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'''Calpain small subunit 1''', also known as '''CAPN4''', is a [[protein]] that in humans is encoded by the ''CAPNS1'' [[gene]].<ref name="pmid3024120">{{cite journal | vauthors = Miyake S, Emori Y, Suzuki K | title = Gene organization of the small subunit of human calcium-activated neutral protease | journal = Nucleic Acids | '''Calpain small subunit 1''', also known as '''CAPN4''', is a [[protein]] that in humans is encoded by the ''CAPNS1'' [[gene]].<ref name="pmid3024120">{{cite journal | vauthors = Miyake S, Emori Y, Suzuki K | title = Gene organization of the small subunit of human calcium-activated neutral protease | journal = Nucleic Acids Research | volume = 14 | issue = 22 | pages = 8805–17 | date = November 1986 | pmid = 3024120 | pmc = 311912 | doi = 10.1093/nar/14.22.8805 }}</ref><ref name="pmid3016651">{{cite journal | vauthors = Ohno S, Emori Y, Suzuki K | title = Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease | journal = Nucleic Acids Research | volume = 14 | issue = 13 | pages = 5559 | date = July 1986 | pmid = 3016651 | pmc = 311560 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CAPNS1 calpain, small subunit 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=826| access-date = }}</ref> | ||
== Function == | |||
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. The small regulatory subunit consists of an N-terminal domain, containing about 30% glycine residues and a C-terminal Ca-binding domain.<ref name="pmid9228946">{{cite journal | vauthors = Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, Hatanaka M, DeLucas LJ, Narayana SV | title = Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding | journal = Nature Structural Biology | volume = 4 | issue = 7 | pages = 539–47 | date = July 1997 | pmid = 9228946 | doi = }}</ref> Two transcript variants encoding the same protein have been identified for this gene.<ref name="entrez" /> | |||
==Functions== | ==Functions== | ||
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Elevated expression of Capn4 has been found to be associated with progression of various cancers such as hepatocellular and [[renal carcinoma]]. | Elevated expression of Capn4 has been found to be associated with progression of various cancers such as hepatocellular and [[renal carcinoma]]. | ||
<ref name=" pmid = 24514433 ">{{cite journal | | <ref name=" pmid = 24514433 ">{{cite journal | vauthors = Zhuang Q, Qian X, Cao Y, Fan M, Xu X, He X | title = Capn4 mRNA level is correlated with tumour progression and clinical outcome in clear cell renal cell carcinoma | journal = The Journal of International Medical Research | volume = 42 | issue = 2 | pages = 282–91 | date = April 2014 | pmid = 24514433 | doi = 10.1177/0300060513505524 }}</ref> | ||
==References== | == References == | ||
{{reflist}} | {{reflist}} | ||
==External links== | == External links == | ||
* {{UCSC gene info|CAPNS1}} | * {{UCSC gene info|CAPNS1}} | ||
==Further reading== | == Further reading == | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
* {{cite journal | vauthors = Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S | title = Calpain: novel family members, activation, and physiologic function | journal = Biological Chemistry Hoppe-Seyler | volume = 376 | issue = 9 | pages = 523–9 | date = September 1995 | pmid = 8561910 | doi = }} | |||
* {{cite journal | vauthors = Tidball JG, Spencer MJ | title = Calpains and muscular dystrophies | journal = The International Journal of Biochemistry & Cell Biology | volume = 32 | issue = 1 | pages = 1–5 | date = January 2000 | pmid = 10661889 | doi = 10.1016/S1357-2725(99)00095-3 }} | |||
*{{cite journal | * {{cite journal | vauthors = Huang Y, Wang KK | title = The calpain family and human disease | journal = Trends in Molecular Medicine | volume = 7 | issue = 8 | pages = 355–62 | date = August 2001 | pmid = 11516996 | doi = 10.1016/S1471-4914(01)02049-4 }} | ||
*{{cite journal | * {{cite journal | vauthors = Reverter D, Sorimachi H, Bode W | title = The structure of calcium-free human m-calpain: implications for calcium activation and function | journal = Trends in Cardiovascular Medicine | volume = 11 | issue = 6 | pages = 222–9 | date = August 2001 | pmid = 11673052 | doi = 10.1016/S1050-1738(01)00112-8 }} | ||
*{{cite journal | * {{cite journal | vauthors = Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL | title = Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP | journal = Journal of Neuroscience Research | volume = 29 | issue = 3 | pages = 346–54 | date = July 1991 | pmid = 1656060 | doi = 10.1002/jnr.490290310 }} | ||
*{{cite journal | * {{cite journal | vauthors = Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K | title = Four genes for the calpain family locate on four distinct human chromosomes | journal = Cytogenetics and Cell Genetics | volume = 53 | issue = 4 | pages = 225–9 | year = 1990 | pmid = 2209092 | doi = 10.1159/000132937 }} | ||
*{{cite journal | * {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–13 | date = April 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }} | ||
*{{cite journal | * {{cite journal | vauthors = Zhang W, Lane RD, Mellgren RL | title = The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells | journal = The Journal of Biological Chemistry | volume = 271 | issue = 31 | pages = 18825–30 | date = August 1996 | pmid = 8702541 | doi = 10.1074/jbc.271.31.18825 }} | ||
*{{cite journal | * {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Research | volume = 7 | issue = 4 | pages = 353–8 | date = April 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }} | ||
*{{cite journal | * {{cite journal | vauthors = Noguchi M, Sarin A, Aman MJ, Nakajima H, Shores EW, Henkart PA, Leonard WJ | title = Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 21 | pages = 11534–9 | date = October 1997 | pmid = 9326644 | pmc = 23528 | doi = 10.1073/pnas.94.21.11534 }} | ||
*{{cite journal | * {{cite journal | vauthors = Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W | title = The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 2 | pages = 588–92 | date = January 2000 | pmid = 10639123 | pmc = 15374 | doi = 10.1073/pnas.97.2.588 }} | ||
*{{cite journal | * {{cite journal | vauthors = Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S | title = Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain | journal = Acta Crystallographica Section D | volume = 56 | issue = Pt 1 | pages = 73–5 | date = January 2000 | pmid = 10666632 | doi = 10.1107/S0907444999013748 }} | ||
*{{cite journal | * {{cite journal | vauthors = Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ | title = Shotgun sequencing of the human transcriptome with ORF expressed sequence tags | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 7 | pages = 3491–6 | date = March 2000 | pmid = 10737800 | pmc = 16267 | doi = 10.1073/pnas.97.7.3491 }} | ||
*{{cite journal | * {{cite journal | vauthors = Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W | title = Structural basis for possible calcium-induced activation mechanisms of calpains | journal = Biological Chemistry | volume = 382 | issue = 5 | pages = 753–66 | date = May 2001 | pmid = 11517928 | doi = 10.1515/BC.2001.091 }} | ||
*{{cite journal | |||
*{{cite journal | |||
}} | |||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=826}} | {{PDB Gallery|geneid=826}} | ||
{{Cysteine proteases}} | {{Cysteine proteases}} | ||
Latest revision as of 03:55, 4 December 2018
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Calpain small subunit 1, also known as CAPN4, is a protein that in humans is encoded by the CAPNS1 gene.[1][2][3]
Function
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. The small regulatory subunit consists of an N-terminal domain, containing about 30% glycine residues and a C-terminal Ca-binding domain.[4] Two transcript variants encoding the same protein have been identified for this gene.[3]
Functions
Myotonic dystrophy
This gene encodes a small subunit common to both calpain I and II and is associated with myotonic dystrophy.[3]
Biomarker
Elevated expression of Capn4 has been found to be associated with progression of various cancers such as hepatocellular and renal carcinoma. [5]
References
- ↑ Miyake S, Emori Y, Suzuki K (November 1986). "Gene organization of the small subunit of human calcium-activated neutral protease". Nucleic Acids Research. 14 (22): 8805–17. doi:10.1093/nar/14.22.8805. PMC 311912. PMID 3024120.
- ↑ Ohno S, Emori Y, Suzuki K (July 1986). "Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease". Nucleic Acids Research. 14 (13): 5559. PMC 311560. PMID 3016651.
- ↑ 3.0 3.1 3.2 "Entrez Gene: CAPNS1 calpain, small subunit 1".
- ↑ Lin GD, Chattopadhyay D, Maki M, Wang KK, Carson M, Jin L, Yuen PW, Takano E, Hatanaka M, DeLucas LJ, Narayana SV (July 1997). "Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding". Nature Structural Biology. 4 (7): 539–47. PMID 9228946.
- ↑ Zhuang Q, Qian X, Cao Y, Fan M, Xu X, He X (April 2014). "Capn4 mRNA level is correlated with tumour progression and clinical outcome in clear cell renal cell carcinoma". The Journal of International Medical Research. 42 (2): 282–91. doi:10.1177/0300060513505524. PMID 24514433.
External links
- Human CAPNS1 genome location and CAPNS1 gene details page in the UCSC Genome Browser.
Further reading
- Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (September 1995). "Calpain: novel family members, activation, and physiologic function". Biological Chemistry Hoppe-Seyler. 376 (9): 523–9. PMID 8561910.
- Tidball JG, Spencer MJ (January 2000). "Calpains and muscular dystrophies". The International Journal of Biochemistry & Cell Biology. 32 (1): 1–5. doi:10.1016/S1357-2725(99)00095-3. PMID 10661889.
- Huang Y, Wang KK (August 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 (August 2001). "The structure of calcium-free human m-calpain: implications for calcium activation and function". Trends in Cardiovascular Medicine. 11 (6): 222–9. doi:10.1016/S1050-1738(01)00112-8. PMID 11673052.
- Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL (July 1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP". Journal of Neuroscience Research. 29 (3): 346–54. doi:10.1002/jnr.490290310. PMID 1656060.
- Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenetics and Cell Genetics. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092.
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Zhang W, Lane RD, Mellgren RL (August 1996). "The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells". The Journal of Biological Chemistry. 271 (31): 18825–30. doi:10.1074/jbc.271.31.18825. PMID 8702541.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Noguchi M, Sarin A, Aman MJ, Nakajima H, Shores EW, Henkart PA, Leonard WJ (October 1997). "Functional cleavage of the common cytokine receptor gamma chain (gammac) by calpain". Proceedings of the National Academy of Sciences of the United States of America. 94 (21): 11534–9. doi:10.1073/pnas.94.21.11534. PMC 23528. PMID 9326644.
- Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W (January 2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium". Proceedings of the National Academy of Sciences of the United States of America. 97 (2): 588–92. doi:10.1073/pnas.97.2.588. PMC 15374. PMID 10639123.
- Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S (January 2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain". Acta Crystallographica Section D. 56 (Pt 1): 73–5. doi:10.1107/S0907444999013748. PMID 10666632.
- Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (March 2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proceedings of the National Academy of Sciences of the United States of America. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
- Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W (May 2001). "Structural basis for possible calcium-induced activation mechanisms of calpains". Biological Chemistry. 382 (5): 753–66. doi:10.1515/BC.2001.091. PMID 11517928.
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