Calpastatin: Difference between revisions

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{{Infobox_gene}}
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'''Calpastatin''' is a [[protein]] that in humans is encoded by the ''CAST'' [[gene]].<ref name="pmid8340353">{{cite journal | vauthors = Ma H, Yang HQ, Takano E, Lee WJ, Hatanaka M, Maki M | title = Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains | journal = J Biochem | volume = 113 | issue = 5 | pages = 591–9 |date=Sep 1993 | pmid = 8340353 | pmc =  | doi =  }}</ref><ref name="pmid14685690">{{cite journal | vauthors = Averna M, De Tullio R, Capini P, Salamino F, Pontremoli S, Melloni E | title = Changes in calpastatin localization and expression during calpain activation: a new mechanism for the regulation of intracellular Ca(2+)-dependent proteolysis | journal = Cell Mol Life Sci | volume = 60 | issue = 12 | pages = 2669–78 |date=Dec 2003 | pmid = 14685690 | pmc =  | doi = 10.1007/s00018-003-3288-0 }}</ref><ref name="pmid15820218">{{cite journal | vauthors = Raynaud P, Jayat-Vignoles C, Laforet MP, Leveziel H, Amarger V | title = Four promoters direct expression of the calpastatin gene | journal = Arch Biochem Biophys | volume = 437 | issue = 1 | pages = 69–77 |date=Apr 2005 | pmid = 15820218 | pmc = | doi = 10.1016/j.abb.2005.02.026 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CAST calpastatin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=831| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Calpastatin
| HGNCid = 1515
| Symbol = CAST
| AltSymbols =; BS-17; MGC9402
| OMIM = 114090
| ECnumber =
  | Homologene = 7658
  | MGIid = 1098236
| GeneAtlas_image1 = PBB_GE_CAST_212586_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAST_207467_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CAST_208908_s_at_tn.png
| Function = {{GNF_GO|id=GO:0030161 |text = calpain inhibitor activity}}
| Component =  
| Process =  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 831
    | Hs_Ensembl = ENSG00000153113
    | Hs_RefseqProtein = NP_001035905
    | Hs_RefseqmRNA = NM_001042440
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 96023533
    | Hs_GenLoc_end = 96136143
    | Hs_Uniprot = P20810
    | Mm_EntrezGene = 12380
    | Mm_Ensembl = ENSMUSG00000021585
    | Mm_RefseqmRNA = XM_990139
    | Mm_RefseqProtein = XP_995233
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 75160288
    | Mm_GenLoc_end = 75274762
    | Mm_Uniprot = Q3TTN2
  }}
}}
'''Calpastatin''', also known as '''CAST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAST calpastatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=831| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein. The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CAST calpastatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=831| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is an endogenous [[calpain]] (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein.{{citation needed|date=August 2018}} The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=LI27.001 LI27.001]
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Murachi T |title=Intracellular regulatory system involving calpain and calpastatin. |journal=Biochem. Int. |volume=18 |issue= 2 |pages= 263-94 |year= 1989 |pmid= 2548504 |doi=  }}
*{{cite journal  | author=Murachi T |title=Intracellular regulatory system involving calpain and calpastatin. |journal=Biochem. Int. |volume=18 |issue= 2 |pages= 263–94 |year= 1989 |pmid= 2548504 |doi=  }}
*{{cite journal  | author=Lee WJ, Ma H, Takano E, ''et al.'' |title=Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8437-42 |year= 1992 |pmid= 1569094 |doi=  }}
*{{cite journal  | vauthors=Lee WJ, Ma H, Takano E |title=Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8437–42 |year= 1992 |pmid= 1569094 |doi=  |display-authors=etal}}
*{{cite journal  | author=Adachi Y, Ishida-Takahashi A, Takahashi C, ''et al.'' |title=Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3968-72 |year= 1991 |pmid= 1995645 |doi=  }}
*{{cite journal  | vauthors=Adachi Y, Ishida-Takahashi A, Takahashi C |title=Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3968–72 |year= 1991 |pmid= 1995645 |doi=  |display-authors=etal}}
*{{cite journal  | author=Inazawa J, Nakagawa H, Misawa S, ''et al.'' |title=Assignment of the human calpastatin gene (CAST) to chromosome 5 at region q14----q22. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 3-4 |pages= 156-8 |year= 1991 |pmid= 2265559 |doi=  }}
*{{cite journal  | vauthors=Inazawa J, Nakagawa H, Misawa S |title=Assignment of the human calpastatin gene (CAST) to chromosome 5 at region q14----q22. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 3-4 |pages= 156–8 |year= 1991 |pmid= 2265559 |doi=10.1159/000132982 |display-authors=etal}}
*{{cite journal  | author=Uemori T, Shimojo T, Asada K, ''et al.'' |title=Characterization of a functional domain of human calpastatin. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 3 |pages= 1485-93 |year= 1990 |pmid= 2407243 |doi=  }}
*{{cite journal  | vauthors=Uemori T, Shimojo T, Asada K |title=Characterization of a functional domain of human calpastatin. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 3 |pages= 1485–93 |year= 1990 |pmid= 2407243 |doi=10.1016/0006-291X(90)91035-Q |display-authors=etal}}
*{{cite journal  | author=Maki M, Bagci H, Hamaguchi K, ''et al.'' |title=Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. |journal=J. Biol. Chem. |volume=264 |issue= 32 |pages= 18866-9 |year= 1989 |pmid= 2553724 |doi=  }}
*{{cite journal  | vauthors=Maki M, Bagci H, Hamaguchi K |title=Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. |journal=J. Biol. Chem. |volume=264 |issue= 32 |pages= 18866–9 |year= 1989 |pmid= 2553724 |doi=  |display-authors=etal}}
*{{cite journal  | author=Murachi T, Takano E, Maki M, ''et al.'' |title=Cloning and expression of the genes for calpains and calpastatins. |journal=Biochem. Soc. Symp. |volume=55 |issue=  |pages= 29-44 |year= 1990 |pmid= 2559735 |doi=  }}
*{{cite journal  | vauthors=Murachi T, Takano E, Maki M |title=Cloning and expression of the genes for calpains and calpastatins. |journal=Biochem. Soc. Symp. |volume=55 |issue=  |pages= 29–44 |year= 1990 |pmid= 2559735 |doi=  |display-authors=etal}}
*{{cite journal  | author=Asada K, Ishino Y, Shimada M, ''et al.'' |title=cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. |journal=J. Enzym. Inhib. |volume=3 |issue= 1 |pages= 49-56 |year= 1991 |pmid= 2577276 |doi=  }}
*{{cite journal  | vauthors=Asada K, Ishino Y, Shimada M |title=cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. |journal=J. Enzym. Inhib. |volume=3 |issue= 1 |pages= 49–56 |year= 1991 |pmid= 2577276 |doi=10.3109/14756368909030363 |display-authors=etal}}
*{{cite journal  | author=Pontremoli S, Salamino F, Sparatore B, ''et al.'' |title=Characterization of the calpastatin defect in erythrocytes from patients with essential hypertension. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 867-74 |year= 1989 |pmid= 2849943 |doi=  }}
*{{cite journal  | vauthors=Pontremoli S, Salamino F, Sparatore B |title=Characterization of the calpastatin defect in erythrocytes from patients with essential hypertension. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 867–74 |year= 1989 |pmid= 2849943 |doi=10.1016/S0006-291X(88)80955-0 |display-authors=etal}}
*{{cite journal  | author=Mimori T, Suganuma K, Tanami Y, ''et al.'' |title=Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7267-71 |year= 1995 |pmid= 7638179 |doi=  }}
*{{cite journal  | vauthors=Mimori T, Suganuma K, Tanami Y |title=Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7267–71 |year= 1995 |pmid= 7638179 |doi=10.1073/pnas.92.16.7267  | pmc=41320 |display-authors=etal}}
*{{cite journal  | author=Després N, Talbot G, Plouffe B, ''et al.'' |title=Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera. |journal=J. Clin. Invest. |volume=95 |issue= 4 |pages= 1891-6 |year= 1995 |pmid= 7706496 |doi=  }}
*{{cite journal  | vauthors=Després N, Talbot G, Plouffe B |title=Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera. |journal=J. Clin. Invest. |volume=95 |issue= 4 |pages= 1891–6 |year= 1995 |pmid= 7706496 |doi=10.1172/JCI117870 | pmc=295733  |display-authors=etal}}
*{{cite journal  | author=Wei SG, Wang LF, Miao SY, ''et al.'' |title=Expression of the calpastatin gene segment during spermiogenesis in human testis: an in situ hybridization study. |journal=Arch. Androl. |volume=34 |issue= 1 |pages= 9-12 |year= 1995 |pmid= 7710300 |doi=  }}
*{{cite journal  | vauthors=Wei SG, Wang LF, Miao SY |title=Expression of the calpastatin gene segment during spermiogenesis in human testis: an in situ hybridization study. |journal=Arch. Androl. |volume=34 |issue= 1 |pages= 9–12 |year= 1995 |pmid= 7710300 |doi=10.3109/01485019508987826 |display-authors=etal}}
*{{cite journal  | author=Wang LF, Wei SG, Miao SY, ''et al.'' |title=Calpastatin gene in human testis. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 2 |pages= 245-51 |year= 1994 |pmid= 7951045 |doi=  }}
*{{cite journal  | vauthors=Wang LF, Wei SG, Miao SY |title=Calpastatin gene in human testis. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 2 |pages= 245–51 |year= 1994 |pmid= 7951045 |doi=  |display-authors=etal}}
*{{cite journal  | author=Schwarz-Benmeir N, Glaser T, Barnoy S, Kosower NS |title=Calpastatin in erythrocytes of young and old individuals. |journal=Biochem. J. |volume=304 ( Pt 2) |issue=  |pages= 365-70 |year= 1995 |pmid= 7998969 |doi=  }}
*{{cite journal  | vauthors=Schwarz-Benmeir N, Glaser T, Barnoy S, Kosower NS |title=Calpastatin in erythrocytes of young and old individuals. |journal=Biochem. J. |volume=304 |issue=  2|pages= 365–70 |year= 1995 |pmid= 7998969 |doi=  | pmc=1137502 }}
*{{cite journal  | author=Ma H, Yang HQ, Takano E, ''et al.'' |title=Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains. |journal=J. Biochem. |volume=113 |issue= 5 |pages= 591-9 |year= 1993 |pmid= 8340353 |doi=  }}
*{{cite journal  | vauthors=Fujitani K, Kambayashi J, Sakon M |title=Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. |journal=J. Cell. Biochem. |volume=66 |issue= 2 |pages= 197–209 |year= 1997 |pmid= 9213221 |doi=10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L |display-authors=etal}}
*{{cite journal  | author=Fujitani K, Kambayashi J, Sakon M, ''et al.'' |title=Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. |journal=J. Cell. Biochem. |volume=66 |issue= 2 |pages= 197-209 |year= 1997 |pmid= 9213221 |doi=  }}
*{{cite journal  | vauthors=Wang KK, Posmantur R, Nadimpalli R |title=Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis. |journal=Arch. Biochem. Biophys. |volume=356 |issue= 2 |pages= 187–96 |year= 1998 |pmid= 9705209 |doi= 10.1006/abbi.1998.0748 |display-authors=etal}}
*{{cite journal  | author=Wang KK, Posmantur R, Nadimpalli R, ''et al.'' |title=Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis. |journal=Arch. Biochem. Biophys. |volume=356 |issue= 2 |pages= 187-96 |year= 1998 |pmid= 9705209 |doi= 10.1006/abbi.1998.0748 }}
*{{cite journal  | vauthors=Han Y, Weinman S, Boldogh I |title=Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 787–94 |year= 1999 |pmid= 9873017 |doi=10.1074/jbc.274.2.787 |display-authors=etal}}
*{{cite journal  | author=Han Y, Weinman S, Boldogh I, ''et al.'' |title=Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 787-94 |year= 1999 |pmid= 9873017 |doi=  }}
*{{cite journal  | vauthors=Ishikawa H, Nakagawa Y, Shimizu K |title=Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 2 |pages= 341–6 |year= 2000 |pmid= 10600505 |doi= 10.1006/bbrc.1999.1819 |display-authors=etal}}
*{{cite journal  | author=Ishikawa H, Nakagawa Y, Shimizu K, ''et al.'' |title=Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 2 |pages= 341-6 |year= 2000 |pmid= 10600505 |doi= 10.1006/bbrc.1999.1819 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Proteases}}
{{Enzymes}}
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[[Category:Peptidase]]
[[Category:EC 3.4]]
 
 
{{gene-5-stub}}

Latest revision as of 07:09, 4 August 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

n/a

n/a

UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Calpastatin is a protein that in humans is encoded by the CAST gene.[1][2][3][4]

The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein.[citation needed] The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined.[4]

References

  1. ↑ Ma H, Yang HQ, Takano E, Lee WJ, Hatanaka M, Maki M (Sep 1993). "Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains". J Biochem. 113 (5): 591–9. PMID 8340353.
  2. ↑ Averna M, De Tullio R, Capini P, Salamino F, Pontremoli S, Melloni E (Dec 2003). "Changes in calpastatin localization and expression during calpain activation: a new mechanism for the regulation of intracellular Ca(2+)-dependent proteolysis". Cell Mol Life Sci. 60 (12): 2669–78. doi:10.1007/s00018-003-3288-0. PMID 14685690.
  3. ↑ Raynaud P, Jayat-Vignoles C, Laforet MP, Leveziel H, Amarger V (Apr 2005). "Four promoters direct expression of the calpastatin gene". Arch Biochem Biophys. 437 (1): 69–77. doi:10.1016/j.abb.2005.02.026. PMID 15820218.
  4. ↑ 4.0 4.1 "Entrez Gene: CAST calpastatin".

External links

  • The MEROPS online database for peptidases and their inhibitors: LI27.001

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=Calpastatin&oldid=1532788"