Aminopeptidase N
From Proteopedia
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'''Aminopeptidase N''' (APN; CD13) is a zinc-dependent integral ectopeptidase composed of 967 amino acids, with a molecular mass of 160 kDa that cleaves neutral amino acids from the N-terminal of peptides.<ref name = cancer>PMID: 21619485</ref><ref>DOI: 10.1002/med.20044</ref> It has been implicated in coronovirus invasion of cells of the respiratory tract, cardiovascular disease, diabetic nephropathy, rheumatoid arthritis, inflammatory bowel disease and numerous cancers.<ref name = cancer/><ref name = currmed>PMID: 15992355</ref><ref>PMID: 24762977</ref> Its expression in cancer cells has been associated with more aggressive phenotypes and a role for it has been determined in: leukaemia, breast cancer, colon cancer, stomach cancer, non-small cell lung cancer, kidney cancer, ovarian cancer, pancreatic cancer and thryoid cancer.<ref name = cancer/> It is also an enkephalinase, that is, it is an enzyme involved in the degradation of enkephalins, such as met-enkephalin and leu-enkephalin.<ref>PMID: 18855623</ref> Additional roles in immunity have also been discovered (such as in the degradation of the pro-inflammatory cytokines, [[interleukin]]-8 and N-formyl-methionine-leucine-phenylalanine and in the regulation of T cell function<ref>PMID: 10373632</ref>) and the use of APN inhibitors has been proposed as a potential drug therapy for inflammatory bowel disease and rheumatoid arthritis.<ref name = currmed/><ref>PMID: 18508466</ref> It is found in abundance in the central nervous system, liver, mucosal layer of the small intestine and kidneys.<ref>PMID: 18008160</ref><ref>DOI: 10.2174/092986707780059571</ref> | '''Aminopeptidase N''' (APN; CD13) is a zinc-dependent integral ectopeptidase composed of 967 amino acids, with a molecular mass of 160 kDa that cleaves neutral amino acids from the N-terminal of peptides.<ref name = cancer>PMID: 21619485</ref><ref>DOI: 10.1002/med.20044</ref> It has been implicated in coronovirus invasion of cells of the respiratory tract, cardiovascular disease, diabetic nephropathy, rheumatoid arthritis, inflammatory bowel disease and numerous cancers.<ref name = cancer/><ref name = currmed>PMID: 15992355</ref><ref>PMID: 24762977</ref> Its expression in cancer cells has been associated with more aggressive phenotypes and a role for it has been determined in: leukaemia, breast cancer, colon cancer, stomach cancer, non-small cell lung cancer, kidney cancer, ovarian cancer, pancreatic cancer and thryoid cancer.<ref name = cancer/> It is also an enkephalinase, that is, it is an enzyme involved in the degradation of enkephalins, such as met-enkephalin and leu-enkephalin.<ref>PMID: 18855623</ref> Additional roles in immunity have also been discovered (such as in the degradation of the pro-inflammatory cytokines, [[interleukin]]-8 and N-formyl-methionine-leucine-phenylalanine and in the regulation of T cell function<ref>PMID: 10373632</ref>) and the use of APN inhibitors has been proposed as a potential drug therapy for inflammatory bowel disease and rheumatoid arthritis.<ref name = currmed/><ref>PMID: 18508466</ref> It is found in abundance in the central nervous system, liver, mucosal layer of the small intestine and kidneys.<ref>PMID: 18008160</ref><ref>DOI: 10.2174/092986707780059571</ref> | ||
APN is inhibited by [[Ezetimibe]] which is used as high blood cholesterol medication. | APN is inhibited by [[Ezetimibe]] which is used as high blood cholesterol medication. | ||
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== References == | == References == | ||
<references/> | <references/> | ||
Current revision
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References
- ↑ 1.0 1.1 1.2 Su L, Fang H, Xu W. Aminopeptidase N (EC 3.4.11.2) inhibitors (2006 - 2010): a patent review. Expert Opin Ther Pat. 2011 Aug;21(8):1241-65. doi: 10.1517/13543776.2011.587002. , Epub 2011 May 28. PMID:21619485 doi:http://dx.doi.org/10.1517/13543776.2011.587002
- ↑ Bauvois B, Dauzonne D. Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects. Med Res Rev. 2006 Jan;26(1):88-130. PMID:16216010 doi:http://dx.doi.org/10.1002/med.20044
- ↑ 3.0 3.1 Xu W, Li Q. Progress in the development of aminopeptidase N (APN/CD13) inhibitors. Curr Med Chem Anticancer Agents. 2005 May;5(3):281-301. PMID:15992355
- ↑ Bosch BJ, Smits SL, Haagmans BL. Membrane ectopeptidases targeted by human coronaviruses. Curr Opin Virol. 2014 Apr 21;6C:55-60. doi: 10.1016/j.coviro.2014.03.011. PMID:24762977 doi:http://dx.doi.org/10.1016/j.coviro.2014.03.011
- ↑ Thanawala V, Kadam VJ, Ghosh R. Enkephalinase inhibitors: potential agents for the management of pain. Curr Drug Targets. 2008 Oct;9(10):887-94. PMID:18855623
- ↑ Lendeckel U, Arndt M, Frank K, Wex T, Ansorge S. Role of alanyl aminopeptidase in growth and function of human T cells (review). Int J Mol Med. 1999 Jul;4(1):17-27. PMID:10373632
- ↑ Bank U, Bohr UR, Reinhold D, Lendeckel U, Ansorge S, Malfertheiner P, Tager M. Inflammatory bowel diseases: multiple benefits from therapy with dipeptidyl- and alanyl-aminopeptidase inhibitors. Front Biosci. 2008 May 1;13:3699-713. PMID:18508466
- ↑ Danziger RS. Aminopeptidase N in arterial hypertension. Heart Fail Rev. 2008 Sep;13(3):293-8. Epub 2007 Nov 16. PMID:18008160 doi:http://dx.doi.org/10.1007/s10741-007-9061-y
- ↑ doi: https://dx.doi.org/10.2174/092986707780059571
