Annexin A5

Annexin A5

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.

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. [cite journal|author=Koopman G, Reutelingsperger CP, Kuijten GAM "et al."|year=1994|title=Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis|journal=Blood|volume=84|issue=5|pages=1415–20|pmid=8068938] [cite journal|author=Vermes I, Haanen C, Steffens-Nakken H, Reutelingsperger C|year=1995|title=A novel assay for apoptosis—flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V|journal=J Immunol Methods|volume=184|issue=1|pages=39|pmid=7622868|doi=10.1016/0022-1759(95)00072-I]

References

Further reading

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citations =
*cite journal | author=Cederholm A, Frostegård J |title=Annexin A5 as a novel player in prevention of atherothrombosis in SLE and in the general population. |journal=Ann. N. Y. Acad. Sci. |volume=1108 |issue= |pages= 96–103 |year= 2007 |pmid= 17893975 |doi=
*cite journal | author=Schlaepfer DD, Jones J, Haigler HT |title=Inhibition of protein kinase C by annexin V. |journal=Biochemistry |volume=31 |issue= 6 |pages= 1886–91 |year= 1992 |pmid= 1310621 |doi=
*cite journal | author=Huber R, Berendes R, Burger A, "et al." |title=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. |journal=J. Mol. Biol. |volume=223 |issue= 3 |pages= 683–704 |year= 1992 |pmid= 1311770 |doi=
*cite journal | author=Kirsch T, Pfäffle M |title=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. |journal=FEBS Lett. |volume=310 |issue= 2 |pages= 143–7 |year= 1992 |pmid= 1397263 |doi=
*cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=
*cite journal | author=Tait JF, Frankenberry DA, Shiang R, "et al." |title=Chromosomal localization of the human gene for annexin V (placental anticoagulant protein I) to 4q26----q28. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 4 |pages= 187–92 |year= 1992 |pmid= 1683830 |doi=
*cite journal | author=Huber R, Römisch J, Paques EP |title=The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. |journal=EMBO J. |volume=9 |issue= 12 |pages= 3867–74 |year= 1991 |pmid= 2147412 |doi=
*cite journal | author=Huber R, Schneider M, Mayr I, "et al." |title=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. |journal=FEBS Lett. |volume=275 |issue= 1-2 |pages= 15–21 |year= 1991 |pmid= 2148156 |doi=
*cite journal | author=Maurer-Fogy I, Reutelingsperger CP, Pieters J, "et al." |title=Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein. |journal=Eur. J. Biochem. |volume=174 |issue= 4 |pages= 585–92 |year= 1988 |pmid= 2455636 |doi=
*cite journal | author=Rothhut B, Coméra C, Cortial S, "et al." |title=A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation. |journal=Biochem. J. |volume=263 |issue= 3 |pages= 929–35 |year= 1990 |pmid= 2532007 |doi=
*cite journal | author=Schlaepfer DD, Mehlman T, Burgess WH, Haigler HT |title=Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 17 |pages= 6078–82 |year= 1987 |pmid= 2957692 |doi=
*cite journal | author=Funakoshi T, Heimark RL, Hendrickson LE, "et al." |title=Human placental anticoagulant protein: isolation and characterization. |journal=Biochemistry |volume=26 |issue= 17 |pages= 5572–8 |year= 1987 |pmid= 2960376 |doi=
*cite journal | author=Iwasaki A, Suda M, Nakao H, "et al." |title=Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1261–73 |year= 1988 |pmid= 2963810 |doi=
*cite journal | author=Funakoshi T, Hendrickson LE, McMullen BA, Fujikawa K |title=Primary structure of human placental anticoagulant protein. |journal=Biochemistry |volume=26 |issue= 25 |pages= 8087–92 |year= 1988 |pmid= 2964863 |doi=
*cite journal | author=Kaplan R, Jaye M, Burgess WH, "et al." |title=Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8037–43 |year= 1988 |pmid= 2967291 |doi=
*cite journal | author=Grundmann U, Abel KJ, Bohn H, "et al." |title=Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3708–12 |year= 1988 |pmid= 2967495 |doi=
*cite journal | author=Pepinsky RB, Tizard R, Mattaliano RJ, "et al." |title=Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10799–811 |year= 1988 |pmid= 2968983 |doi=
*cite journal | author=Ahn NG, Teller DC, Bienkowski MJ, "et al." |title=Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18657–63 |year= 1989 |pmid= 2974032 |doi=
*cite journal | author=Demange P, Voges D, Benz J, "et al." |title=Annexin V: the key to understanding ion selectivity and voltage regulation? |journal=Trends Biochem. Sci. |volume=19 |issue= 7 |pages= 272–6 |year= 1994 |pmid= 7519374 |doi=
*cite journal | author=Fernández MP, Morgan RO, Fernández MR, Carcedo MT |title=The gene encoding human annexin V has a TATA-less promoter with a high G+C content. |journal=Gene |volume=149 |issue= 2 |pages= 253–60 |year= 1994 |pmid= 7958998 |doi=

External links

*MeshName|Annexin+A5

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