tissue factor

組織因子、TF、factor III、CD142

WordNet

1. coagulation factor that is converted to an enzyme that converts prothrombin to thrombin in a reaction that depends on calcium ions and other coagulation factors (同)factor_X
2. be a contributing factor; "make things factor into a companys profitability"
3. any of the numbers (or symbols) that form a product when multiplied together
4. an independent variable in statistics
5. anything that contributes causally to a result; "a number of factors determined the outcome"
6. consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
7. resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
8. an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
9. a concept whose truth can be proved; "scientific hypotheses are not facts"
10. a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
11. a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"
12. a soft thin (usually translucent) paper (同)tissue_paper
13. part of an organism consisting of an aggregate of cells having a similar structure and function

PrepTutorEJDIC

1. (…の)『要因』,(…を生み出す)要素《+『in』+『名』(do『ing』)》 / 囲数,約数 / 代理人,《おもに英》仲買人 / =factorize
2. 〈C〉『事実』,実際にある(あった)事 / 〈U〉真相,真実(truth) / 《the~》(法律用語で)犯行
3. 〈U〉〈C〉(生物体の)『組織』 / 〈U〉〈C〉『薄織物』 / 〈U〉〈C〉水を吸収する柔らかな薄紙 / 〈C〉カーボンコピー用薄紙 / 〈C〉《a ~》(…を)織り交ぜて作ったもの《+of+名》 / =tissue paper

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/10/09 17:00:01」(JST)

wiki en

[Wiki en表示]

Coagulation factor III (thromboplastin, tissue factor)
PDB rendering based on 1ahw.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AHW, 1BOY, 1DAN, 1FAK, 1J9C, 1JPS, 1NL8, 1O5D, 1TFH, 1UJ3, 1W0Y, 1W2K, 1WQV, 1WSS, 1WTG, 1WUN, 1WV7, 1Z6J, 2A2Q, 2AEI, 2AER, 2B7D, 2B8O, 2C4F, 2CEF, 2CEH, 2CEZ, 2CFJ, 2EC9, 2F9B, 2FIR, 2FLB, 2FLR, 2HFT, 2PUQ, 2ZP0, 2ZWL, 2ZZU, 3ELA, 3TH2, 3TH3, 3TH4, 4IBL
Identifiers
Symbols	F3 ; CD142; TF; TFA
External IDs	OMIM: 134390 MGI: 88381 HomoloGene: 1511 ChEMBL: 4081 GeneCards: F3 Gene
Gene ontology Molecular function • protease binding • protein binding • phospholipid binding Cellular component • extracellular space • plasma membrane • cell surface • integral component of membrane • extracellular matrix • intrinsic component of external side of plasma membrane • extracellular vesicular exosome Biological process • positive regulation of endothelial cell proliferation • activation of plasma proteins involved in acute inflammatory response • activation of blood coagulation via clotting cascade • activation of cysteine-type endopeptidase activity involved in apoptotic process • blood coagulation • blood coagulation, extrinsic pathway • positive regulation of platelet-derived growth factor receptor signaling pathway • positive regulation of cell migration • positive regulation of angiogenesis • positive regulation of positive chemotaxis • positive regulation of protein kinase B signaling Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2152	14066
Ensembl	ENSG00000117525	ENSMUSG00000028128
UniProt	P13726	P20352
RefSeq (mRNA)	NM_001178096	NM_010171
RefSeq (protein)	NP_001171567	NP_034301
Location (UCSC)	Chr 1: 94.99 – 95.01 Mb	Chr 3: 121.72 – 121.74 Mb
PubMed search	[1]	[2]

Tissue factor, also called platelet tissue factor, factor III, thromboplastin, or CD142 is a protein present in subendothelial tissue and leukocytes necessary for the initiation of thrombin formation from the zymogen prothrombin.

This gene encodes coagulation factor III which is a cell surface glycoprotein. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. The resulting complex provides a catalytic event that is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Unlike the other cofactors of these protease cascades, which circulate as nonfunctional precursors, this factor is a potent initiator that is fully functional when expressed on cell surfaces. There are 3 distinct domains of this factor: extracellular, transmembrane, and cytoplasmic. This protein is the only one in the coagulation pathway for which a congenital deficiency has not been described. In addition to the membrane-bound tissue factor, soluble form of tissue factor was also found which results from alternatively spliced tissue factor mRNA transcripts, in which exon 5 is absent and exon 4 is spliced directly to exon 6.

Structure

The protein structure of TF consists of three domains:

1. a domain which is located outside the cell, this domain binds factor VIIa. The binding of VIIa to TF occurs via protein-protein interactions by both molecules.
   1. Factor VIIa is a protein which consists of several domains. One of these domains, the carboxylated GLA domain, binds in the presence of calcium to negatively charged phospholipids. Binding of VIIa to negatively charged phospholipids greatly enhances the protein-protein binding of VIIa to TF.
2. a domain which crosses the hydrophobic membrane.
3. a domain of 21 amino acids length inside the cell which is involved in the signaling function of TF.

Functions

Coagulation

TF is the cell surface receptor for the serine protease factor VIIa.

The best known function of tissue factor is its role in blood coagulation. The complex of TF with factor VIIa activates factor IX and catalyzes the conversion of the inactive protease factor X into the active protease factor Xa.

Together with factor VIIa, tissue factor forms the tissue factor or extrinsic pathway of coagulation. This is opposed to the intrinsic (amplification) pathway which involves both activated factor IX and factor VIII. Both pathways lead to the activation of factor X (the common pathway) which combines with activated factor V in the presence of calcium and phospholipid to produce thrombin (thromboplastin activity).

The coagulation cascade.

Cytokine

TF is related to a protein family known as the cytokine receptor class II family. The members of this receptor family are activated by cytokines. Cytokines are small proteins that can influence the behavior of white blood cells. Binding of VIIa to TF has also been found to start signaling processes inside the cell. The signaling function of TF/VIIa plays a role in angiogenesis and apoptosis.

Location

Some cells release TF in response to blood vessel damage (see next paragraph) and some do only in response to inflammatory mediators (endothelial cells/macrophages).

TF is expressed by cells which are normally not exposed to flowing blood such as sub-endothelial cells (e.g. smooth muscle cells) and cells surrounding blood vessels (e.g. fibroblasts). This can change when the blood vessel is damaged by for example physical injury or rupture of atherosclerotic plaques. Exposure of TF expressing cells during injury allows the complex formation of TF with factor VII. Factor VII and TF form an equal molar complex in the presence of calcium ions and this leads to the activation of factor VII on a membrane surface.

The inner surface of the blood vessel consists of endothelial cells. Endothelial cells do not express TF except when they are exposed to inflammatory molecules such as tumor necrosis factor-alpha (TNF-alpha). Another cell type that expresses TF on the cell surface in inflammatory conditions is the monocyte (a white blood cell).

Thromboplastin

Historically, thromboplastin was a lab reagent, usually derived from placental sources, used to assay prothrombin times (PT time). Thromboplastin, by itself, could activate the extrinsic coagulation pathway. When manipulated in the laboratory, a derivative could be created called partial thromboplastin. Partial thromboplastin was used to measure the intrinsic pathway. This test is called the aPTT, or activated partial thromboplastin time. It was not until much later that the subcomponents of thromboplastin and partial thromboplastin were identified. Thromboplastin is the combination of both phospholipids and tissue factor, both needed in the activation of the extrinsic pathway, and partial thromboplastin is just phospholipids without tissue factor. Tissue factor is not needed to activate the intrinsic pathway.

Additional images

• Tissue factor

• Blood plasma after the addition of tissue factor

Interactions

Tissue factor has been shown to interact with Factor VII.

References

Further reading

• Gouault-Helimann M, Josso F (1980). "[Initiation in vivo of blood coagulation. The role of white blood cells and tissue factor (author's transl)]". La Nouvelle presse médicale 8 (40): 3249–53. PMID 392457. 
• Mackman N (1995). "Regulation of the tissue factor gene.". FASEB J. 9 (10): 883–9. PMID 7615158. 
• McVey JH (2000). "Tissue factor pathway.". Baillieres Best Pract. Res. Clin. Haematol. 12 (3): 361–72. PMID 10856975. 
• Konigsberg W, Kirchhofer D, Riederer MA, Nemerson Y (2002). "The TF:VIIa complex: clinical significance, structure-function relationships and its role in signaling and metastasis.". Thromb. Haemost. 86 (3): 757–71. PMID 11583305. 
• Versteeg HH, Peppelenbosch MP, Spek CA (2002). "The pleiotropic effects of tissue factor: a possible role for factor VIIa-induced intracellular signalling?". Thromb. Haemost. 86 (6): 1353–9. PMID 11776298. 
• Fernandez PM, Rickles FR (2003). "Tissue factor and angiogenesis in cancer.". Curr. Opin. Hematol. 9 (5): 401–6. doi:10.1097/00062752-200209000-00003. PMID 12172458. 
• Golino P (2003). "The inhibitors of the tissue factor:factor VII pathway.". Thromb. Res. 106 (3): V257–65. doi:10.1016/S0049-3848(02)00079-8. PMID 12356487. 
• Engelmann B, Luther T, Müller I (2004). "Intravascular tissue factor pathway--a model for rapid initiation of coagulation within the blood vessel.". Thromb. Haemost. 89 (1): 3–8. doi:10.1267/THRO03010003 (inactive 2010-06-23). PMID 12540946. 
• Morrissey JH (2004). "Tissue factor: in at the start...and the finish?". J. Thromb. Haemost. 1 (5): 878–80. doi:10.1046/j.1538-7836.2003.00219.x. PMID 12871349. 
• Yu JL, May L, Klement P et al. (2004). "Oncogenes as regulators of tissue factor expression in cancer: implications for tumor angiogenesis and anti-cancer therapy". Semin. Thromb. Hemost. 30 (1): 21–30. doi:10.1055/s-2004-822968. PMID 15034795. 
• Fernandez PM, Patierno SR, Rickles FR (2004). "Tissue factor and fibrin in tumor angiogenesis". Semin. Thromb. Hemost. 30 (1): 31–44. doi:10.1055/s-2004-822969. PMID 15034796. 
• Mackman N (2004). "Role of tissue factor in hemostasis, thrombosis, and vascular development". Arterioscler. Thromb. Vasc. Biol. 24 (6): 1015–22. doi:10.1161/01.ATV.0000130465.23430.74. PMID 15117736. 
• Belting M, Ahamed J, Ruf W (2005). "Signaling of the tissue factor coagulation pathway in angiogenesis and cancer". Arterioscler. Thromb. Vasc. Biol. 25 (8): 1545–50. doi:10.1161/01.ATV.0000171155.05809.bf. PMID 15905465. 
• Engelmann B (2007). "Initiation of coagulation by tissue factor carriers in blood". Blood Cells Mol. Dis. 36 (2): 188–90. doi:10.1016/j.bcmd.2005.12.020. PMID 16473535. 
• Furie B, Furie BC (2007). "Cancer-associated thrombosis". Blood Cells Mol. Dis. 36 (2): 177–81. doi:10.1016/j.bcmd.2005.12.018. PMID 16490369. 
• Mackman N (2007). "Alternatively spliced tissue factor - one cut too many?". Thromb. Haemost. 97 (1): 5–8. doi:10.1160/th06-11. PMID 17200762. 
• Wiiger MT, Prydz H (2007). "The changing faces of tissue factor biology. A personal tribute to the understanding of the "extrinsic coagulation activation"". Thromb. Haemost. 98 (1): 38–42. doi:10.1160/th07-04-0289. PMID 17597988. 

• Online 'Mendelian Inheritance in Man' (OMIM) 134390
• PDB Molecule of the Month pdb75_1 - March 2006

See also

• hemostasis

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. 止血の概要 overview of hemostasis
• 2. 凝固検査の臨床使用 clinical use of coagulation tests
• 3. 悪性腫瘍に関連した凝固亢進状態の病因 pathogenesis of the hypercoagulable state associated with malignancy
• 4. 敗血症に対する治験剤および無効剤 investigational and ineffective therapies for sepsis
• 5. 成人における播種性血管内凝固の臨床的特徴、診断、および治療 clinical features diagnosis and treatment of disseminated intravascular coagulation in adults

English Journal

• Resveratrol Restores Sirtuin 1 (SIRT1) Activity and Pyruvate Dehydrogenase Kinase 1 (PDK1) Expression after Hemorrhagic Injury in a Rat Model.

• Jian B, Yang S, Chaudry IH, Raju R.Author information Department of Surgery, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.AbstractSevere hemorrhage leads to decreased blood flow to tissues resulting in decreased oxygen and nutrient availability affecting mitochondrial function. A mitoscriptome profiling study demonstrated alteration in several genes related to mitochondria, consistent with the mitochondrial functional decline observed after trauma hemorrhage (T-H). Our experiments led to the identification of sirtuin 1 (SIRT1) as a potential target in T-H. Administration of resveratrol (a naturally occurring polyphenol and activator of SIRT1) after T-H improved left ventricular function and tissue ATP levels. Our hypothesis was that mitochondrial function after T-H depends on SIRT1 activity. In this study, we evaluated the activity of SIRT1, a mitochondrial functional modulator, and the mitochondrial-glycolytic balance after T-H. We determined the changes in protein levels of pyruvate dehydrogenase kinase (PDK)-1 and nuclear c-Myc, peroxisome proliferator-activated receptor-γ coactivator (PGC)-1α and NF-E2-related factor (NRF)2 after T-H and after treatment with resveratrol or a combination of sirtinol (a SIRT1 inhibitor) and resveratrol. We have also tested the activity of mitochondrial complex 1. SIRT1 enzyme activity was significantly decreased after T-H, whereas resveratrol treatment restored the activity. We found elevated PDK1 and c-Myc levels and decreased PGC-1α, NRF2 and mitochondrial complex I activity after T-H. The reduced SIRT1 activity after T-H may be related to declining mitochondrial function, since resveratrol was able to reinstate SIRT1 activity and mitochondrial function. The elevated level of PDK1 (an inhibitor of pyruvate dehydrogenase complex) after T-H indicates a possible shift in cellular energetics from mitochondria to glycolysis. In conclusion, SIRT1 modulation alters left ventricular function after T-H through regulation of cellular energetics.
• Molecular medicine (Cambridge, Mass.).Mol Med.2014 Dec 24;20(1):10-6. doi: 10.2119/molmed.2013.00077.
• Severe hemorrhage leads to decreased blood flow to tissues resulting in decreased oxygen and nutrient availability affecting mitochondrial function. A mitoscriptome profiling study demonstrated alteration in several genes related to mitochondria, consistent with the mitochondrial functional decline
• PMID 24395567

• Toxicity and bio-accumulation of inhaled cerium oxide nanoparticles in CD1 mice.

• Aalapati S1, Ganapathy S, Manapuram S, Anumolu G, Prakya BM.Author information 1Department of Toxicology, International Institute of Biotechnology and Toxicology [IIBAT] , Chennai , India.AbstractMale CD1 mice were subjected to nose-inhalation exposure of CeO2 nanoparticles (NPs) for 0, 7, 14 or 28 days with 14 or 28 days of recovery time at an aerosol concentration of 2 mg/m(3). Markers of lung injury and pro-inflammatory cytokines (interleukin-1beta, tumour necrosis factor-alpha, interleukin-6 and macrophage inflammatory protein-2) in bronchoalveolar lavage fluid (BALF), oxidative stress in lungs, bio-accumulation, and histopathology of pulmonary and extrapulmonary tissues were assessed. BALF analysis revealed the induction of pulmonary inflammation, as evident by an increase in the influx of neutrophils with a significant secretion of pro-inflammatory cytokines that lead to generation of oxidative stress and cytotoxicity, as is evident by induction of lipid peroxidation, depletion of glutathione and increased BALF lactate dehydrogenase and protein. The histopathological examination revealed that these inhaled CeO2 NPs were located all over the pulmonary parenchyma, inducing a severe, chronic, active inflammatory response characterised by necrosis, proteinosis, fibrosis and well-formed discrete granulomas in the pulmonary tissue and tubular degeneration leading to coagulative necrosis in kidneys. Inductively coupled plasma optical emission spectrometer results showed a significant bio-accumulation of these particles in the pulmonary and extrapulmonary tissues, even after one month of post-inhalation exposure. Together, these findings suggest that inhalation exposure of CeO2 NPs can induce pulmonary and extrapulmonary toxicity.
• Nanotoxicology.Nanotoxicology.2014 Nov;8(7):786-98. doi: 10.3109/17435390.2013.829877. Epub 2013 Aug 22.
• Male CD1 mice were subjected to nose-inhalation exposure of CeO2 nanoparticles (NPs) for 0, 7, 14 or 28 days with 14 or 28 days of recovery time at an aerosol concentration of 2 mg/m(3). Markers of lung injury and pro-inflammatory cytokines (interleukin-1beta, tumour necrosis factor-alpha, interleuk
• PMID 23914771

• A murine model of airway fibrosis induced by repeated naphthalene exposure.

• Aoshiba K1, Tsuji T2, Itoh M2, Semba S2, Yamaguchi K3, Nakamura H2, Watanabe H2.Author information 1Department of Respiratory Medicine, Tokyo Medical University Ibaraki Medical Center, Japan. Electronic address: kaoshiba@tokyo-med.ac.jp.2Department of Respiratory Medicine, Tokyo Medical University Ibaraki Medical Center, Japan.3Comprehensive and Internal Medicine, Tokyo Women's Medical University Medical Center East, Japan.AbstractThe airway epithelium serves as a biological barrier essential for host defense against inhaled pollutants. While chronic epithelial injury, commonly associated with chronic obstructive pulmonary disease and bronchiolitis obliterans syndrome, often results in airway fibrosis, limited animal models of airway fibrosis have been established. Club cells (Clara cells) in the small airways represent an important population of epithelial progenitor cells and also the principal site of localization of the cytochrome P-450 monooxygenase system, which metabolically activates xenobiotic chemicals such as naphthalene by converting them to toxic epoxide intermediates. We hypothesized that repeated exposure to naphthalene may cause prolonged loss of club cells, triggering aberrant local epithelial repair mechanisms that lead to peribronchial fibrosis. We administered intraperitoneal injections of naphthalene to C57/BL6J mice once a week for 14 consecutive weeks. Repeated club cell injury caused by naphthalene triggered regional hyperproliferation of epithelial progenitor cells, while other regions remained denuded or squamated, resulting in fibroblast proliferation and peribronchial collagen deposition associated with upregulation of the fibrogenic cytokines transforming growth factor-β and connective tissue growth factor. The total collagen content of the lung assessed by measurement of the hydroxyproline content was also increased after repeated exposure to naphthalene. These results lend support to the relevance of repeated injury of airway epithelial cells as a trigger for resting fibroblast proliferation and airway fibrosis. This model of airway fibrosis is simple and easy to reproduce, and may be expected to advance our understanding of the pathogenesis and potential treatment of airway fibrotic disorders.
• Experimental and toxicologic pathology : official journal of the Gesellschaft für Toxikologische Pathologie.Exp Toxicol Pathol.2014 Jul;66(4):169-77. doi: 10.1016/j.etp.2014.01.001. Epub 2014 Jan 28.
• The airway epithelium serves as a biological barrier essential for host defense against inhaled pollutants. While chronic epithelial injury, commonly associated with chronic obstructive pulmonary disease and bronchiolitis obliterans syndrome, often results in airway fibrosis, limited animal models o
• PMID 24480153

Japanese Journal

• The Use of Bone Marrow Stromal Cells (Bone Marrow-Derived Multipotent Mesenchymal Stromal Cells) for Alveolar Bone Tissue Engineering: Basic Science to Clinical Translation

• Kagami Hideaki,Agata Hideki,Inoue Minoru,Asahina Izumi,Tojo Arinobu,Yamashita Naohide,Imai Kohzoh
• Tissue
• … Bone tissue engineering is a promising field of regenerative medicine in which cultured cells, scaffolds, and osteogenic inductive signals are used to regenerate bone. … Human bone marrow stromal cells (BMSCs) are the most commonly used cell source for bone tissue engineering. … Application of basic fibroblast growth factor helped to maintain the in vivo osteogenic ability of BMSCs. …
• NAID 120005447068

• Ki-67 is a strong prognostic marker of non-small cell lung cancer when tissue heterogeneity is considered

• Tabata Kazuhiro,Tanaka Tomonori,Hayashi Tomayoshi,Hori Takashi,Nunomura Sayuri,Yonezawa Suguru,Fukuoka Junya
• BMC Clinical Pathology 14(1), 23, 2014-05-13
• … Cox multivariate analysis of Ki-67 showed that HS was an independent risk factor affecting overall survival. …
• NAID 120005451798

• CCN2 as a Novel Molecule Supporting Energy Metabolism of Chondrocytes

• Maeda-Uematsu Aya,Kubota Satoshi,Kawaki Harumi,Kawata Kazumi,Miyake Yoshiaki,Hattori Takako,Nishida Takashi,Moritani Norifumi,Lyons Karen M.,Iida Seiji,Takigawa Masaharu
• Journal of Cellular Biochemistry 115(5), 854-865, 2014-05
• … CCN2/connective tissue growth factor (CTGF) is a unique molecule that promotes both chondrocytic differentiation and proliferation through its matricellular interaction with a number of extracellular biomolecules. …
• NAID 120005468290

Related Links

• tissue factor - definition of tissue factor in the Medical ...

rheumatoid factor (RF) antibodies directed against antigenic determinants on IgG molecules, found in the serum of about 80 per cent of patients with classic or definite rheumatoid arthritis; but in only about 20 per cent of patients with ...

• 組織因子（tissue factor: TF） - 山口大学大学院 ...- Yahoo!ブログ

組織因子（tissue factor: TF）は細胞膜結合型の1本鎖糖蛋白質で，外因系血液凝固反応の開始因子である．TFは細胞表面のリン脂質層上でⅦ因子または活性化Ⅶ（Ⅶa）因子と複合体を形成し，Ⅸ因子およびⅩ因子を活性化させ ...

Related Pictures

---

★リンクテーブル★

リンク元	「第VIII因子」「組織因子」「TF」「prothrombinase」「blood coagulation factor III」
拡張検索	「tissue factor pathway inhibitor」
関連記事	「fact」「factor」

「第VIII因子」

　　[★]

英

factor VIII, FVIII

同

血漿トロンボプラスチン因子 plasma thromboplastin factor PTF

抗血友病グロブリン antihemophilic globulin、抗血友病因子A antihemophilic factor A platelet cofactor I、抗血友病因子

商

(オクトコグアルファ)コージネイト

(ルリオクトコグアルファ)アドベイト

クロスエイト、コンコエイト、コンファクト

関

血液凝固因子、血友病

[show details]

第VIII因子 : 約 233,000 件
凝固第VIII因子 : 約 65,300 件
血液凝固第VIII因子 : 約 52,200 件

存在部位

• von Willebrand因子と結合
• 血小板のα顆粒の中

半減期

• 12 hr

• 第IX因子の半減期は24hrなので、血友病Aは血友病Bより短い間隔で第VIII因子を投与する必要がある。

産生組織

• 細網系?

肝以外で産生される凝固因子

• 第III因子(tissue factor)
• 第VIII因子
• von Willebrand factor

座乗染色体

• xq28

臨床関連

• 血友病A

「組織因子」

　　[★]

英

tissue factor TF

同

第III因子、factor III

関

血液凝固因子、組織トロンボプラスチン

• 組織で産生される
• 糖タンパク質
• 45kDa
• 外因系カスケードの起点となる
• 第VII因子を活性化し(第VIIa因子)、また複合体を形成して以下の反応を起こす

第X因子の活性化

第IX因子の活性化

「TF」

　　[★]

• 転写因子 transcription factor
• 組織因子 tissue factor
• ファロー四徴症 tetralogy of Fallot
• トランスフェリン transferrin

「prothrombinase」

　　[★]

プロトロンビナーゼ

関

blood coagulation factor III、coagulation factor III、factor III、thromboplastin、tissue factor

　

「blood coagulation factor III」

　　[★]

血液凝固第III因子

関

coagulation factor III、factor III、prothrombinase、thromboplastin、tissue factor

「tissue factor pathway inhibitor」

　　[★] 組織因子経路インヒビター TFPI

同

TFPI

「fact」

　　[★]

• n.

• 事実、現状、実際、実態

関

actual、actually、in fact、in practice、indeed、practically

　 　 　 　 　

「factor」

　　[★]

• n.

• 因子、要因、要素、ファクター

関

element、elementary、factorial、parameter