関: annexin A5、placental anticoagulant protein I

WordNet

an addition that extends a main building (同)annexe, extension, wing
take (territory) as if by conquest; "Hitler annexed Lithuania"
attach to
the 22nd letter of the Roman alphabet (同)v

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verb / verso / 《話》very / velocity / volt[s] / volume / vide

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/09/06 14:11:43」(JST)

wiki en

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.

Pathology

Antibodies directed against annexin A5 are found in patients with a disease called the antiphospholipid syndrome (APS), a thrombophilic disease associated with autoantibodies against phospholipid compounds.

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.
Annexin A5 showed upregulation in papillary thyroid carcinoma.^[4]

Laboratory use

Annexin A5 is used as a non-quantitative probe to detect cells that have expressed phosphatidylserine (PS) on the cell surface, an event found in apoptosis as well as other forms of cell death.^[5]^[6]^[7] Platelets also expose PS and PE on their surface when activated, which serves as binding site for various coagulation factors.

The annexin A5 affinity assay typically uses a conjugate of annexin V and a fluorescent or enzymatic label, biotin or other tags, or a radioelement, in a suitable buffer (annexin V binding to aminophospholipids is Ca²⁺ dependent). The assay combines annexin V staining of PS and PE membrane events with the staining of DNA in the cell nucleus with propidium iodide (PI) or 7-Aminoactinomycin D (AAD-7), distinguishing viable cells from apoptotic cells and necrotic cells.^[8] Detection occurs by flow cytometry or a fluorescence microscope.

Interactions

Annexin A5 has been shown to interact with Kinase insert domain receptor^[9] and Integrin, beta 5.^[10]

References

^ "chibi.ubc.ca/Gemma/phenotypes.html?phenotypeUrlId=DOID_3083&geneId=7245".
^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Sofiadis A, Becker S, Hellman U, Hultin-Rosenberg L, Dinets A, Hulchiy M, Zedenius J, Wallin G, Foukakis T, Höög A, Auer G, Lehtiö J, Larsson C (Apr 2012). "Proteomic profiling of follicular and papillary thyroid tumors". European Journal of Endocrinology / European Federation of Endocrine Societies. 166 (4): 657–67. doi:10.1530/EJE-11-0856. PMID 22275472.
^ Meers P and Mealy T (1994). "Phospholipid determinants for annexin V binding sites and the role of tryptophan". Biochemistry. 33 (19): 5829–37. doi:10.1021/bi00185a022.
^ Koopman G, Reutelingsperger CP, Kuijten GA, Keehnen RM, Pals ST, van Oers MH (Sep 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 (Jul 1995). "A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V". Journal of Immunological Methods. 184 (1): 39–51. doi:10.1016/0022-1759(95)00072-I. PMID 7622868.
^ Annexin-FP488 fluorescent staining protocol at Interchim
^ Wen Y, Edelman JL, Kang T, Sachs G (May 1999). "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1". Biochemical and Biophysical Research Communications. 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. PMID 10329451.
^ Cardó-Vila M, Arap W, Pasqualini R (May 2003). "Alpha v beta 5 integrin-dependent programmed cell death triggered by a peptide mimic of annexin V". Molecular Cell. 11 (5): 1151–62. doi:10.1016/S1097-2765(03)00138-2. PMID 12769841.

External links

Annexin A5 at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 血管内皮機能および血栓溶解療法の基本的メカニズム vascular endothelial function and fundamental mechanisms of fibrinolysis thrombolysis
2. 抗リン脂質抗体症候群の病因 pathogenesis of the antiphospholipid syndrome
3. 抗リン脂質抗体症候群の診断 diagnosis of the antiphospholipid syndrome
4. 抗リン脂質抗体症候群の臨床症状 clinical manifestations of the antiphospholipid syndrome
5. 急性心臓同種移植拒絶反応：診断 acute cardiac allograft rejection diagnosis

English Journal

Role of Penaeus monodon hemocyte homeostasis associated protein (PmHHAP) in regulation of caspase-mediated apoptosis.

Apitanyasai K1, Amparyup P2, Charoensapsri W3, Senapin S3, Tassanakajon A4.
Developmental and comparative immunology.Dev Comp Immunol.2015 Nov;53(1):234-43. doi: 10.1016/j.dci.2015.06.004. Epub 2015 Jun 23.
The viral responsive protein, PmHHAP, plays an important role in the control of hemocyte homeostasis in shrimps during viral infection. In this study, we further investigate the role of PmHHAP in the regulation of hemocyte apoptosis. RNA interference (RNAi) mediated gene silencing was used to suppre
PMID 26111999

Xanthan gum protects rabbit articular chondrocytes against sodium nitroprusside-induced apoptosis in vitro.

Chen Q1, Mei X2, Han G3, Ling P4, Guo B2, Guo Y5, Shao H4, Wang G1, Cui Z2, Bai Y1, Xu F1.
Carbohydrate polymers.Carbohydr Polym.2015 Oct 20;131:363-9. doi: 10.1016/j.carbpol.2015.06.004. Epub 2015 Jun 8.
We have previously reported that intra-articular injection of xanthan gum (XG) could significantly ameliorate the degree of joint cartilage degradation and pain in experimental osteoarthritis (OA) model in vivo. In this present study, we evaluated the protective effect of XG against Sodium nitroprus
PMID 26256195

Inherited and acquired thrombophilia in Indian women experiencing unexplained recurrent pregnancy loss.

Patil R1, Ghosh K1, Vora S1, Shetty S2.
Blood cells, molecules & diseases.Blood Cells Mol Dis.2015 Oct;55(3):200-5. doi: 10.1016/j.bcmd.2015.06.008. Epub 2015 Jun 23.
The most frequently hypothesized cause of unexplained recurrent pregnancy loss (RPL) refers to a defective maternal haemostatic response leading to uteroplacental thrombosis. Approximately 20% women suffering from pregnancy loss (PL) are associated with autoimmune disorders and more than 50% remain
PMID 26227844

Japanese Journal

高速原子間力顕微鏡による生体試料のダイナミクス観察 (特集境界領域シンポジウム「膜解析の最前線 : 生体膜・膜タンパク質から模擬膜,ソフトマターまで)

内橋貴之
膜 = Membrane 39(5), 322-328, 2014-09
NAID 40020215607

Suppressive Effects of Irbesartan on Inflammation and Apoptosis in Atherosclerotic Plaques of apoE(-/-) Mice: Molecular Imaging with C-14-FDG and Tc-99m-Annexin A5

Zhao Yan,Watanabe Ayahisa,Zhao Songji,Kobayashi Tatsuo,Fukao Keita,Tanaka Yoshikazu,Nakano Toru,Yoshida Tetsuya,Takemoto Hiroshi,Tamaki Nagara,Kuge Yuji
Plos one 9(2), e89338, 2014-02-19
… Objectives: To investigate the effects of irbesartan on inflammation and apoptosis in atherosclerotic plaques by histochemical examination and molecular imaging using C-14-FDG and Tc-99m-annexin A5. … Molecular imaging using F-18-FDG and Tc-99m-annexin A5 is useful for evaluating inflammation and apoptosis in atherosclerotic plaques. … One week after the treatment, the mice were co-injected with C-14-FDG and Tc-99m-annexin A5, and cryostat sections of the aortic root were prepared. …
NAID 120005427743

P1-15-7 Annexin A4の発現は細胞内クロールイオン濃度を上昇させ,プラチナ耐性を誘導する(Group 15 卵巣腫瘍・基礎2,一般演題,公益社団法人日本産科婦人科学会第66回学術講演会)

森本晶子,松崎慎哉,高田友美,小林栄仁,木村敏啓,上田豊,吉野潔,藤田征巳,榎本隆之,仲哲治,木村正
日本産科婦人科學會雜誌 66(2), 511, 2014-02-01
NAID 110009811754

Related Pictures

★リンクテーブル★

リンク元	「アネキシンV」「placental anticoagulant protein I」
拡張検索	「annexin VII」「annexin VI」
関連記事	「Vd」「V」「annex」「annexin」

「アネキシンV」

ANXA5
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2XO3, 1ANW, 1ANX, 1AVH, 1AVR, 1HAK, 1HVD, 1HVE, 1HVF, 1HVG, 1SAV, 2XO2
Identifiers
Aliases	ANXA5, ANX5, ENX2, HEL-S-7, PP4, RPRGL3, annexin A5
External IDs	OMIM: 131230 MGI: 106008 HomoloGene: 20312 GeneCards: 308
Genetically Related Diseases
Disease Name	References
Gene ontology
Molecular function	• phospholipase inhibitor activity; • calcium ion binding; • calcium-transporting ATPase activity; • receptor tyrosine kinase binding; • peptide hormone binding; • protein binding; • calcium-dependent phospholipid binding; • phospholipid binding;
Cellular component	• cytoplasm; • axon terminus; • cytosol; • perikaryon; • cell projection; • membrane; • synaptic vesicle; • intercalated disc; • focal adhesion; • plasma membrane; • intracellular; • Q14325730; • endothelial microparticle; • neuronal cell body; • dendrite; • Z disc; • endoplasmic reticulum; • sarcolemma; • extracellular exosome; • external side of plasma membrane; • nucleus;
Biological process	• hemostasis; • cellular response to lead ion; • mitophagy in response to mitochondrial depolarization; • regulation of sperm motility; • negative regulation of blood coagulation; • negative regulation of coagulation; • response to thyroid hormone; • blood coagulation; • negative regulation of apoptotic process; • cellular response to gonadotropin-releasing hormone; • response to organic substance; • response to calcium ion; • calcium ion transmembrane transport; • positive regulation of apoptotic process; • negative regulation of prolactin secretion; • protein homooligomerization; • xenophagy; • signal transduction; • positive regulation of defense response to virus by host; • negative regulation of catalytic activity;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	308
	11747
	ENSG00000164111
	ENSMUSG00000027712
	P08758
	P48036
	NM_001154
	NM_009673
	NP_001145.1
	NP_033803.1
	Wikidata
View/Edit Human	View/Edit Mouse