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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/10 14:39:07」(JST)

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Leucyl/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.^[1]^[2]

This 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.^[2]

Mutations in this gene have been associated to psoriasis risk.(doi:10.1038/jid.2013.317)

Interactions

Cystinyl aminopeptidase has been shown to interact with TNKS2.^[3]^[4]^[5]

References

^ 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): 56–61. doi:10.1074/jbc.271.1.56. PMID 8550619.
^ ^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. (United States) 277 (35): 31887–92. doi:10.1074/jbc.M203916200. ISSN 0021-9258. PMID 12080061.
^ 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. (UNITED STATES) 275 (49): 38437–44. doi:10.1074/jbc.M007635200. ISSN 0021-9258. PMID 10988299.
^ 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. (England) 361 (Pt 3): 451–9. doi:10.1042/0264-6021:3610451. ISSN 0264-6021. PMC 1222327. PMID 11802774.

External links

The MEROPS online database for peptidases and their inhibitors: M01.011

External links

Cystinyl aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Molecular and Cellular Biology portal

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English Journal

The complement of family M1 aminopeptidases of Haemonchus contortus - Biotechnological implications.

Mohandas N1, Young ND1, Jabbar A1, Korhonen PK1, Koehler AV1, Hall RS1, Hu M2, Hofmann A3, Gasser RB4.
Biotechnology advances.Biotechnol Adv.2015 Oct 24. pii: S0734-9750(15)30041-0. doi: 10.1016/j.biotechadv.2015.10.003. [Epub ahead of print]
Although substantial research has been focused on the 'hidden antigen' H11 of Haemonchus contortus as a vaccine against haemonchosis in small ruminants, little is know about this and related aminopeptidases. In the present article, we reviewed genomic and transcriptomic data sets to define, for the
PMID 26597954

Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope Precursor Recognition and Processing.

Mpakali A1, Saridakis E1, Harlos K2, Zhao Y2, Papakyriakou A1, Kokkala P3, Georgiadis D4, Stratikos E5.
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2015 Sep 15;195(6):2842-51. doi: 10.4049/jimmunol.1501103. Epub 2015 Aug 10.
Aminopeptidases that generate antigenic peptides influence immunodominance and adaptive cytotoxic immune responses. The mechanisms that allow these enzymes to efficiently process a vast number of different long peptide substrates are poorly understood. In this work, we report the structure of insuli
PMID 26259583

Trans-Modulation of the Somatostatin Type 2A Receptor Trafficking by Insulin-Regulated Aminopeptidase Decreases Limbic Seizures.

De Bundel D1, Fafouri A2, Csaba Z2, Loyens E1, Lebon S2, El Ghouzzi V2, Peineau S3, Vodjdani G2, Kiagiadaki F4, Aourz N1, Coppens J1, Walrave L1, Portelli J1, Vanderheyden P5, Chai SY6, Thermos K4, Bernard V7, Collingridge G8, Auvin S2, Gressens P2, Smolders I1, Dournaud P9.
The Journal of neuroscience : the official journal of the Society for Neuroscience.J Neurosci.2015 Aug 26;35(34):11960-75. doi: 10.1523/JNEUROSCI.0476-15.2015.
Within the hippocampus, the major somatostatin (SRIF) receptor subtype, the sst2A receptor, is localized at postsynaptic sites of the principal neurons where it modulates neuronal activity. Following agonist exposure, this receptor rapidly internalizes and recycles slowly through the trans-Golgi net
PMID 26311777

Japanese Journal

Two Molecular Species of Oxytocinase (L-Cystine Aminopeptidase) in Human Placenta : Purification and Characterization

ITOH Chie,WATANABE Maho,NAGAMATSU Atsuo,SOEDA Shinji,KAWARABAYASHI Tatsuhiko,SHIMENO Hiroshi
Biological & pharmaceutical bulletin 20(1), 20-24, 1997-01-15
… Two different forms of oxytocinase (L-cystine aminopeptidase, CAP; …
NAID 110003638924

「シスチンアミノペプチダーゼ」

Leucyl/cystinyl aminopeptidase
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	4P8Q, 4PJ6
Identifiers
Symbols	LNPEP ; CAP; IRAP; P-LAP; PLAP
External IDs	OMIM: 151300 MGI: 2387123 HomoloGene: 21148 ChEMBL: 2693 GeneCards: LNPEP Gene
EC number	3.4.11.3
Gene ontology
Molecular function	• aminopeptidase activity; • protein binding; • metallopeptidase activity; • zinc ion binding; • peptide binding; • metalloaminopeptidase activity;
Cellular component	• extracellular region; • intracellular; • lysosomal membrane; • cytosol; • plasma membrane; • integral component of plasma membrane; • membrane; • cytoplasmic vesicle membrane; • early endosome lumen; • perinuclear region of cytoplasm;
Biological process	• protein polyubiquitination; • antigen processing and presentation of peptide antigen via MHC class I; • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; • proteolysis; • signal transduction; • cell-cell signaling; • female pregnancy; • regulation of blood pressure; • protein catabolic process; • antigen processing and presentation of exogenous peptide antigen via MHC class I; • peptide catabolic process; • SMAD protein signal transduction; • membrane organization;
	Sources: Amigo / QuickGO
Orthologs
	v; t; e;