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{{ | '''Carboxypeptidase N catalytic chain''' is an [[enzyme]] that in humans is encoded by the ''CPN1'' [[gene]].<ref name="pmid9628828">{{cite journal | vauthors = Riley DA, Tan F, Miletich DJ, Skidgel RA | title = Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1) | journal = Genomics | volume = 50 | issue = 1 | pages = 105–8 |date=Apr 1999 | pmid = 9628828 | pmc = | doi = 10.1006/geno.1998.5295 }}</ref><ref name="pmid2912725">{{cite journal | vauthors = Gebhard W, Schube M, Eulitz M | title = cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) | journal = Eur J Biochem | volume = 178 | issue = 3 | pages = 603–7 |date=Mar 1989 | pmid = 2912725 | pmc = | doi =10.1111/j.1432-1033.1989.tb14488.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1369| accessdate = }}</ref> | ||
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| summary_text = Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer | | summary_text = Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer composed of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.<ref name="entrez" /> | ||
In melanocytic cells CPN1 gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell Melanoma Res. | volume = 21 | issue = 6 | pages = 665–76 | year = 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x | issn = |display-authors=etal}}</ref> | |||
}} | }} | ||
==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|CPN1}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Matthews KW, Mueller-Ortiz SL, Wetsel RA |title=Carboxypeptidase N: a pleiotropic regulator of inflammation. |journal=Mol. Immunol. |volume=40 |issue= 11 |pages= 785–93 |year= 2004 |pmid= 14687935 |doi=10.1016/j.molimm.2003.10.002 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Gebhard W, Schube M, Eulitz M |title=cDNA cloning of kininase 1. |journal=Adv. Exp. Med. Biol. |volume=247B |issue= |pages= 261–4 |year= 1990 |pmid= 2610070 |doi= 10.1007/978-1-4615-9546-5_43}} | ||
*{{cite journal | vauthors=Skidgel RA, Bennett CD, Schilling JW |title=Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases. |journal=Biochem. Biophys. Res. Commun. |volume=154 |issue= 3 |pages= 1323–9 |year= 1988 |pmid= 3408501 |doi=10.1016/0006-291X(88)90284-7 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Hendriks D, Vingron M, Vriend G |title=On the specificity of carboxypeptidase N, a comparative study. |journal=Biol. Chem. Hoppe-Seyler |volume=374 |issue= 9 |pages= 843–9 |year= 1994 |pmid= 8267877 |doi= 10.1515/bchm3.1993.374.7-12.843|display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Sato T, Miwa T, Akatsu H |title=Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not. |journal=J. Immunol. |volume=165 |issue= 2 |pages= 1053–8 |year= 2000 |pmid= 10878383 |doi= 10.4049/jimmunol.165.2.1053|display-authors=etal}} | ||
*{{cite journal | vauthors=Campbell WD, Lazoura E, Okada N, Okada H |title=Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. |journal=Microbiol. Immunol. |volume=46 |issue= 2 |pages= 131–4 |year= 2002 |pmid= 11939578 |doi= 10.1111/j.1348-0421.2002.tb02669.x}} | |||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Cao H, Hegele RA |title=DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency. |journal=J. Hum. Genet. |volume=48 |issue= 1 |pages= 20–2 |year= 2003 |pmid= 12560874 |doi= 10.1007/s100380300003 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Shimomura Y, Kawamura T, Komura H |title=Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin. |journal=Microbiol. Immunol. |volume=47 |issue= 3 |pages= 241–5 |year= 2003 |pmid= 12725295 |doi= 10.1111/j.1348-0421.2003.tb03383.x|display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Davis DA, Singer KE, De La Luz Sierra M |title=Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation. |journal=Blood |volume=105 |issue= 12 |pages= 4561–8 |year= 2005 |pmid= 15718415 |doi= 10.1182/blood-2004-12-4618 | pmc=1895000 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal}} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=1369}} | |||
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Latest revision as of 09:59, 30 August 2017
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Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.[1][2][3]
Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer composed of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.[3]
In melanocytic cells CPN1 gene expression may be regulated by MITF.[4]
References
- ↑ Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1)". Genomics. 50 (1): 105–8. doi:10.1006/geno.1998.5295. PMID 9628828.
- ↑ Gebhard W, Schube M, Eulitz M (Mar 1989). "cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)". Eur J Biochem. 178 (3): 603–7. doi:10.1111/j.1432-1033.1989.tb14488.x. PMID 2912725.
- ↑ 3.0 3.1 "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1".
- ↑ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
External links
- Human CPN1 genome location and CPN1 gene details page in the UCSC Genome Browser.
Further reading
- Matthews KW, Mueller-Ortiz SL, Wetsel RA (2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Mol. Immunol. 40 (11): 785–93. doi:10.1016/j.molimm.2003.10.002. PMID 14687935.
- Gebhard W, Schube M, Eulitz M (1990). "cDNA cloning of kininase 1". Adv. Exp. Med. Biol. 247B: 261–4. doi:10.1007/978-1-4615-9546-5_43. PMID 2610070.
- Skidgel RA, Bennett CD, Schilling JW, et al. (1988). "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases". Biochem. Biophys. Res. Commun. 154 (3): 1323–9. doi:10.1016/0006-291X(88)90284-7. PMID 3408501.
- Hendriks D, Vingron M, Vriend G, et al. (1994). "On the specificity of carboxypeptidase N, a comparative study". Biol. Chem. Hoppe-Seyler. 374 (9): 843–9. doi:10.1515/bchm3.1993.374.7-12.843. PMID 8267877.
- Sato T, Miwa T, Akatsu H, et al. (2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2): 1053–8. doi:10.4049/jimmunol.165.2.1053. PMID 10878383.
- Campbell WD, Lazoura E, Okada N, Okada H (2002). "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.". Microbiol. Immunol. 46 (2): 131–4. doi:10.1111/j.1348-0421.2002.tb02669.x. PMID 11939578.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Cao H, Hegele RA (2003). "DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency". J. Hum. Genet. 48 (1): 20–2. doi:10.1007/s100380300003. PMID 12560874.
- Shimomura Y, Kawamura T, Komura H, et al. (2003). "Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin". Microbiol. Immunol. 47 (3): 241–5. doi:10.1111/j.1348-0421.2003.tb03383.x. PMID 12725295.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Davis DA, Singer KE, De La Luz Sierra M, et al. (2005). "Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation". Blood. 105 (12): 4561–8. doi:10.1182/blood-2004-12-4618. PMC 1895000. PMID 15718415.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
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