Annexin A5
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| Annexin A5
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| 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 | ||||||||||||||
| Symbol(s) | ANXA5; ANX5; ENX2; PP4 | |||||||||||||
| External IDs | OMIM: 131230 MGI: 106008 Homologene: 20312 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 308 | 11747 | ||||||||||||
| Ensembl | ENSG00000164111 | ENSMUSG00000027712 | ||||||||||||
| Uniprot | P08758 | Q3U5Q1 | ||||||||||||
| Refseq | NM_001154 (mRNA) NP_001145 (protein) | NM_009673 (mRNA) NP_033803 (protein) | ||||||||||||
| Location | 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 also by competing for phosphatidylserine binding sites. These properties have been found by in vitro experiments (in a test tube) and they have not been confirmed by experiments with laboratory animals.
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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]
References
- ↑ Koopman G, Reutelingsperger CP, Kuijten GAM et al. (1994). "Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis". Blood 84 (5): 1415–20. PMID 8068938.
- ↑ Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C (1995). "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. PMID 7622868.
Further reading
- Cederholm A, Frostegård J (2007). "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. PMID 17893975.
- Schlaepfer DD, Jones J, Haigler HT (1992). "Inhibition of protein kinase C by annexin V.". Biochemistry 31 (6): 1886-91. PMID 1310621.
- Huber R, Berendes R, Burger A, et al. (1992). "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. PMID 1311770.
- Kirsch T, Pfäffle M (1992). "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. PMID 1397263.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317-20. PMID 1602151.
- Tait JF, Frankenberry DA, Shiang R, et al. (1992). "Chromosomal localization of the human gene for annexin V (placental anticoagulant protein I) to 4q26----q28.". Cytogenet. Cell Genet. 57 (4): 187-92. PMID 1683830.
- Huber R, Römisch J, Paques EP (1991). "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). "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. PMID 2148156.
- Maurer-Fogy I, Reutelingsperger CP, Pieters J, et al. (1988). "Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein.". Eur. J. Biochem. 174 (4): 585-92. PMID 2455636.
- Rothhut B, Coméra C, Cortial S, et al. (1990). "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). "Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein.". Proc. Natl. Acad. Sci. U.S.A. 84 (17): 6078-82. PMID 2957692.
- Funakoshi T, Heimark RL, Hendrickson LE, et al. (1987). "Human placental anticoagulant protein: isolation and characterization.". Biochemistry 26 (17): 5572-8. PMID 2960376.
- Iwasaki A, Suda M, Nakao H, et al. (1988). "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). "Primary structure of human placental anticoagulant protein.". Biochemistry 26 (25): 8087-92. PMID 2964863.
- Kaplan R, Jaye M, Burgess WH, et al. (1988). "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). "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. PMID 2967495.
- Pepinsky RB, Tizard R, Mattaliano RJ, et al. (1988). "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). "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). "Annexin V: the key to understanding ion selectivity and voltage regulation?". Trends Biochem. Sci. 19 (7): 272-6. PMID 7519374.
- Fernández MP, Morgan RO, Fernández MR, Carcedo MT (1994). "The gene encoding human annexin V has a TATA-less promoter with a high G+C content.". Gene 149 (2): 253-60. PMID 7958998.
External links
Template:Membrane-protein-stubAcknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
