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definitions - Annexin_A5

Annexin A5 (n.)

1.(MeSH)A protein of the annexin family isolated from human PLACENTA and other tissues. It inhibits cytosolic PHOSPHOLIPASE A2, and displays anticoagulant activity.

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Annexin A5

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Annexin A5

PDB rendering based on 1a8a.
Available structures
1a8a, 1a8b, 1anw, 1anx, 1avh, 1avr, 1bc0, 1bc1, 1bc3, 1bcw, 1bcy, 1bcz, 1g5n, 1hak, 1hvd, 1hve, 1hvf, 1hvg, 1n41, 1n42, 1n44, 1sav, 2ie6, 2ie7, 2ran
Identifiers
SymbolsANXA5; ANX5; ENX2; PP4
External IDsOMIM131230 MGI106008 HomoloGene20312 GeneCards: ANXA5 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez30811747
EnsemblENSG00000164111ENSMUSG00000027712
UniProtP08758Q3U5Q1
RefSeq (mRNA)NM_001154NM_009673
RefSeq (protein)NP_001145NP_033803
Location (UCSC)Chr 4:
122.81 - 122.84 Mb
Chr 3:
36.64 - 36.66 Mb
PubMed search[1][2]

Annexin A5 (or annexin V) is a cellular protein in the annexin group. The function of the protein is unknown, however annexin A5 has been proposed to play a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with prothrombin and also to inhibit the activity of phospholipase A1. These properties have been found by in vitro experiments.

Contents

Annexin A5 in pathology

Antibodies directed against annexin A5 are the cause of a syndrome called the antiphospholipid syndrome.

Annexin A5 forms a shield around negatively-charged phospholipid molecules. The formation of an annexin A5 shield blocks the entry of phospholipids into coagulation (clotting) reactions. In the antiphospholipid antibody syndrome, the formation of the shield is disrupted by antibodies. Without the shield, there is an increased quantity of phospholipid molecules on cell membranes, speeding up coagulation reactions and causing the blood-clotting characteristic of the antiphospholipid antibody syndrome.

Laboratory use of annexin A5

Annexin A5 is used as a probe in the annexin A5 affinity assay to detect cells that have expressed phosphatidylserine on the cell surface, a feature found in apoptosis as well as other forms of cell death.[1][2] Platelets also expose phosphatidylserine on their surface when activated, which serves as binding site for various coagulation factors.

Interactions

Annexin A5 has been shown to interact with Kinase insert domain receptor[3] and Integrin, beta 5.[4]

References

  1. Koopman G, Reutelingsperger CP, Kuijten GAM et al. (1994). [Expression error: Missing operand for > "Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis"]. Blood 84 (5): 1415–20. PMID 8068938. 
  2. Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C (1995). [Expression error: Missing operand for > "A novel assay for apoptosis—flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V"]. J Immunol Methods 184 (1): 39. doi:10.1016/0022-1759(95)00072-I. PMID 7622868. 
  3. Wen, Y; Edelman J L, Kang T, Sachs G (May. 1999). [Expression error: Missing operand for > "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1"]. Biochem. Biophys. Res. Commun. (UNITED STATES) 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. ISSN 0006-291X. PMID 10329451. 
  4. Cardó-Vila, Marina; Arap Wadih, Pasqualini Renata (May. 2003). [Expression error: Missing operand for > "Alpha v beta 5 integrin-dependent programmed cell death triggered by a peptide mimic of annexin V"]. Mol. Cell (United States) 11 (5): 1151–62. ISSN 1097-2765. PMID 12769841. 

Further reading

  • Cederholm A, Frostegård J (2007). [Expression error: Missing operand for > "Annexin A5 as a novel player in prevention of atherothrombosis in SLE and in the general population."]. Ann. N. Y. Acad. Sci. 1108: 96–103. doi:10.1196/annals.1422.011. PMID 17893975. 
  • Schlaepfer DD, Jones J, Haigler HT (1992). [Expression error: Missing operand for > "Inhibition of protein kinase C by annexin V."]. Biochemistry 31 (6): 1886–91. doi:10.1021/bi00121a043. PMID 1310621. 
  • Huber R, Berendes R, Burger A, et al. (1992). [Expression error: Missing operand for > "Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins."]. J. Mol. Biol. 223 (3): 683–704. doi:10.1016/0022-2836(92)90984-R. PMID 1311770. 
  • Kirsch T, Pfäffle M (1992). [Expression error: Missing operand for > "Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins."]. FEBS Lett. 310 (2): 143–7. doi:10.1016/0014-5793(92)81316-E. PMID 1397263. 
  • Dawson SJ, White LA (1992). [Expression error: Missing operand for > "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin."]. J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151. 
  • Tait JF, Frankenberry DA, Shiang R, et al. (1992). [Expression error: Missing operand for > "Chromosomal localization of the human gene for annexin V (placental anticoagulant protein I) to 4q26----q28."]. Cytogenet. Cell Genet. 57 (4): 187–92. doi:10.1159/000133143. PMID 1683830. 
  • Huber R, Römisch J, Paques EP (1991). [Expression error: Missing operand for > "The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes."]. Embo J. 9 (12): 3867–74. PMID 2147412. 
  • Huber R, Schneider M, Mayr I, et al. (1991). [Expression error: Missing operand for > "The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity."]. FEBS Lett. 275 (1-2): 15–21. doi:10.1016/0014-5793(90)81428-Q. PMID 2148156. 
  • Maurer-Fogy I, Reutelingsperger CP, Pieters J, et al. (1988). [Expression error: Missing operand for > "Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein."]. Eur. J. Biochem. 174 (4): 585–92. doi:10.1111/j.1432-1033.1988.tb14139.x. PMID 2455636. 
  • Rothhut B, Coméra C, Cortial S, et al. (1990). [Expression error: Missing operand for > "A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation."]. Biochem. J. 263 (3): 929–35. PMID 2532007. 
  • Schlaepfer DD, Mehlman T, Burgess WH, Haigler HT (1987). [Expression error: Missing operand for > "Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein."]. Proc. Natl. Acad. Sci. U.S.A. 84 (17): 6078–82. doi:10.1073/pnas.84.17.6078. PMID 2957692. 
  • Funakoshi T, Heimark RL, Hendrickson LE, et al. (1987). [Expression error: Missing operand for > "Human placental anticoagulant protein: isolation and characterization."]. Biochemistry 26 (17): 5572–8. doi:10.1021/bi00391a053. PMID 2960376. 
  • Iwasaki A, Suda M, Nakao H, et al. (1988). [Expression error: Missing operand for > "Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein."]. J. Biochem. 102 (5): 1261–73. PMID 2963810. 
  • Funakoshi T, Hendrickson LE, McMullen BA, Fujikawa K (1988). [Expression error: Missing operand for > "Primary structure of human placental anticoagulant protein."]. Biochemistry 26 (25): 8087–92. doi:10.1021/bi00399a011. PMID 2964863. 
  • Kaplan R, Jaye M, Burgess WH, et al. (1988). [Expression error: Missing operand for > "Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein."]. J. Biol. Chem. 263 (17): 8037–43. PMID 2967291. 
  • Grundmann U, Abel KJ, Bohn H, et al. (1988). [Expression error: Missing operand for > "Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family."]. Proc. Natl. Acad. Sci. U.S.A. 85 (11): 3708–12. doi:10.1073/pnas.85.11.3708. PMID 2967495. 
  • Pepinsky RB, Tizard R, Mattaliano RJ, et al. (1988). [Expression error: Missing operand for > "Five distinct calcium and phospholipid binding proteins share homology with lipocortin I."]. J. Biol. Chem. 263 (22): 10799–811. PMID 2968983. 
  • Ahn NG, Teller DC, Bienkowski MJ, et al. (1989). [Expression error: Missing operand for > "Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor."]. J. Biol. Chem. 263 (35): 18657–63. PMID 2974032. 
  • Demange P, Voges D, Benz J, et al. (1994). [Expression error: Missing operand for > "Annexin V: the key to understanding ion selectivity and voltage regulation?"]. Trends Biochem. Sci. 19 (7): 272–6. doi:10.1016/0968-0004(94)90002-7. PMID 7519374. 
  • Fernández MP, Morgan RO, Fernández MR, Carcedo MT (1994). [Expression error: Missing operand for > "The gene encoding human annexin V has a TATA-less promoter with a high G+C content."]. Gene 149 (2): 253–60. doi:10.1016/0378-1119(94)90157-0. PMID 7958998. 

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