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]


Further reading

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


update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = no
update_citations = yes

Wikimedia Foundation. 2010.

Игры ⚽ Нужно сделать НИР?

Look at other dictionaries:

  • Annexin A1 — (or Lipocortin I) is a human protein encoded by the ANXA1 gene. PBB Summary section title = summary text = Annexin I belongs to a family of Ca(2+) dependent phospholipid binding proteins that have a molecular weight of approximately 35,000 to… …   Wikipedia

  • Annexin A2 — is a pleiotropic protein, meaning that its function is dependent on place and time in the body. PBB Summary section title = summary text = This gene encodes a member of the annexin family. Members of this calcium dependent phospholipid binding… …   Wikipedia

  • Annexin A3 — Annexin A3, also known as ANXA3, is a human gene.cite web | title = Entrez Gene: ANXA3 annexin A3| url = Cmd=ShowDetailView TermToSearch=306| accessdate = ] PBB Summary section title = summary text …   Wikipedia

  • Annexin V — is the cause of a syndrome called the antiphospholipid antibody syndrome with abnormal blood clotting. The annexins are a family of proteins first described in 1990. All of the annexin proteins share the property of binding calcium and… …   Medical dictionary

  • Annexin 2 — is a protein shown to be 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… …   Wikipedia

  • Annexin — Pfam box Symbol = Annexin Name = width = 220 caption = Structure of human annexin III. Pfam= PF00191 InterPro= IPR001464 SMART= PROSITE= PDOC00195 SCOP = 2ran TCDB = 1.A.31 OPM family= 43 OPM protein= 1w3w PDB=PDB3|1n00A:14 79 PDB3|1dk5B:15 80… …   Wikipedia

  • Annexin II — Structure cristallographique modélisée de l annexine II Annexine II (autres noms : Annexin II, Annexin A2, Annexin 2, Lipocortin II, Calpactin I heavy chain, Chromobindin 8, p. 36, Placental anticoagulant protein IV). UniProtKB/Swiss… …   Wikipédia en Français

  • Annexin A5 affinity assay — Annexin A5 is a protein that binds in a calcium dependent manner to phosphatidylserine containing membrane surfaces. Cell surface expression of phosphatidylserine during cell deathApoptosis is a form of programmed cell death which is used by the… …   Wikipedia

  • annexin — noun Any of a group of cellular proteins found in all kingdoms (animal, plant and fungi) with the exception of the bacteria …   Wiktionary

  • annexin — an·nex·in (ə nekґsin) any of a family of Ca2+ dependent phospholipid binding proteins, which share a common primary structure in the C terminal region, four or eight repeats of an approximately 70 amino acid sequence. Proposed functions… …   Medical dictionary

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”