Plasminogen activator inhibitor-1 (serpin E1) is a serine protease inhibitor which belongs to the serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.
Serpin E2 is a member of the Serpin superfamily of the serine protease inhibitors. Serpin E2 is apotent inhibitor of thrombin, plasmin and plasminogen activators. It is differentially expressed during neuronal differentiation and is able to transform humanembryonic kidney cells into neuronlikecells. Its over-expressionin mice leads to progressive neuronal and motor dysfunction in these animals. It is also over-expressedin the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples whereas it is weakly expressed in all normal pancreas and chronicpancreatitis tissue samples. It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from theonset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction.
Serpin F1 is secreted Neurotrophic protein and belongs to the serpin family. Serpin F1 Highly expressed in the liver, gastric glandular mucosa and renal tubules. It is also expressed in the brain, heart, lung retina and testes. It induces extensive neuronal differentiation in retinoblastoma cells. It is potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, exhibits no serine protease inhibitory activity.
Pigment epithelium-derived factor, also known as PEDF, Serpin F1, and SERPINF1, is a multiple functional protein which has both anti-angiogenic activity and neurotrophic activity at the same time. PEDF is a secreted glycoprotein that belongs to the noninhibitory serpin. It has an alpha/beta core serine-protease inhibitor domain, three major beta-sheets, and ten alpha-helices. PEDF does not inhibit either serine or cysteine proteinases. PEDF exerts diverse physiological activities including anti-angiogenesis, anti-vasopermeability, anti-tumor, and neurotrophic activities. PEDF acts via multiple high affinity ligands and cell receptors. It has been described as a natural angiogenesis inhibitor with neurotrophic and immune-modulation properties. PEDF induces macrophages apoptosis and necrosis through the activation of peroxisome proliferator-activated receptor-gamma by which PEDF could modulate inflammatory reactions in septic shock. It balances angiogenesis in the eye and blocks tumor progression.
Alpha-2-antiplasmin, also called Serpin F2, is a serine protease inhibitor (serpin) responsible for inactivating plasmin, and an important enzyme participates in fibrinolysis and degradation of other proteins. In liver cirrhosis, there is decreased production of alpha 2-antiplasmin, leading to decreased inactivation of plasmin and an increase in fibrinolysis. Serpin F2 is major expressed on liver and kidney. Some other tissues such as muscle, intestine, central nervous system, and placenta also express Serpin F2 mRNA at a moderate level indicated that it is a key regulator of plasmin-mediated proteolysis in these tissues.
SerpinF2, also known as alpha-2 antiplasmin (alpha-2 AP), is a member of the Serpin superfamily. SerpinF2 is the principal physiological inhibitor of serine protease plasmin, and as well as, an efficient inhibitor of trypsin and chymotrypsin. This protease is produced mainly by liver and kidney, and also expressed in muscle, intestine, central nervous system, and placenta also express this protein at a moderate level. It is indicated that Serpin F2 is a key regulator of plasmin-mediated proteolysis in these tissues. Alpha-2 AP is an unusual serpin in that it contains extensive N-and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. SerpinF2 is one of the inhibitors of fibrinolysis, which acts as the primary inhibitor of plasmin(ogen). It is a specific plasmin inhibitor, and is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. Alpha-2 AP plays the dominant role in inhibiting both plasma clot lysis and thrombus lysis, and accordingly, the congenital deficiency of Alpha-2 antiplasmin causes a rare bleeding disorder because of increased fibrinolysis. Thus, it may be a useful target for developing more effective treatment of thrombotic diseases.
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