関: annexin A2

WordNet

an addition that extends a main building (同)annexe, extension, wing
take (territory) as if by conquest; "Hitler annexed Lithuania"
attach to
the 9th letter of the Roman alphabet (同)i

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iodineの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/05/27 05:53:55」(JST)

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Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.^[3]

Annexin 2 is involved in diverse cellular processes such as cell motility (especially that of the epithelial cells), linkage of membrane-associated protein complexes to the actin cytoskeleton, endocytosis, fibrinolysis, ion channel formation, and cell matrix interactions. It is a calcium-dependent phospholipid-binding protein whose function is to help organize exocytosis of intracellular proteins to the extracellular domain. Annexin II is a pleiotropic protein meaning that its function is dependent on place and time in the body.

Gene

The ANXA2 gene, located at 15q22.2, has three pseudogenes located on chromosomes 4, 9 and 10, respectively. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.^[4]

Function

This protein is a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions as an autocrine factor which heightens osteoclast formation and bone resorption.^[4] Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.^[5]

Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.

Interactions

Annexin A2 has been shown to interact with Prohibitin,^[6] CEACAM1,^[7] S100A10,^[8]^[9] PCNA^[10] and complement Factor H ^[11]

References

^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (Nov 1994). "Cloning and identification of annexin II as an autocrine/paracrine factor that increases osteoclast formation and bone resorption". The Journal of Biological Chemistry. 269 (46): 28696–701. PMID 7961821.
^ ^a ^b "Entrez Gene: ANXA2 annexin A2".
^ Kling T, Ferrarese R, Ó hAilín D, Johansson P, Heiland DH, Dai F, Vasilikos I, Weyerbrock A, Jörnsten R, Carro MS, Nelander S (Sep 2016). "Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma". EBioMedicine.
^ Bacher S, Achatz G, Schmitz ML, Lamers MC (Dec 2002). "Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2". Biochimie. 84 (12): 1207–20. doi:10.1016/S0300-9084(02)00027-5. PMID 12628297.
^ Kirshner J, Schumann D, Shively JE (Dec 2003). "CEACAM1, a cell-cell adhesion molecule, directly associates with annexin II in a three-dimensional model of mammary morphogenesis". The Journal of Biological Chemistry. 278 (50): 50338–45. doi:10.1074/jbc.M309115200. PMID 14522961.
^ Réty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, Russo-Marie F, Lewit-Bentley A (Jan 1999). "The crystal structure of a complex of p11 with the annexin II N-terminal peptide". Nature Structural Biology. 6 (1): 89–95. doi:10.1038/4965. PMID 9886297.
^ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (Jul 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". The Journal of Biological Chemistry. 283 (28): 19192–200. doi:10.1074/jbc.M800100200. PMC 2443646 . PMID 18434302.
^ Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (Oct 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". The Journal of Biological Chemistry. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
^ Leffler J, Herbert AP, Norström E, Schmidt CQ, Barlow PN, Blom AM, Martin M (Feb 2010). "Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells". The Journal of Biological Chemistry. 285 (6): 3766–76. doi:10.1074/jbc.M109.045427. PMC 2823518 . PMID 19951950.

External links

Annexin A2 at the US National Library of Medicine Medical Subject Headings (MeSH)
Human ANXA2 genome location and ANXA2 gene details page in the UCSC Genome Browser.

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English Journal

Environmental toxicants perturb human Sertoli cell adhesive function via changes in F-actin organization mediated by actin regulatory proteins.

Xiao X1, Mruk DD, Tang EI, Wong CK, Lee WM, John CM, Turek PJ, Silvestrini B, Cheng CY.
Human reproduction (Oxford, England).Hum Reprod.2014 Jun;29(6):1279-91. doi: 10.1093/humrep/deu011. Epub 2014 Feb 13.
STUDY QUESTION: Can human Sertoli cells cultured in vitro and that have formed an epithelium be used as a model to monitor toxicant-induced junction disruption and to better understand the mechanism(s) by which toxicants disrupt cell adhesion at the Sertoli cell blood-testis barrier (BTB) SUMMARY AN
PMID 24532171

Biochemical and immunological characterization of annexin B30 from Clonorchis sinensis excretory/secretory products.

He L1, Ren M, Chen X, Wang X, Li S, Lin J, Liang C, Liang P, Hu Y, Lei H, Bian M, Huang Y, Wu Z, Li X, Yu X.
Parasitology research.Parasitol Res.2014 May 27. [Epub ahead of print]
Clonorchis sinensis has been classified as group I biological carcinogen for cholangiocarcinoma by the World Health Organization. Biological studies on excretory/secretory products (ESPs) enabled us to understand the pathogenesis mechanism of C. sinensis and develop new strategies for the prevention
PMID 24861011

Serum annexin A2 levels in acute brucellosis and brucellar spondylodiscitis.

Aktug Demir N1, Kolgelier S, Sumer S, Inkaya AC, Ozcimen S, Demir LS, Ural O, Arpaci A.
European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology.Eur J Clin Microbiol Infect Dis.2014 May 23. [Epub ahead of print]
Brucellosis is a chronic granulomatous infection and may present with various clinical manifestations. Brucellar spondylodiscitis symptoms are initially subtle and nonspecific. Annexin A2 (ANXA2) is involved in various biological functions, including osteoclast formation, bone resorption, and cell g
PMID 24853056

Japanese Journal

Radiolabeled apoptosis imaging agents for early detection of response to therapy

Scientific World Journal 2014, 732603, 2014
NAID 120005516433

The Involvement of Annexin Ⅱ in Resistance to UVB-Induced Cell Death and in the Increased Nucleotide Excision Repair Capacity of UV-Damaged DNA in Human Cells

Bioscience, biotechnology, and biochemistry 77(2), 307-311, 2013-02-23
NAID 10031164733

P-105

日本繁殖生物学会　講演要旨集 106(0), P-105-P-105, 2013
NAID 130005051108

「アネキシンII」

ANXA2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1W7B, 1XJL, 2HYU, 2HYV, 2HYW, 4DRW, 4FTG, 4HRH
Identifiers
Aliases	ANXA2, ANX2, ANX2L4, CAL1H, HEL-S-270, LIP2, LPC2, LPC2D, P36, PAP-IV, annexin A2
External IDs	OMIM: 151740 MGI: 88246 HomoloGene: 20857 GeneCards: ANXA2
Gene ontology
Molecular function	• phospholipase inhibitor activity; • calcium ion binding; • S100 protein binding; • phospholipase A2 inhibitor activity; • calcium-dependent protein binding; • protease binding; • receptor activator activity; • cytoskeletal protein binding; • Rab GTPase binding; • protein binding; • calcium-dependent phospholipid binding; • phosphatidylinositol-4,5-bisphosphate binding; • cadherin binding involved in cell-cell adhesion; • RNA binding; • identical protein binding;
Cellular component	• vesicle; • cytosol; • endosome; • membrane; • late endosome membrane; • extracellular matrix; • melanosome; • ruffle; • proteinaceous extracellular matrix; • plasma membrane; • lipid particle; • myelin sheath adaxonal region; • Schmidt-Lanterman incisure; • protein complex; • PCSK9-AnxA2 complex; • macropinosome; • basement membrane; • cell surface; • lysosomal membrane; • basolateral plasma membrane; • cell cortex; • midbody; • early endosome; • perinuclear region of cytoplasm; • sarcolemma; • extrinsic component of plasma membrane; • extracellular exosome; • nucleus; • cell-cell adherens junction; • extracellular region; • extracellular space; • azurophil granule lumen; • cytoplasm; • membrane raft;
Biological process	• negative regulation of low-density lipoprotein particle receptor catabolic process; • positive regulation of protein phosphorylation; • protein heterotetramerization; • fibrinolysis; • body fluid secretion; • collagen fibril organization; • positive regulation of fibroblast proliferation; • response to thyroid hormone; • protein targeting to plasma membrane; • positive regulation of binding; • positive regulation of vesicle fusion; • membrane raft assembly; • angiogenesis; • membrane budding; • osteoclast development; • cell-cell adhesion; • negative regulation of catalytic activity; • positive regulation of receptor recycling; • neutrophil degranulation; • positive regulation of low-density lipoprotein particle clearance; • positive regulation of low-density lipoprotein particle receptor binding; • positive regulation of low-density lipoprotein receptor activity; • positive regulation of receptor-mediated endocytosis involved in cholesterol transport; • negative regulation of development of symbiont involved in interaction with host; • catabolism by host of symbiont protein; • negative regulation by host of symbiont molecular function; • positive regulation of vacuole organization;
	Sources:Amigo / QuickGO
RNA expression pattern
	; ; ; ;
	More reference expression data
Orthologs
	302
	12306
	ENSG00000182718
	ENSMUSG00000032231
	P07355
	P07356
	NM_001002857; NM_001002858; NM_001136015; NM_004039
	NM_007585
	NP_001002857; NP_001002858; NP_001129487; NP_004030
	NP_031611.1; NP_031611
	Wikidata
View/Edit Human	View/Edit Mouse