Search results for SERPINE2

Showing 6 results out of 6

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Species

Types

Compartments

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Protein (2 results from a total of 2)

Identifier: R-HSA-4127459
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: SERPINE2: P07093
Identifier: R-HSA-4127461
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: SERPINE2: P07093

Complex (2 results from a total of 2)

Identifier: R-HSA-5607782
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-5607781
Species: Homo sapiens
Compartment: plasma membrane

Reaction (1 results from a total of 1)

Identifier: R-HSA-5602080
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
SERPINE2 (Protease nexin-1, PN1) is a specific and extremely efficient inhibitor of thrombin. Unlike other thrombin inhibitors belonging to the serpin family, SERPINE2 does not circulate in the blood (Bouton et al. 2012). Rather, it is bound to glycosaminoglycans on the surface of cell types including macrophages, smooth muscle cells and platelets, where it inhibits the signaling functions of thrombin. SERPINE2 sets the threshold for thrombin-induced platelet activation (Gronke et al. 1987, Boulaftali et al. 2010) and has been implicated in atherosclerosis (Bouton et al. 2012). Recent studies have demonstrated an important antithrombotic effect of platelet SERPINE2 in vitro and in vivo (Boulaftali et al. 2010).

Pathway (1 results from a total of 1)

Identifier: R-HSA-140875
Species: Homo sapiens
Compartment: extracellular region
The common pathway consists of the cascade of activation events leading from the formation of activated factor X to the formation of active thrombin, the cleavage of fibrinogen by thrombin, and the formation of cleaved fibrin into a stable multimeric, cross-linked complex. Thrombin also efficiently catalyzes the activation of several factors required earlier in the clotting cascade, thus acting in effect as a positive regulator of clotting. At the same time, thrombin activates protein C, which in turn catalyzes the inactivation of several of these upstream factors, thereby limiting the clotting process. Thrombin can be trapped in stable, inactive complexes with: antithrombin-III (SERPINC1), a circulating blood protein; heparin cofactor II (SERPIND1) which inhibits thrombin in a dermatan sulfate–dependent manner in the arterial vasculature; protein C inhibitor (SERPINA5) that inhibits thrombin in complex with thrombomodulin; and Protease nexin-1 (SERPINE2) that inhibits thrombin at the vessel wall and platelet surface. The quantitative interplay among these positive and negative modulators is critical to the normal regulation of clotting, facilitating the rapid formation of a protective clot at the site of injury, while limiting and physically confining the process.
These events are outlined in the drawing: black arrows connect the substrates (inputs) and products (outputs) of individual reactions, and blue lines connect output activated enzymes to the other reactions that they catalyze.
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