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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Calpain-1 catalytic subunit''' is a [[protein]] that in humans is encoded by the ''CAPN1'' [[gene]].<ref name="pmid3017764">{{cite journal | vauthors = Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K | title = Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence | journal = FEBS Lett | volume = 205 | issue = 2 | pages = 313–7 | date = Oct 1986 | pmid = 3017764 | pmc =  | doi = 10.1016/0014-5793(86)80919-X }}</ref><ref name="pmid2209092">{{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 = Cytogenet Cell Genet | volume = 53 | issue = 4 | pages = 225–9 | date = Nov 1990 | pmid = 2209092 | pmc = | doi = 10.1159/000132937 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_CAPN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zcm.
| PDB = {{PDB2|1zcm}}, {{PDB2|2ary}}
| Name = Calpain 1, (mu/I) large subunit
| HGNCid = 1476
| Symbol = CAPN1
| AltSymbols =; CANP; CANPL1; muCANP; muCL
| OMIM = 114220
| ECnumber = 
| Homologene = 3800
| MGIid = 88263
| GeneAtlas_image1 = PBB_GE_CAPN1_200752_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004198 |text = calpain activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 823
    | Hs_Ensembl = ENSG00000014216
    | Hs_RefseqProtein = NP_005177
    | Hs_RefseqmRNA = NM_005186
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 64705792
    | Hs_GenLoc_end = 64736048
    | Hs_Uniprot = P07384
    | Mm_EntrezGene = 12333
    | Mm_Ensembl = ENSMUSG00000024942
    | Mm_RefseqmRNA = NM_007600
    | Mm_RefseqProtein = NP_031626
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 5988546
    | Mm_GenLoc_end = 6015163
    | Mm_Uniprot = Q3TB79
  }}
}}
'''Calpain 1, (mu/I) large subunit''', also known as '''CAPN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The [[calpain]]s, calcium-activated neutral proteases, are nonlysosomal, intracellular [[cysteine protease]]s. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.<ref name="entrez">{{cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
CAPN1 has been shown to [[Protein-protein interaction|interact]] with [[PSEN2]].<ref name="pmid9852298">{{cite journal | vauthors = Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K | title = The presenilin 2 loop domain interacts with the mu-calpain C-terminal region | journal = Int. J. Mol. Med. | volume = 1 | issue = 5 | pages = 797–9 | year = 1998 | pmid = 9852298 | doi = 10.3892/ijmm.1.5.797 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S | title = Calpain: novel family members, activation, and physiologic function | journal = Biol. Chem. Hoppe-Seyler | volume = 376 | issue = 9 | pages = 523–9 | year = 1996 | pmid = 8561910 | doi =  }}
| citations =
* {{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 | year = 2001 | pmid = 11516996 | doi = 10.1016/S1471-4914(01)02049-4 }}
*{{cite journal | author=Suzuki K, Sorimachi H, Yoshizawa T, ''et al.'' |title=Calpain: novel family members, activation, and physiologic function. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 9 |pages= 523-9 |year= 1996 |pmid= 8561910 |doi=  }}
* {{cite journal | vauthors = Goll DE, Thompson VF, Li H, Wei W, Cong J | title = The calpain system | journal = Physiol. Rev. | volume = 83 | issue = 3 | pages = 731–801 | year = 2003 | pmid = 12843408 | doi = 10.1152/physrev.00029.2002 }}
*{{cite journal | author=Huang Y, Wang KK |title=The calpain family and human disease. |journal=Trends in molecular medicine |volume=7 |issue= 8 |pages= 355-62 |year= 2001 |pmid= 11516996 |doi= }}
* {{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 = J. Neurosci. Res. | volume = 29 | issue = 3 | pages = 346–54 | year = 1991 | pmid = 1656060 | doi = 10.1002/jnr.490290310 }}
*{{cite journal | author=Goll DE, Thompson VF, Li H, ''et al.'' |title=The calpain system. |journal=Physiol. Rev. |volume=83 |issue= 3 |pages= 731-801 |year= 2003 |pmid= 12843408 |doi= 10.1152/physrev.00029.2002 }}
* {{cite journal | vauthors = Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K | title = A novel member of the calcium-dependent cysteine protease family | journal = Biol. Chem. Hoppe-Seyler | volume = 371 Suppl | issue = | pages = 171–6 | year = 1990 | pmid = 2400579 | doi =  }}
*{{cite journal | author=Banik NL, DeVries GH, Neuberger T, ''et al.'' |title=Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. |journal=J. Neurosci. Res. |volume=29 |issue= 3 |pages= 346-54 |year= 1991 |pmid= 1656060 |doi= 10.1002/jnr.490290310 }}
* {{cite journal | vauthors = Harris AS, Croall DE, Morrow JS | title = The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site | journal = J. Biol. Chem. | volume = 263 | issue = 30 | pages = 15754–61 | year = 1988 | pmid = 2844821 | doi =  }}
*{{cite journal | author=Ohno S, Minoshima S, Kudoh J, ''et al.'' |title=Four genes for the calpain family locate on four distinct human chromosomes. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 225-9 |year= 1990 |pmid= 2209092 |doi=  }}
* {{cite journal | vauthors = Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M | title = Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations | journal = Biochemistry | volume = 26 | issue = 10 | pages = 2863–70 | year = 1987 | pmid = 3038169 | doi = 10.1021/bi00384a030 }}
*{{cite journal | author=Sorimachi H, Ohmi S, Emori Y, ''et al.'' |title=A novel member of the calcium-dependent cysteine protease family. |journal=Biol. Chem. Hoppe-Seyler |volume=371 Suppl |issue= |pages= 171-6 |year= 1990 |pmid= 2400579 |doi=  }}
* {{cite journal | vauthors = Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y, Mizuno K, Ohno S, Kozawa O | title = Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C | journal = J. Biol. Chem. | volume = 270 | issue = 49 | pages = 29469–75 | year = 1996 | pmid = 7493986 | doi = 10.1074/jbc.270.49.29469 }}
*{{cite journal | author=Harris AS, Croall DE, Morrow JS |title=The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15754-61 |year= 1988 |pmid= 2844821 |doi= }}
* {{cite journal | vauthors = Kavita U, Mizel SB | title = Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease | journal = J. Biol. Chem. | volume = 270 | issue = 46 | pages = 27758–65 | year = 1996 | pmid = 7499244 | doi = 10.1074/jbc.270.46.27758 }}
*{{cite journal | author=Aoki K, Imajoh S, Ohno S, ''et al.'' |title=Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence. |journal=FEBS Lett. |volume=205 |issue= 2 |pages= 313-7 |year= 1986 |pmid= 3017764 |doi= }}
* {{cite journal | vauthors = Du X, Saido TC, Tsubuki S, Indig FE, Williams MJ, Ginsberg MH | title = Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit | journal = J. Biol. Chem. | volume = 270 | issue = 44 | pages = 26146–51 | year = 1995 | pmid = 7592818 | doi = 10.1074/jbc.270.44.26146 }}
*{{cite journal | author=Ishiguro H, Higashiyama S, Namikawa C, ''et al.'' |title=Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. |journal=Biochemistry |volume=26 |issue= 10 |pages= 2863-70 |year= 1987 |pmid= 3038169 |doi= }}
* {{cite journal | vauthors = Bradford HN, Jameson BA, Adam AA, Wassell RP, Colman RW | title = Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain | journal = J. Biol. Chem. | volume = 268 | issue = 35 | pages = 26546–51 | year = 1994 | pmid = 8253784 | doi =  }}
*{{cite journal | author=Morishita R, Nakayama H, Isobe T, ''et al.'' |title=Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C. |journal=J. Biol. Chem. |volume=270 |issue= 49 |pages= 29469-75 |year= 1996 |pmid= 7493986 |doi= }}
* {{cite journal | vauthors = Oda A, Ozaki K, Druker BJ, Miyakawa Y, Miyazaki H, Handa M, Morita H, Ohashi H, Ikeda Y | title = p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin | journal = Blood | volume = 88 | issue = 4 | pages = 1330–8 | year = 1996 | pmid = 8695851 | doi =  }}
*{{cite journal | author=Kavita U, Mizel SB |title=Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27758-65 |year= 1996 |pmid= 7499244 |doi=  }}
* {{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 = J. Biol. Chem. | volume = 271 | issue = 31 | pages = 18825–30 | year = 1996 | pmid = 8702541 | doi = 10.1074/jbc.271.31.18825 }}
*{{cite journal | author=Du X, Saido TC, Tsubuki S, ''et al.'' |title=Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26146-51 |year= 1995 |pmid= 7592818 |doi=  }}
* {{cite journal | vauthors = Courseaux A, Grosgeorge J, Gaudray P, Pannett AA, Forbes SA, Williamson C, Bassett D, Thakker RV, Teh BT, Farnebo F, Shepherd J, Skogseid B, Larsson C, Giraud S, Zhang CX, Salandre J, Calender A | title = Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1) | journal = Genomics | volume = 37 | issue = 3 | pages = 354–65 | year = 1997 | pmid = 8938448 | doi = 10.1006/geno.1996.0570 }}
*{{cite journal | author=Bradford HN, Jameson BA, Adam AA, ''et al.'' |title=Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26546-51 |year= 1994 |pmid= 8253784 |doi= }}
* {{cite journal | vauthors = Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A | title = NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain | journal = Biochem. Biophys. Res. Commun. | volume = 229 | issue = 1 | pages = 299–304 | year = 1997 | pmid = 8954122 | doi = 10.1006/bbrc.1996.1796 }}
*{{cite journal | author=Oda A, Ozaki K, Druker BJ, ''et al.'' |title=p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin. |journal=Blood |volume=88 |issue= 4 |pages= 1330-8 |year= 1996 |pmid= 8695851 |doi= }}
* {{cite journal | vauthors = Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS | title = Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility | journal = Biochemistry | volume = 36 | issue = 1 | pages = 57–65 | year = 1997 | pmid = 8993318 | doi = 10.1021/bi962034i }}
*{{cite journal | author=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=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18825-30 |year= 1996 |pmid= 8702541 |doi= }}
* {{cite journal | vauthors = Norris FA, Atkins RC, Majerus PW | title = Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets | journal = J. Biol. Chem. | volume = 272 | issue = 17 | pages = 10987–9 | year = 1997 | pmid = 9110986 | doi = 10.1074/jbc.272.17.10987 }}
*{{cite journal | author=Courseaux A, Grosgeorge J, Gaudray P, ''et al.'' |title=Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1). |journal=Genomics |volume=37 |issue= 3 |pages= 354-65 |year= 1997 |pmid= 8938448 |doi=  }}
*{{cite journal | author=Corasaniti MT, Navarra M, Catani MV, ''et al.'' |title=NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 299-304 |year= 1997 |pmid= 8954122 |doi= 10.1006/bbrc.1996.1796 }}
*{{cite journal  | author=Stabach PR, Cianci CD, Glantz SB, ''et al.'' |title=Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. |journal=Biochemistry |volume=36 |issue= 1 |pages= 57-65 |year= 1997 |pmid= 8993318 |doi= 10.1021/bi962034i }}
*{{cite journal  | author=Norris FA, Atkins RC, Majerus PW |title=Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 10987-9 |year= 1997 |pmid= 9110986 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C02.001 C02.001]
* {{UCSC gene info|CAPN1}}
 
{{PDB Gallery|geneid=823}}
{{Cysteine proteases}}
 
[[Category:EF-hand-containing proteins]]
 
 
{{gene-11-stub}}

Latest revision as of 19:49, 1 November 2017

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

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Calpain-1 catalytic subunit is a protein that in humans is encoded by the CAPN1 gene.[1][2][3]

Function

The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.[3]

Interactions

CAPN1 has been shown to interact with PSEN2.[4]

References

  1. ↑ Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K (Oct 1986). "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence". FEBS Lett. 205 (2): 313–7. doi:10.1016/0014-5793(86)80919-X. PMID 3017764.
  2. ↑ Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (Nov 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.
  3. ↑ 3.0 3.1 "Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit".
  4. ↑ Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K (1998). "The presenilin 2 loop domain interacts with the mu-calpain C-terminal region". Int. J. Mol. Med. 1 (5): 797–9. doi:10.3892/ijmm.1.5.797. PMID 9852298.

Further reading

  • Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (1996). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler. 376 (9): 523–9. PMID 8561910.
  • 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.
  • Goll DE, Thompson VF, Li H, Wei W, Cong J (2003). "The calpain system". Physiol. Rev. 83 (3): 731–801. doi:10.1152/physrev.00029.2002. PMID 12843408.
  • Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL (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.
  • Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K (1990). "A novel member of the calcium-dependent cysteine protease family". Biol. Chem. Hoppe-Seyler. 371 Suppl: 171–6. PMID 2400579.
  • Harris AS, Croall DE, Morrow JS (1988). "The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site". J. Biol. Chem. 263 (30): 15754–61. PMID 2844821.
  • Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M (1987). "Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations". Biochemistry. 26 (10): 2863–70. doi:10.1021/bi00384a030. PMID 3038169.
  • Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y, Mizuno K, Ohno S, Kozawa O (1996). "Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C". J. Biol. Chem. 270 (49): 29469–75. doi:10.1074/jbc.270.49.29469. PMID 7493986.
  • Kavita U, Mizel SB (1996). "Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease". J. Biol. Chem. 270 (46): 27758–65. doi:10.1074/jbc.270.46.27758. PMID 7499244.
  • Du X, Saido TC, Tsubuki S, Indig FE, Williams MJ, Ginsberg MH (1995). "Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit". J. Biol. Chem. 270 (44): 26146–51. doi:10.1074/jbc.270.44.26146. PMID 7592818.
  • Bradford HN, Jameson BA, Adam AA, Wassell RP, Colman RW (1994). "Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain". J. Biol. Chem. 268 (35): 26546–51. PMID 8253784.
  • Oda A, Ozaki K, Druker BJ, Miyakawa Y, Miyazaki H, Handa M, Morita H, Ohashi H, Ikeda Y (1996). "p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin". Blood. 88 (4): 1330–8. PMID 8695851.
  • 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.
  • Courseaux A, Grosgeorge J, Gaudray P, Pannett AA, Forbes SA, Williamson C, Bassett D, Thakker RV, Teh BT, Farnebo F, Shepherd J, Skogseid B, Larsson C, Giraud S, Zhang CX, Salandre J, Calender A (1997). "Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1)". Genomics. 37 (3): 354–65. doi:10.1006/geno.1996.0570. PMID 8938448.
  • Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A (1997). "NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain". Biochem. Biophys. Res. Commun. 229 (1): 299–304. doi:10.1006/bbrc.1996.1796. PMID 8954122.
  • Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS (1997). "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility". Biochemistry. 36 (1): 57–65. doi:10.1021/bi962034i. PMID 8993318.
  • Norris FA, Atkins RC, Majerus PW (1997). "Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets". J. Biol. Chem. 272 (17): 10987–9. doi:10.1074/jbc.272.17.10987. PMID 9110986.

External links


Retrieved from "https://www.wikidoc.org/index.php?title=CAPN1&oldid=1415430"