This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Aminopeptidase N

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(Creating page.)
(Fixing refs.)
Line 1: Line 1:
<Structure load='4FYQ' size='350' frame='true' align='right' caption='The structure of human aminopeptidase N (PDB code [http://www.rcsb.org/pdb/explore/explore.do?structureId=4FYQ 4FYQ])' scene='Insert optional scene name here' />
<Structure load='4FYQ' size='350' frame='true' align='right' caption='The structure of human aminopeptidase N (PDB code [http://www.rcsb.org/pdb/explore/explore.do?structureId=4FYQ 4FYQ])' scene='Insert optional scene name here' />
-
'''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>PMID: 16216010‎</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>PMID: 17346152‎</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>
== References ==
== References ==
<references/>
<references/>

Revision as of 05:01, 7 May 2014

The structure of human aminopeptidase N (PDB code 4FYQ)

Drag the structure with the mouse to rotate

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.[1][2] 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.[1][3][4] 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.[1] It is also an enkephalinase, that is, it is an enzyme involved in the degradation of enkephalins, such as met-enkephalin and leu-enkephalin.[5] 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[6]) and the use of APN inhibitors has been proposed as a potential drug therapy for inflammatory bowel disease and rheumatoid arthritis.[3][7] It is found in abundance in the central nervous system, liver, mucosal layer of the small intestine and kidneys.[8][9]

References

  1. ↑ 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
  2. ↑ 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. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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
  9. ↑ doi: https://dx.doi.org/10.2174/092986707780059571‎

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Brenton Horne, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Aminopeptidase_N"
Personal tools