[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/leucyl-cystinyl-aminopeptidase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/leucyl-cystinyl-aminopeptidase-wikipedia\/","headline":"Leucyl\/cystinyl aminopeptidase – Wikipedia","name":"Leucyl\/cystinyl aminopeptidase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Leucyl\/cystinyl aminopeptidase, also known as cystinyl","datePublished":"2016-08-07","dateModified":"2016-08-07","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/leucyl-cystinyl-aminopeptidase-wikipedia\/","about":["Wiki"],"wordCount":5402,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensLeucyl\/cystinyl aminopeptidase, also known as cystinyl aminopeptidase (CAP), insulin-regulated aminopeptidase (IRAP), human placental leucine aminopeptidase (PLAP), oxytocinase, and vasopressinase, is an enzyme of the aminopeptidase group that in humans is encoded by the LNPEP gene.[5][6]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4This gene encodes a zinc-dependent aminopeptidase (metalloexopeptidase) that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms.[6]Mutations in this gene have been associated to psoriasis risk.(doi:10.1038\/jid.2013.317)Table of Contents       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Interactions[edit]References[edit]Further reading[edit]External links[edit]Interactions[edit]Cystinyl aminopeptidase has been shown to interact with TNKS2.[7][8][9]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000113441 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023845 – Ensembl, May 2017^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Rogi T, Tsujimoto M, Nakazato H, Mizutani S, Tomoda Y (February 1996). “Human placental leucine aminopeptidase\/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family”. J Biol Chem. 271 (1): 56\u201361. doi:10.1074\/jbc.271.1.56. PMID\u00a08550619.^ a b “Entrez Gene: LNPEP leucyl\/cystinyl aminopeptidase”.^ Sbodio, Juan I; Chi Nai-Wen (August 2002). “Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner”. J. Biol. Chem. 277 (35): 31887\u201392. doi:10.1074\/jbc.M203916200. ISSN\u00a00021-9258. PMID\u00a012080061.^ Chi, N W; Lodish H F (December 2000). “Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles”. J. Biol. Chem. 275 (49): 38437\u201344. doi:10.1074\/jbc.M007635200. ISSN\u00a00021-9258. PMID\u00a010988299.^ Sbodio, Juan I; Lodish Harvey F; Chi Nai-Wen (February 2002). “Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)”. Biochem. J. 361 (Pt 3): 451\u20139. doi:10.1042\/0264-6021:3610451. ISSN\u00a00264-6021. PMC\u00a01222327. PMID\u00a011802774.Further reading[edit]Albiston AL, Mustafa T, McDowall SG,  et\u00a0al. (2003). “AT4 receptor is insulin-regulated membrane aminopeptidase: potential mechanisms of memory enhancement”. Trends Endocrinol. Metab. 14 (2): 72\u20137. doi:10.1016\/S1043-2760(02)00037-1. PMID\u00a012591177. S2CID\u00a06481079.Keller SR (2004). “The insulin-regulated aminopeptidase: a companion and regulator of GLUT4”. Front. Biosci. 8 (6): s410\u201320. doi:10.2741\/1078. PMID\u00a012700100.Keller SR (2005). “Role of the insulin-regulated aminopeptidase IRAP in insulin action and diabetes”. Biol. Pharm. Bull. 27 (6): 761\u20134. doi:10.1248\/bpb.27.761. PMID\u00a015187412.Nomura S, Ito T, Yamamoto E,  et\u00a0al. (2005). “Gene regulation and physiological function of placental leucine aminopeptidase\/oxytocinase during pregnancy”. Biochim. Biophys. Acta. 1751 (1): 19\u201325. doi:10.1016\/j.bbapap.2005.04.006. PMID\u00a015894523.Tsujimoto M, Hattori A (2005). “The oxytocinase subfamily of M1 aminopeptidases”. Biochim. Biophys. Acta. 1751 (1): 9\u201318. doi:10.1016\/j.bbapap.2004.09.011. PMID\u00a016054015.Mizutani S, Shibata K, Kikkawa F,  et\u00a0al. (2007). “Essential role of placental leucine aminopeptidase in gynecologic malignancy”. Expert Opin. Ther. Targets. 11 (4): 453\u201361. doi:10.1517\/14728222.11.4.453. PMID\u00a017373876. S2CID\u00a042839602.Tsujimoto M, Mizutani S, Adachi H,  et\u00a0al. (1992). “Identification of human placental leucine aminopeptidase as oxytocinase”. Arch. Biochem. Biophys. 292 (2): 388\u201392. doi:10.1016\/0003-9861(92)90007-J. PMID\u00a01731608.Mizutani S, Akiyama H, Kurauchi O,  et\u00a0al. (1985). “In vitro degradation of angiotensin II (A-II) by human placental subcellular fractions, pregnancy sera and purified placental aminopeptidases”. Acta Endocrinol. 110 (1): 135\u20139. doi:10.1530\/acta.0.1100135. PMID\u00a03898693.Beckman L, Bj\u00f6rling G, Christodoulou C (1966). “Pregnancy enzymes and placental polymorphism. II. Leucine aminopeptidase”. Acta Genetica et Statistica Medica. 16 (2): 122\u201331. doi:10.1159\/000151957. PMID\u00a05953194.Itoh C, Watanabe M, Nagamatsu A,  et\u00a0al. (1997). “Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization”. Biol. Pharm. Bull. 20 (1): 20\u20134. doi:10.1248\/bpb.20.20. PMID\u00a09013800.Laustsen PG, Rasmussen TE, Petersen K,  et\u00a0al. (1997). “The complete amino acid sequence of human placental oxytocinase”. Biochim. Biophys. Acta. 1352 (1): 1\u20137. doi:10.1016\/S0167-4781(97)00036-5. PMID\u00a09177475.Nagasaka T, Nomura S, Okamura M,  et\u00a0al. (1998). “Immunohistochemical localization of placental leucine aminopeptidase\/oxytocinase in normal human placental, fetal and adult tissues”. Reprod. Fertil. Dev. 9 (8): 747\u201353. doi:10.1071\/R97055. PMID\u00a09733056.Horio J, Nomura S, Okada M,  et\u00a0al. (1999). “Structural organization of the 5′-end and chromosomal assignment of human placental leucine aminopeptidase\/insulin-regulated membrane aminopeptidase gene”. Biochem. Biophys. Res. Commun. 262 (1): 269\u201374. doi:10.1006\/bbrc.1999.1184. PMID\u00a010448104.Rasmussen TE, Pedraza-D\u00edaz S, Hardr\u00e9 R,  et\u00a0al. (2000). “Structure of the human oxytocinase\/insulin-regulated aminopeptidase gene and localization to chromosome 5q21”. Eur. J. Biochem. 267 (8): 2297\u2013306. doi:10.1046\/j.1432-1327.2000.01234.x. PMID\u00a010759854.Nakanishi Y, Nomura S, Okada M,  et\u00a0al. (2001). “Immunoaffinity purification and characterization of native placental leucine aminopeptidase\/oxytocinase from human placenta”. Placenta. 21 (7): 628\u201334. doi:10.1053\/plac.2000.0564. PMID\u00a010985965.Chi NW, Lodish HF (2001). “Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles”. J. Biol. Chem. 275 (49): 38437\u201344. doi:10.1074\/jbc.M007635200. PMID\u00a010988299.Matsumoto H, Nagasaka T, Hattori A,  et\u00a0al. (2001). “Expression of placental leucine aminopeptidase\/oxytocinase in neuronal cells and its action on neuronal peptides”. Eur. J. Biochem. 268 (11): 3259\u201366. doi:10.1046\/j.1432-1327.2001.02221.x. PMID\u00a011389728.Iwase A, Nomura S, Mizutani S (2001). “Characterization of a secretase activity for placental leucine aminopeptidase”. Arch. Biochem. Biophys. 393 (1): 163\u20139. doi:10.1006\/abbi.2001.2489. PMID\u00a011516173.Ito T, Nomura S, Okada M,  et\u00a0al. (2001). “Transcriptional regulation of human placental leucine aminopeptidase\/oxytocinase gene”. Mol. Hum. Reprod. 7 (9): 887\u201394. doi:10.1093\/molehr\/7.9.887. PMID\u00a011517297.External links[edit]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/leucyl-cystinyl-aminopeptidase-wikipedia\/#breadcrumbitem","name":"Leucyl\/cystinyl aminopeptidase – Wikipedia"}}]}]