Tissue factor: Difference between revisions

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Revision as of 23:05, 2 December 2017

Tissue factor, also called platelet tissue factor, factor III, thromboplastin, or CD142 is a protein encoded by the F3 gene present in subendothelial tissue and leukocytes. Its role in the clotting process is the initiation of thrombin formation from the zymogen prothrombin. Thromboplastin defines the cascade that leads to the activation of factor X - the tissue factor pathway. In doing so it has replaced the previously named extrinsic pathway in order to eliminate ambiguity.

Function

The F3 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.^[1] 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.^[2]^[3]

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 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).

Cytokine signaling

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.

Structure

Tissue factor belongs to the cytokine receptor protein superfamily and consists of three domains:^[4]

an extracellular domain, which consists of two fibronectin type III modules whose hydrophobic cores merge in the domain-domain interface. This serves as a (probably rigid) template for factor VIIa binding.
a transmembrane domain.
a cytosolic domain of 21 amino acids length inside the cell which is involved in the signaling function of TF.

Note that one of factor VIIa's domains, GLA domain, binds in the presence of calcium to negatively charged phospholipids, and this binding greatly enhances factor VIIa binding to tissue factor.

Tissue distribution

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, which 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 contains phospholipids as well as tissue factor, both of which needed in the activation of the extrinsic pathway, whereas partial thromboplastin does not contain tissue factor. Tissue factor is not needed to activate the intrinsic pathway.

Interactions

Tissue factor has been shown to interact with Factor VII.^[5]^[6]

Additional images

Tissue factor
Blood plasma after the addition of tissue factor

Blood plasma after the addition of tissue factor

References

↑ "Entrez Gene: F3 coagulation factor III (thromboplastin, tissue factor)".
↑ Guo W, Wang H, Zhao W, Zhu J, Ju B, Wang X (2001). "Effect of all-trans retinoic acid and arsenic trioxide on tissue factor expression in acute promyelocytic leukemia cells". Chin. Med. J. 114 (1): 30–4. PMID 11779431.
↑ Bogdanov VY, Balasubramanian V, Hathcock J, Vele O, Lieb M, Nemerson Y (April 2003). "Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein". Nat. Med. 9 (4): 458–62. doi:10.1038/nm841. PMID 12652293.
↑ Muller YA, Ultsch MH, de Vos AM (Feb 1996). "The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution". Journal of Molecular Biology. 256 (1): 144–159. doi:10.1006/jmbi.1996.0073. PMID 8609606.
↑ Carlsson K, Freskgård PO, Persson E, Carlsson U, Svensson M (Jun 2003). "Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor". Eur. J. Biochem. 270 (12): 2576–82. doi:10.1046/j.1432-1033.2003.03625.x. PMID 12787023.
↑ Zhang E, St Charles R, Tulinsky A (Feb 1999). "Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant". J. Mol. Biol. 285 (5): 2089–104. doi:10.1006/jmbi.1998.2452. PMID 9925787.

External links

Online Mendelian Inheritance in Man (OMIM) 134390
PDB Molecule of the Month Tissue factor - March 2006

[1] "Entrez Gene: F3 coagulation factor III (thromboplastin, tissue factor)".

[2] Guo W, Wang H, Zhao W, Zhu J, Ju B, Wang X (2001). "Effect of all-trans retinoic acid and arsenic trioxide on tissue factor expression in acute promyelocytic leukemia cells". Chin. Med. J. 114 (1): 30–4. PMID 11779431.

[3] Bogdanov VY, Balasubramanian V, Hathcock J, Vele O, Lieb M, Nemerson Y (April 2003). "Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein". Nat. Med. 9 (4): 458–62. doi:10.1038/nm841. PMID 12652293.

[4] Muller YA, Ultsch MH, de Vos AM (Feb 1996). "The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution". Journal of Molecular Biology. 256 (1): 144–159. doi:10.1006/jmbi.1996.0073. PMID 8609606.

[pmid12787023-5] Carlsson K, Freskgård PO, Persson E, Carlsson U, Svensson M (Jun 2003). "Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor". Eur. J. Biochem. 270 (12): 2576–82. doi:10.1046/j.1432-1033.2003.03625.x. PMID 12787023.

[pmid9925787-6] Zhang E, St Charles R, Tulinsky A (Feb 1999). "Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant". J. Mol. Biol. 285 (5): 2089–104. doi:10.1006/jmbi.1998.2452. PMID 9925787.

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@@ Line 1: / Line 1: @@
-{{PBB_Controls
+{{Refimprove|date=August 2015}}
-| update_page = yes
+{{Infobox_gene}}
-| require_manual_inspection = no
+'''Tissue factor''', also called '''platelet tissue factor''', '''factor III''', '''thromboplastin''', or '''[[cluster of differentiation|CD142]]''' is a [[protein]] encoded by the '''F3''' [[gene]] present in [[endothelium|subendothelial tissue]] and [[leukocyte]]s. Its role in the clotting process is the initiation of [[thrombin]] formation from the [[zymogen]] [[prothrombin]]. Thromboplastin defines the cascade that leads to the activation of [[factor X]] - the tissue factor pathway. In doing so it has replaced the previously named extrinsic pathway in order to eliminate ambiguity.
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-{{GNF_Protein_box
- | image = PBB_Protein_F3_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ahw.
- | Name = Coagulation factor III (thromboplastin, tissue factor)
- | HGNCid = 3541
- | Symbol = F3
- | AltSymbols =; CD142; TF; TFA
- | OMIM = 134390
- | ECnumber =
- | Homologene = 1511
- | MGIid = 88381
- | GeneAtlas_image1 = PBB_GE_F3_204363_at_tn.png
- | Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}}
- | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
- | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 2152
-    | Hs_Ensembl = ENSG00000117525
-    | Hs_RefseqProtein = NP_001984
-    | Hs_RefseqmRNA = NM_001993
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 1
-    | Hs_GenLoc_start = 94767369
-    | Hs_GenLoc_end = 94779944
-    | Hs_Uniprot = P13726
-    | Mm_EntrezGene = 14066
-    | Mm_Ensembl = ENSMUSG00000028128
-    | Mm_RefseqmRNA = NM_010171
-    | Mm_RefseqProtein = NP_034301
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 3
-    | Mm_GenLoc_start = 121715560
-    | Mm_GenLoc_end = 121727071
-    | Mm_Uniprot = Q8R3Q1
-  }}
-}}
-{{SI}}
-{{CMG}}
+== Function ==
+The '''F3''' 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.<ref>{{cite web | title = Entrez Gene: F3 coagulation factor III (thromboplastin, tissue factor)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2152| accessdate = }}</ref> In addition to the membrane-bound tissue factor, soluble form of tissue factor was also found which results from [[alternative splicing|alternatively spliced]] tissue factor mRNA transcripts, in which [[exon]] 5 is absent and exon 4 is spliced directly to exon 6.<ref>{{cite journal | vauthors = Guo W, Wang H, Zhao W, Zhu J, Ju B, Wang X | title = Effect of all-trans retinoic acid and arsenic trioxide on tissue factor expression in acute promyelocytic leukemia cells | journal = Chin. Med. J. | volume = 114 | issue = 1 | pages = 30–4 | year = 2001 | pmid = 11779431 | doi =  }}</ref><ref>{{cite journal | vauthors = Bogdanov VY, Balasubramanian V, Hathcock J, Vele O, Lieb M, Nemerson Y | title = Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein | journal = Nat. Med. | volume = 9 | issue = 4 | pages = 458–62  | date = April 2003 | pmid = 12652293 | doi = 10.1038/nm841 }}</ref>
+=== Coagulation ===
+[[Image:Coagulation full.svg|thumb|left|300px|The coagulation cascade.]]
+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 VII]]a 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).
+{{clear|left}}
+=== Cytokine signaling ===
+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 cell]]s. 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]].
-'''Tissue factor''', also called '''thromboplastin''', '''factor III''' or '''[[cluster of differentiation|CD142]]''' is a [[protein]] present in [[endothelium|subendothelial tissue]], [[platelets]], and [[leukocyte]]s necessary for the initiation of [[thrombin]] formation from the zymogen [[prothrombin]]. Thrombin formation ultimately leads to the [[coagulation]] of [[blood]].
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = 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.<ref>{{cite web | title = Entrez Gene: F3 coagulation factor III (thromboplastin, tissue factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2152| accessdate = }}</ref>
-}}
 ==Structure==
+Tissue factor belongs to the [[cytokine receptor]] [[protein superfamily]] and consists of three [[protein domain|domain]]s:<ref>{{cite journal |vauthors=Muller YA, Ultsch MH, de Vos AM | title = The crystal structure of the extracellular domain of human tissue factor refined to 1.7 Å resolution | journal = Journal of Molecular Biology | volume = 256 | issue = 1 | pages = 144–159 |date=Feb 1996 | pmid = 8609606 | doi = 10.1006/jmbi.1996.0073}}</ref>
-The protein structure of TF consists of three domains:
+# an extracellular domain, which consists of two [[fibronectin]] type III modules whose hydrophobic cores merge in the domain-domain interface. This serves as a (probably rigid) template for [[factor VIIa]] binding.
+# a [[transmembrane]] domain.
+# a cytosolic domain of 21 amino acids length inside the cell which is involved in the signaling function of TF.
-* 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.
+Note that one of factor VIIa's domains, [[GLA domain]], binds in the presence of calcium to negatively charged [[phospholipids]], and this binding greatly enhances factor VIIa binding to tissue factor.
-** 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.
+== Tissue distribution ==
-* 3.  a domain of 21 amino acids length inside the cell which is involved in the signaling function of TF.
+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).
-==Functions==
+TF is expressed by cells which are normally not exposed to flowing blood such as sub-endothelial cells (e.g. [[smooth muscle cell]]s) and cells surrounding blood vessels (e.g. [[fibroblast]]s). This can change when the blood vessel is damaged by for example physical injury or rupture of [[atherosclerotic plaque]]s. 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.
-===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 VII]]a catalyzes the conversion of the inactive protease [[factor X]] into the active protease factor Xa.
+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).
-Together with factor VII, 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).
+== Thromboplastin ==
-[[Image:Coagulation full.svg|thumb|center|400px|The coagulation cascade.]]
+Historically, [[thromboplastin]] was a lab reagent, usually derived from placental sources, used to assay [[prothrombin time]]s (PT time). Thromboplastin, by itself, could activate the extrinsic coagulation pathway. When manipulated in the laboratory, a derivative could be created called partial thromboplastin, which was used to measure the intrinsic pathway. This test is called the [[Partial thromboplastin time|aPTT]], or activated partial thromboplastin time. It was not until much later that the subcomponents of thromboplastin and partial thromboplastin were identified. Thromboplastin contains phospholipids as well as tissue factor, both of which needed in the activation of the extrinsic pathway, whereas partial thromboplastin does not contain tissue factor. Tissue factor is not needed to activate the intrinsic pathway.
-===Cytokine===
+== Interactions ==
-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==
+Tissue factor has been shown to [[Protein-protein interaction|interact]] with [[Factor VII]].<ref name=pmid12787023>{{cite journal | vauthors = Carlsson K, Freskgård PO, Persson E, Carlsson U, Svensson M | title = Probing the interface between factor Xa and tissue factor in the quaternary complex tissue factor-factor VIIa-factor Xa-tissue factor pathway inhibitor | journal = Eur. J. Biochem. | volume = 270 | issue = 12 | pages = 2576–82  | date = Jun 2003 | pmid = 12787023 | doi = 10.1046/j.1432-1033.2003.03625.x }}</ref><ref name=pmid9925787>{{cite journal | vauthors = Zhang E, St Charles R, Tulinsky A | title = Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant | journal = J. Mol. Biol. | volume = 285 | issue = 5 | pages = 2089–104  | date = Feb 1999 | pmid = 9925787 | doi = 10.1006/jmbi.1998.2452 }}</ref>
-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).
+== Additional images ==
-==Additional images==
 <gallery>
   Image:Tissue factor.png|Tissue factor
-  Image:Tissue factor activation.png|Tissue factor activation
+  File:Fibrin-nach-Thromboplastin.jpg|Blood plasma after the addition of tissue factor
 </gallery>
-==References==
+== See also ==
-{{reflist|2}}
+*[[hemostasis]]
-==Further reading==
+== References ==
+{{reflist}}
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Gouault-Helimann M, Josso F | title = [Initiation in vivo of blood coagulation. The role of white blood cells and tissue factor (author's transl)] | journal = Nouv Presse Med | volume = 8 | issue = 40 | pages = 3249–53 | year = 1979 | pmid = 392457 | doi =  }}
-| citations =
+* {{cite journal | vauthors = Mackman N | title = Regulation of the tissue factor gene | journal = FASEB J. | volume = 9 | issue = 10 | pages = 883–9 | year = 1995 | pmid = 7615158 | doi =  }}
-*{{cite journal  | author=Gouault-Helimann M, Josso F |title=[Initiation in vivo of blood coagulation. The role of white blood cells and tissue factor (author's transl)] |journal=La Nouvelle presse médicale |volume=8 |issue= 40 |pages= 3249-53 |year= 1980 |pmid= 392457 |doi=  }}
+* {{cite journal | vauthors = McVey JH | title = Tissue factor pathway | journal = Best Practice & Research. Clinical Haematology | volume = 12 | issue = 3 | pages = 361–72 | year = 1999 | pmid = 10856975 | doi =  }}
-*{{cite journal  | author=Mackman N |title=Regulation of the tissue factor gene. |journal=FASEB J. |volume=9 |issue= 10 |pages= 883-9 |year= 1995 |pmid= 7615158 |doi=  }}
+* {{cite journal | vauthors = Konigsberg W, Kirchhofer D, Riederer MA, Nemerson Y | title = The TF:VIIa complex: clinical significance, structure-function relationships and its role in signaling and metastasis | journal = Thromb. Haemost. | volume = 86 | issue = 3 | pages = 757–71 | year = 2001 | pmid = 11583305 | doi =  }}
-*{{cite journal  | author=McVey JH |title=Tissue factor pathway. |journal=Baillieres Best Pract. Res. Clin. Haematol. |volume=12 |issue= 3 |pages= 361-72 |year= 2000 |pmid= 10856975 |doi=  }}
+* {{cite journal | vauthors = Versteeg HH, Peppelenbosch MP, Spek CA | title = The pleiotropic effects of tissue factor: a possible role for factor VIIa-induced intracellular signalling? | journal = Thromb. Haemost. | volume = 86 | issue = 6 | pages = 1353–9 | year = 2001 | pmid = 11776298 | doi =  }}
-*{{cite journal  | author=Konigsberg W, Kirchhofer D, Riederer MA, Nemerson Y |title=The TF:VIIa complex: clinical significance, structure-function relationships and its role in signaling and metastasis. |journal=Thromb. Haemost. |volume=86 |issue= 3 |pages= 757-71 |year= 2002 |pmid= 11583305 |doi=  }}
+* {{cite journal | vauthors = Fernandez PM, Rickles FR | title = Tissue factor and angiogenesis in cancer | journal = Curr. Opin. Hematol. | volume = 9 | issue = 5 | pages = 401–6 | year = 2002 | pmid = 12172458 | doi = 10.1097/00062752-200209000-00003 }}
-*{{cite journal  | author=Versteeg HH, Peppelenbosch MP, Spek CA |title=The pleiotropic effects of tissue factor: a possible role for factor VIIa-induced intracellular signalling? |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1353-9 |year= 2002 |pmid= 11776298 |doi=  }}
+* {{cite journal | vauthors = Golino P | title = The inhibitors of the tissue factor:factor VII pathway | journal = Thromb. Res. | volume = 106 | issue = 3 | pages = V257–65 | year = 2002 | pmid = 12356487 | doi = 10.1016/S0049-3848(02)00079-8 }}
-*{{cite journal  | author=Fernandez PM, Rickles FR |title=Tissue factor and angiogenesis in cancer. |journal=Curr. Opin. Hematol. |volume=9 |issue= 5 |pages= 401-6 |year= 2003 |pmid= 12172458 |doi=  }}
+* {{cite journal | vauthors = Engelmann B, Luther T, Müller I | title = Intravascular tissue factor pathway--a model for rapid initiation of coagulation within the blood vessel | journal = Thromb. Haemost. | volume = 89 | issue = 1 | pages = 3–8 | year = 2003 | pmid = 12540946 | doi = 10.1267/THRO03010003 | doi-broken-date = 2017-01-15 }}
-*{{cite journal  | author=Golino P |title=The inhibitors of the tissue factor:factor VII pathway. |journal=Thromb. Res. |volume=106 |issue= 3 |pages= V257-65 |year= 2003 |pmid= 12356487 |doi=  }}
+* {{cite journal | vauthors = Morrissey JH | title = Tissue factor: in at the start...and the finish? | journal = J. Thromb. Haemost. | volume = 1 | issue = 5 | pages = 878–80 | year = 2003 | pmid = 12871349 | doi = 10.1046/j.1538-7836.2003.00219.x }}
-*{{cite journal  | author=Engelmann B, Luther T, Müller I |title=Intravascular tissue factor pathway--a model for rapid initiation of coagulation within the blood vessel. |journal=Thromb. Haemost. |volume=89 |issue= 1 |pages= 3-8 |year= 2004 |pmid= 12540946 |doi= 10.1267/THRO03010003 }}
+* {{cite journal | vauthors = Yu JL, May L, Klement P, Weitz JI, Rak J | title = Oncogenes as regulators of tissue factor expression in cancer: implications for tumor angiogenesis and anti-cancer therapy | journal = Semin. Thromb. Hemost. | volume = 30 | issue = 1 | pages = 21–30 | year = 2004 | pmid = 15034795 | doi = 10.1055/s-2004-822968 }}
-*{{cite journal  | author=Morrissey JH |title=Tissue factor: in at the start...and the finish? |journal=J. Thromb. Haemost. |volume=1 |issue= 5 |pages= 878-80 |year= 2004 |pmid= 12871349 |doi=  }}
+* {{cite journal | vauthors = Fernandez PM, Patierno SR, Rickles FR | title = Tissue factor and fibrin in tumor angiogenesis | journal = Semin. Thromb. Hemost. | volume = 30 | issue = 1 | pages = 31–44 | year = 2004 | pmid = 15034796 | doi = 10.1055/s-2004-822969 }}
-*{{cite journal  | author=Yu JL, May L, Klement P, ''et al.'' |title=Oncogenes as regulators of tissue factor expression in cancer: implications for tumor angiogenesis and anti-cancer therapy. |journal=Semin. Thromb. Hemost. |volume=30 |issue= 1 |pages= 21-30 |year= 2004 |pmid= 15034795 |doi= 10.1055/s-2004-822968 }}
+* {{cite journal | vauthors = Mackman N | title = Role of tissue factor in hemostasis, thrombosis, and vascular development | journal = Arterioscler. Thromb. Vasc. Biol. | volume = 24 | issue = 6 | pages = 1015–22 | year = 2004 | pmid = 15117736 | doi = 10.1161/01.ATV.0000130465.23430.74 }}
-*{{cite journal  | author=Fernandez PM, Patierno SR, Rickles FR |title=Tissue factor and fibrin in tumor angiogenesis. |journal=Semin. Thromb. Hemost. |volume=30 |issue= 1 |pages= 31-44 |year= 2004 |pmid= 15034796 |doi= 10.1055/s-2004-822969 }}
+* {{cite journal | vauthors = Belting M, Ahamed J, Ruf W | title = Signaling of the tissue factor coagulation pathway in angiogenesis and cancer | journal = Arterioscler. Thromb. Vasc. Biol. | volume = 25 | issue = 8 | pages = 1545–50 | year = 2005 | pmid = 15905465 | doi = 10.1161/01.ATV.0000171155.05809.bf }}
-*{{cite journal  | author=Mackman N |title=Role of tissue factor in hemostasis, thrombosis, and vascular development. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 6 |pages= 1015-22 |year= 2004 |pmid= 15117736 |doi= 10.1161/01.ATV.0000130465.23430.74 }}
+* {{cite journal | vauthors = Engelmann B | title = Initiation of coagulation by tissue factor carriers in blood | journal = Blood Cells Mol. Dis. | volume = 36 | issue = 2 | pages = 188–90 | year = 2007 | pmid = 16473535 | doi = 10.1016/j.bcmd.2005.12.020 }}
-*{{cite journal  | author=Belting M, Ahamed J, Ruf W |title=Signaling of the tissue factor coagulation pathway in angiogenesis and cancer. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=25 |issue= 8 |pages= 1545-50 |year= 2005 |pmid= 15905465 |doi= 10.1161/01.ATV.0000171155.05809.bf }}
+* {{cite journal | vauthors = Furie B, Furie BC | title = Cancer-associated thrombosis | journal = Blood Cells Mol. Dis. | volume = 36 | issue = 2 | pages = 177–81 | year = 2007 | pmid = 16490369 | doi = 10.1016/j.bcmd.2005.12.018 }}
-*{{cite journal  | author=Engelmann B |title=Initiation of coagulation by tissue factor carriers in blood. |journal=Blood Cells Mol. Dis. |volume=36 |issue= 2 |pages= 188-90 |year= 2007 |pmid= 16473535 |doi= 10.1016/j.bcmd.2005.12.020 }}
+* {{cite journal | vauthors = Mackman N | title = Alternatively spliced tissue factor - one cut too many? | journal = Thromb. Haemost. | volume = 97 | issue = 1 | pages = 5–8 | year = 2007 | pmid = 17200762 | doi = 10.1160/th06-11 }}
-*{{cite journal  | author=Furie B, Furie BC |title=Cancer-associated thrombosis. |journal=Blood Cells Mol. Dis. |volume=36 |issue= 2 |pages= 177-81 |year= 2007 |pmid= 16490369 |doi= 10.1016/j.bcmd.2005.12.018 }}
+* {{cite journal | vauthors = Wiiger MT, Prydz H | title = The changing faces of tissue factor biology. A personal tribute to the understanding of the "extrinsic coagulation activation" | journal = Thromb. Haemost. | volume = 98 | issue = 1 | pages = 38–42 | year = 2007 | pmid = 17597988 | doi = 10.1160/th07-04-0289 }}
-*{{cite journal  | author=Mackman N |title=Alternatively spliced tissue factor - one cut too many? |journal=Thromb. Haemost. |volume=97 |issue= 1 |pages= 5-8 |year= 2007 |pmid= 17200762 |doi=  }}
-*{{cite journal  | author=Wiiger MT, Prydz H |title=The changing faces of tissue factor biology. A personal tribute to the understanding of the "extrinsic coagulation activation". |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 38-42 |year= 2007 |pmid= 17597988 |doi=  }}
-}}
 {{refend}}
+== External links ==
 * {{OMIM|134390}}
-* {{PDB Molecule of the Month|pdb75_1}} - March 2006
+* {{PDB Molecule of the Month|75|Tissue factor}} - March 2006
-==See also==
-*[[hemostasis]]
+{{PDB Gallery|geneid=2152}}
 {{Coagulation}}
 {{Clusters of differentiation}}
@@ Line 125: / Line 93: @@
 [[Category:Coagulation system]]
 [[Category:Clusters of differentiation|CD142]]
-[[de:Thromboplastin]]
-[[it:Fattore tissutale]]
-[[pl:Tromboplastyna]]
-[[pt:Fator tissular]]
-{{WH}}
-{{WikiDoc Sources}}

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350