CAPNS1: Information from Answers.com

Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases. Calpain families have been implicated in neurodegenerative processes, as their activation can be triggered by calcium influx and oxidative stress. Calpain I and II are heterodimeric with distinct large subunits associated with common small subunits, all of which are encoded by different genes. This gene encodes a small subunit common to both calpain I and II and is associated with myotonic dystrophy. Two transcript variants encoding the same protein have been identified for this gene.^[3]

References

^ Miyake S, Emori Y, Suzuki K (Jan 1987). "Gene organization of the small subunit of human calcium-activated neutral protease". Nucleic Acids Res 14 (22): 8805-17. PMID 3024120.
^ Ohno S, Emori Y, Suzuki K (Sep 1986). "Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease". Nucleic Acids Res 14 (13): 5559. PMID 3016651.
^ ^a ^b "Entrez Gene: CAPNS1 calpain, small subunit 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=826.

Suzuki K, Sorimachi H, Yoshizawa T, et al. (1996). "Calpain: novel family members, activation, and physiologic function.". Biol. Chem. Hoppe-Seyler 376 (9): 523–9. PMID 8561910.
Tidball JG, Spencer MJ (2000). "Calpains and muscular dystrophies.". Int. J. Biochem. Cell Biol. 32 (1): 1–5. doi:10.1016/S1357-2725(99)00095-3. PMID 10661889.
Huang Y, Wang KK (2001). "The calpain family and human disease.". Trends in molecular medicine 7 (8): 355–62. doi:10.1016/S1471-4914(01)02049-4. PMID 11516996.
Reverter D, Sorimachi H, Bode W (2001). "The structure of calcium-free human m-calpain: implications for calcium activation and function.". Trends Cardiovasc. Med. 11 (6): 222–9. doi:10.1016/S1050-1738(01)00112-8. PMID 11673052.
Banik NL, DeVries GH, Neuberger T, et al. (1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP.". J. Neurosci. Res. 29 (3): 346–54. doi:10.1002/jnr.490290310. PMID 1656060.
Ohno S, Minoshima S, Kudoh J, et al. (1990). "Four genes for the calpain family locate on four distinct human chromosomes.". Cytogenet. Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Zhang W, Lane RD, Mellgren RL (1996). "The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells.". J. Biol. Chem. 271 (31): 18825–30. doi:10.1074/jbc.271.31.18825. PMID 8702541.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Noguchi M, Sarin A, Aman MJ, et al. (1997). "Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain.". Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11534–9. doi:10.1073/pnas.94.21.11534. PMID 9326644.
Strobl S, Fernandez-Catalan C, Braun M, et al. (2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 588–92. doi:10.1073/pnas.97.2.588. PMID 10639123.
Masumoto H, Nakagawa K, Irie S, et al. (2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain.". Acta Crystallogr. D Biol. Crystallogr. 56 (Pt 1): 73–5. doi:10.1107/S0907444999013748. PMID 10666632.
Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMID 10737800.
Reverter D, Strobl S, Fernandez-Catalan C, et al. (2002). "Structural basis for possible calcium-induced activation mechanisms of calpains.". Biol. Chem. 382 (5): 753–66. doi:10.1515/BC.2001.091. PMID 11517928.

PDB Gallery

1aj5: CALPAIN DOMAIN VI APO

1alv: CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN

1alw: INHIBITOR AND CALCIUM BOUND DOMAIN VI OF PORCINE CALPAIN

1df0: CRYSTAL STRUCTURE OF M-CALPAIN

1dvi: CALPAIN DOMAIN VI WITH CALCIUM BOUND

1kfu: Crystal Structure of Human m-Calpain Form II

1kfx: Crystal Structure of Human m-Calpain Form I

1np8: 18-k C-terminally trunucated small subunit of calpain

1nx0: Structure of Calpain Domain 6 in Complex with Calpastatin DIC

1nx1: Calpain Domain VI Complexed with Calpastatin Inhibitory Domain C (DIC)

1nx2: Calpain Domain VI

1nx3: Calpain Domain VI in Complex with the Inhibitor PD150606

1u5i: Crystal Structure analysis of rat m-calpain mutant Lys10 Thr

This article on a gene on chromosome 19 is a stub. You can help Wikipedia by expanding it.

v • d • e Proteases: cysteine proteases (EC 3.4.22)

Caspase	Caspase 1 · Caspase 2 · Caspase 3 · Caspase 4 · Caspase 5 · Caspase 6 · Caspase 7 · Caspase 8 · Caspase 9 · Caspase 10 · Caspase 12 · Caspase 13 · Caspase 14

Fruit-derived	Papain · Ficain · Bromelain · Actinidain

Calpain	CAPN1 · CAPN2 · CAPN3 · CAPN5 · CAPN6 · CAPN7 · CAPN8 · CAPN9 · CAPN10 · CAPN11 · CAPN12 · CAPN13 · CAPN14 · CAPNS1 · CAPNS2

Cathepsin	B · C · F · H · K · L1/L2 · S · W · Z

Other	Clostripain · Cancer procoagulant · Separase · Autophagin · Cruzipain

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CAPNS1

References

Further reading