoni. Andresen, K., Tom, T.D., Strand, M. J. Biol. Chem. (1991) [Pubmed]
  17. Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. Banik, N.L., DeVries, G.H., Neuberger, T., Russell, T., Chakrabarti, A.K., Hogan, E.L. J. Neurosci. Res. (1991) [Pubmed]
  18. Immunoassay and activity of calcium-activated neutral proteinase (mCANP): distribution in soluble and membrane-associated fractions in human and mouse brain. Takeuchi, K.H., Saito, K.I., Nixon, R.A. J. Neurochem. (1992) [Pubmed]
  19. Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human mu CANP and mCANP. Saito, K., Nixon, R.A. Neurochem. Res. (1993) [Pubmed]
  20. Multiple proteases regulate neurite outgrowth in NB2a/dl neuroblastoma cells. Shea, T.B., Beermann, M.L., Nixon, R.A. J. Neurochem. (1991) [Pubmed]
  21. Purification and characterization of Ca2+-activated neutral protease inhibitor from human platelets. Shiba, E., Tsujinaka, T., Kambayashi, J., Kosaki, G. Thromb. Res. (1983) [Pubmed]
  22. Ca(2+)-activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form. Molinari, M., Anagli, J., Carafoli, E. J. Biol. Chem. (1994) [Pubmed]
  23. Phospholipids inhibit proteolysis of protein kinase C alpha by mM calcium-requiring calpain. Lang, D., Beermann, M.L., Hauser, G., Cressman, C.M., Shea, T.B. Neurochem. Res. (1995) [Pubmed]
  24. Genetic mapping studies of 40 loci and 23 cosmids in chromosome 11p13-11q13, and exclusion of mu-calpain as the multiple endocrine neoplasia type 1 gene. Pang, J.T., Lloyd, S.E., Wooding, C., Farren, B., Pottinger, B., Harding, B., Leigh, S.E., Pook, M.A., Benham, F.J., Gillett, G.T., Taggart, R.T., Thakker, R.V. Hum. Genet. (1996) [Pubmed]
  25. A low-calcium-requiring calcium-activated neutral proteinase from human placenta. Shastri, R., Anandaraj, M.P. Biochim. Biophys. Acta (1986) [Pubmed]
  26. The selective anticancer activity of the endogenous inhibitor of calcium-activated neutral proteinase. A histological, cytological and chemosensitivity study. Logothetou-Rella, H. Histol. Histopathol. (1994) [Pubmed]
WikiGenes - Universities