Serine protease inhibitors

Antithrombin (AT) is a small glycoprotein that inactivates several enzymes of the coagulation system. It is a 464-amino-acid protein produced by the liver. It contains three disulfide bonds and a total of four possible glycosylation sites. α-Antithrombin is the dominant form of antithrombin found in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites. A single glycosylation site remains consistently un-occupied in the minor form of antithrombin, β-antithrombin. Its activity is increased manyfold by the anticoagulant drug heparin, which enhances the binding of

mammalian protein found in Homo sapiens

Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors). They are notable for their unusual mechanism of action, in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt the target's active site. This contrasts with the more common competitive mechanism for protease inhibitors t

Camostat is a serine protease inhibitor. Serine protease enzymes have a variety of functions in the body, and so camostat has a diverse range of uses. Camostat is approved in Japan for the treatment of chronic pancreatitis and postoperative reflux esophagitis. The oral proteolytic enzyme inhibitor has been on the market since 1985 under the trade name Foipan Tablets. The manufacturer is Ono Pharmaceutical. The drug is used in the treatment of some forms of cancer and is also effective against some viral infections, as well as inhibiting fibrosis in liver or kidney disease or pancreatitis.

In biochemistry, phenylmethylsulfonyl fluoride (PMSF) is a serine protease inhibitor (serine hydrolase inactivator) commonly used in the preparation of cell lysates. PMSF does not inactivate all serine proteases. The effective concentration of PMSF is between 0.1 - 1 mM. The half-life is short in aqueous solutions (110 min at pH 7, 55 min at pH 7.5, and 35 min at pH 8, all at 25 °C). At 4˚C, pH 8, PMSF is almost completely degraded after 1 day. Stock solutions are usually made up in anhydrous ethanol, isopropanol, or corn oil and diluted immediately before use.

mammalian protein found in Homo sapiens

AEBSF or 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride is a water-soluble, irreversible serine protease inhibitor with a molecular weight of 239.5 Da. It inhibits proteases like chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. The specificity is similar to the inhibitor PMSF, nevertheless AEBSF is more stable at low pH values. Typical usage is 0.1 - 1.0 mM. AEBSF (marketed as Pefabloc SC from the company Pentapharm) was first reported for use in biochemistry in 1993, and came into common use for the inhibition serine proteases and of non-protease enzymes such as acetylhydrola

C1-inhibitor (C1-inh, C1 esterase inhibitor) is a protease inhibitor belonging to the serpin superfamily. Its main function is the inhibition of the complement system (C1r, C1s) to prevent spontaneous activation but also as the major regulator of the contact system (PK, FXIIa, and FXIa).

Nafamostat mesylate (INN), a synthetic serine protease inhibitor, is a short-acting anticoagulant, and it is also used for the treatment of pancreatitis. It also has some potential antiviral and anti-cancer properties. Nafamostat is a fast-acting proteolytic inhibitor and used during hemodialysis to prevent the proteolysis of fibrinogen into fibrin. The mechanism of action of nafamostat is as a slow tight-binding substrate, trapping the target protein in the acyl-enzyme intermediate form, resulting in apparent observed inhibition.

Serpin B3 is a protein that in humans is encoded by the SERPINB3 gene.

Serpin B4 is a protein that in humans is encoded by the SERPINB4 gene.

protein-coding gene in the species Homo sapiens

chemical compound

Leukocyte elastase inhibitor (LEI) also known as serpin B1 is a protein that in humans is encoded by the SERPINB1 gene. It is a member of the clade B serpins or ov-serpins (ovalbumin related serpins) founded by ovalbumin.

Kallistatin is a protein that in humans is encoded by the SERPINA4 gene.

Kunitz-type protease inhibitor 1 is an enzyme that in humans is encoded by the SPINT1 gene.

Serpin B6 is a protein that in humans is encoded by the SERPINB6 gene.

protein-coding gene in the species Homo sapiens

Serpin B7 is a protein that in humans is encoded by the SERPINB7 gene.

Glia-derived nexin is a protein that in humans is encoded by the SERPINE2 gene.

Serpin A9 also known as centerin or GCET1 is a protein that in humans is encoded by the SERPINA9 gene located on chromosome 14q32.1. Serpin A9 is a member of the serpin family of serine protease inhibitors.

Serpin B8 is a protein that in humans is encoded by the SERPINB8 gene.

Serpin B9 is a protein that in humans is encoded by the SERPINB9 gene. Serpin B9 is an inhibitor of Granzyme B (GzmB). GzmB is a potent cytotoxic molecule that is secreted by cytotoxic T lymphocytes and natural killer (NK) cells to induce apoptosis in target cells during an immune response. Serpin B9, expressed in the cytosol and nucleus, thus protects from apoptosis by cytotoxic T lymphocytes and NK cells.

protein family

Maspin (mammary serine protease inhibitor) is a protein that in humans is encoded by the SERPINB5 gene. This protein belongs to the serpin (serine protease inhibitor) superfamily. SERPINB5 was originally reported to function as a tumor suppressor gene in epithelial cells, suppressing the ability of cancer cells to invade and metastasize to other tissues. Furthermore, and consistent with an important biological function, Maspin knockout mice were reported to be non-viable, dying in early embryogenesis. However, a subsequent study using viral transduction as a method of gene transfer (rather tha