Annexin A2
From Wikipedia the free encyclopedia
Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.[5]
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[edit]
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.[6]
Function[edit]
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.[6] Epigenetic regulation of Annexin A2 has been identified as a key determinant of mesenchymal transformation in brain tumors.[7] Maternal deficiency of the ANXA2 gene contributes to shallow decidual invasion by placental cytotrophoblast cells. These findings highlight the maternal contribution to the pathogenesis of severe preeclampsia.[8]
Annexin A2 has been proposed to function inside the cell in sorting of endosomes and outside the cell in anticoagulant reactions.
Interactions[edit]
Annexin A2 has been shown to interact with Prohibitin,[9] CEACAM1,[10] S100A10,[11][12] PCNA,[13] complement Factor H,[14] and a number of viral factors including the HPV16 minor capsid protein L2.[15][16]
See also[edit]
References[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000182718 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032231 – 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.
- ^ Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (November 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): 28696–28701. doi:10.1016/S0021-9258(19)61961-7. PMID 7961821.
- ^ a b "Entrez Gene: ANXA2 annexin A2".
- ^ Kling T, Ferrarese R, Ó hAilín D, Johansson P, Heiland DH, Dai F, et al. (October 2016). "Integrative Modeling Reveals Annexin A2-mediated Epigenetic Control of Mesenchymal Glioblastoma". eBioMedicine. 12: 72–85. doi:10.1016/j.ebiom.2016.08.050. PMC 5078587. PMID 27667176.
- ^ Ng SW, Norwitz GA, Pavlicev M, Tilburgs T, Simón C, Norwitz ER (June 2020). "Endometrial Decidualization: The Primary Driver of Pregnancy Health". International Journal of Molecular Sciences. 21 (11): 4092. doi:10.3390/ijms21114092. PMC 7312091. PMID 32521725.
- ^ Bacher S, Achatz G, Schmitz ML, Lamers MC (December 2002). "Prohibitin and prohibitone are contained in high-molecular weight complexes and interact with alpha-actinin and annexin A2". Biochimie. 84 (12): 1207–1220. doi:10.1016/S0300-9084(02)00027-5. PMID 12628297.
- ^ Kirshner J, Schumann D, Shively JE (December 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): 50338–50345. doi:10.1074/jbc.M309115200. PMID 14522961.
- ^ Réty S, Sopkova J, Renouard M, Osterloh D, Gerke V, Tabaries S, et al. (January 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. S2CID 26400923.
- ^ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R, Hajjar KA (July 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". The Journal of Biological Chemistry. 283 (28): 19192–19200. doi:10.1074/jbc.M800100200. PMC 2443646. PMID 18434302.
- ^ Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (October 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): 40362–40367. doi:10.1074/jbc.M206194200. PMID 12171929.
- ^ Leffler J, Herbert AP, Norström E, Schmidt CQ, Barlow PN, Blom AM, Martin M (February 2010). "Annexin-II, DNA, and histones serve as factor H ligands on the surface of apoptotic cells". The Journal of Biological Chemistry. 285 (6): 3766–3776. doi:10.1074/jbc.M109.045427. PMC 2823518. PMID 19951950.
- ^ Woodham AW, Da Silva DM, Skeate JG, Raff AB, Ambroso MR, Brand HE, et al. (2012). "The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection". PLOS ONE. 7 (8): e43519. Bibcode:2012PLoSO...743519W. doi:10.1371/journal.pone.0043519. PMC 3425544. PMID 22927980.
- ^ Woodham AW, Raff AB, Raff LM, Da Silva DM, Yan L, Skeate JG, et al. (May 2014). "Inhibition of Langerhans cell maturation by human papillomavirus type 16: a novel role for the annexin A2 heterotetramer in immune suppression". Journal of Immunology. 192 (10): 4748–4757. doi:10.4049/jimmunol.1303190. PMC 4019435. PMID 24719459.
Further reading[edit]
- Kwon M, MacLeod TJ, Zhang Y, Waisman DM (January 2005). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors". Frontiers in Bioscience. 10 (1–3): 300–325. doi:10.2741/1529. PMID 15574370.
- Babiychuk EB, Draeger A (June 2006). "Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement?". Biochemical Society Transactions. 34 (Pt 3): 374–376. doi:10.1042/BST0340374. PMID 16709165.
- Bohn E, Gerke V, Kresse H, Löffler BM, Kunze H (January 1992). "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase". FEBS Letters. 296 (3): 237–240. doi:10.1016/0014-5793(92)80294-Q. PMID 1531641. S2CID 19633878.
- Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–320. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Jindal HK, Chaney WG, Anderson CW, Davis RG, Vishwanatha JK (March 1991). "The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha". The Journal of Biological Chemistry. 266 (8): 5169–5176. doi:10.1016/S0021-9258(19)67770-7. PMID 1825830.
- Filipek A, Gerke V, Weber K, Kuźnicki J (February 1991). "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography". European Journal of Biochemistry. 195 (3): 795–800. doi:10.1111/j.1432-1033.1991.tb15768.x. PMID 1999197.
- Becker T, Weber K, Johnsson N (December 1990). "Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11". The EMBO Journal. 9 (13): 4207–4213. doi:10.1002/j.1460-2075.1990.tb07868.x. PMC 552202. PMID 2148288.
- Spano F, Raugei G, Palla E, Colella C, Melli M (November 1990). "Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication". Gene. 95 (2): 243–251. doi:10.1016/0378-1119(90)90367-Z. PMID 2174397.
- Johnsson N, Johnsson K, Weber K (August 1988). "A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins". FEBS Letters. 236 (1): 201–204. doi:10.1016/0014-5793(88)80314-4. PMID 2456953. S2CID 38734898.
- Gould KL, Woodgett JR, Isacke CM, Hunter T (July 1986). "The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo". Molecular and Cellular Biology. 6 (7): 2738–2744. doi:10.1128/mcb.6.7.2738. PMC 367834. PMID 2946940.
- Huebner K, Cannizzaro LA, Frey AZ, Hecht BK, Hecht F, Croce CM, Wallner BP (May 1988). "Chromosomal localization of the human genes for lipocortin I and lipocortin II". Oncogene Research. 2 (4): 299–310. PMID 2969496.
- Huang KS, Wallner BP, Mattaliano RJ, Tizard R, Burne C, Frey A, et al. (July 1986). "Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase". Cell. 46 (2): 191–199. doi:10.1016/0092-8674(86)90736-1. PMID 3013422. S2CID 24557024.
- Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J (March 1994). "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells". The Journal of Biological Chemistry. 269 (12): 9019–9023. doi:10.1016/S0021-9258(17)37070-9. PMID 7510700.
- Chung CY, Erickson HP (July 1994). "Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C". The Journal of Cell Biology. 126 (2): 539–548. doi:10.1083/jcb.126.2.539. PMC 2200039. PMID 7518469.
- Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, et al. (December 1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–250. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
- Richard I, Broux O, Chiannilkulchai N, Fougerousse F, Allamand V, Bourg N, et al. (October 1994). "Regional localization of human chromosome 15 loci". Genomics. 23 (3): 619–627. doi:10.1006/geno.1994.1550. PMID 7851890.
- Takahashi S, Reddy SV, Chirgwin JM, Devlin R, Haipek C, Anderson J, Roodman GD (November 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): 28696–28701. doi:10.1016/S0021-9258(19)61961-7. PMID 7961821.
- Hyatt SL, Liao L, Chapline C, Jaken S (February 1994). "Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells". Biochemistry. 33 (5): 1223–1228. doi:10.1021/bi00171a023. PMID 8110754.
- Wright JF, Kurosky A, Wasi S (February 1994). "An endothelial cell-surface form of annexin II binds human cytomegalovirus". Biochemical and Biophysical Research Communications. 198 (3): 983–989. doi:10.1006/bbrc.1994.1140. PMID 8117306.
- Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
External links[edit]
- Annexin+A2 at the U.S. 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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