User:Cody Couperus/Sandbox 1: Difference between revisions

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==Regulation and Inhibition==

~~Regulation~~

Thrombin is regulated by inhibition and down regulation of production.

Antithrombin and heparin cofactor II are serpin inhibitors of thrombin that bind to specific sequences of sugar residues within a heparin chain on the endothelial lining.<ref>PMID: 15311269</ref> Thrombin also <scene name='58/583418/Antithrombin/1'>interacts with heparin</scene> nonspecific to sequence through its exosite II.<ref name='five'/> Thus, heparin acts as a surface that is outside of the procoagulant environment of the blood clot for thrombin interaction with inhibitors.

Thrombomodulin also binds to heparin (through an [http://en.wikipedia.org/wiki/EGF-like_domain EGF-like domain]) and thombin, it causes a conformation in thrombin that increases activity for TAFI and protein C by 1000-fold. APC then inactivates FVa and FVIIIa effectively decreasing the concentration of prothrombinase and Xase respectively, and thereby down regulating thrombin production.

<scene name='58/583418/Thrombomodulin/1'>Thrombomodulin</scene> also binds to heparin (through an [http://en.wikipedia.org/wiki/EGF-like_domain EGF-like domain]) and thombin, it causes a conformation in thrombin that increases activity for TAFI and protein C by 1000-fold. APC then inactivates FVa and FVIIIa effectively decreasing the concentration of prothrombinase and Xase respectively, and thereby down regulating thrombin production.

Central to both of these regulation pathways are specific cofactor binding at thrombins exosites; thrombomodulin and antithrombin at exosite I and heparin at exosite II. Therefore the structure of thrombin uniquely provides it the functional properties necessary for regulation.

@@ Line 74: / Line 74: @@
 ==Regulation and Inhibition==
-Regulation
 Thrombin is regulated by inhibition and down regulation of production.
 Antithrombin and heparin cofactor II are serpin inhibitors of thrombin that bind to specific sequences of sugar residues within a heparin chain on the endothelial lining.<ref>PMID: 15311269</ref> Thrombin also <scene name='58/583418/Antithrombin/1'>interacts with heparin</scene> nonspecific to sequence through its exosite II.<ref name='five'/> Thus, heparin acts as a surface that is outside of the procoagulant environment of the blood clot for thrombin interaction with inhibitors.
-Thrombomodulin also binds to heparin (through an [http://en.wikipedia.org/wiki/EGF-like_domain EGF-like domain]) and thombin, it causes a conformation in thrombin that increases activity for TAFI and protein C by 1000-fold. APC then inactivates FVa and FVIIIa effectively decreasing the concentration of prothrombinase and Xase respectively, and thereby down regulating thrombin production.
+<scene name='58/583418/Thrombomodulin/1'>Thrombomodulin</scene> also binds to heparin (through an [http://en.wikipedia.org/wiki/EGF-like_domain EGF-like domain]) and thombin, it causes a conformation in thrombin that increases activity for TAFI and protein C by 1000-fold. APC then inactivates FVa and FVIIIa effectively decreasing the concentration of prothrombinase and Xase respectively, and thereby down regulating thrombin production.
 Central to both of these regulation pathways are specific cofactor binding at thrombins exosites; thrombomodulin and antithrombin at exosite I and heparin at exosite II. Therefore the structure of thrombin uniquely provides it the functional properties necessary for regulation.