serpin

(redirected from Serpins)

serpin

 [ser´pin]
any of a superfamily of inhibitors of serine endopeptidase (serine proteinase), found in plasma and tissues; all are similarly structured single-chain glycoproteins although each one acts specifically on particular endopeptidases. Among their targets are serine proteinases involved in coagulation, complement activation, fibrinolysis, inflammation, and tissue remodeling. The serpins include alpha1-antitrypsin, antithrombin III, α2-antiplasmin, C1 inhibitor, and plasminogen activator inhibitor 1 (PAI-1). Called also serine protease or proteinase inhibitor.

serpin

(ser′pĭn) [ ser(ine) + p(roteinase) + in(hibitor)]
A serine protease inhibitor.
References in periodicals archive ?
Serpins promote cancer cell survival and vascular Co-option in brain metastasis.
Some studies have identified a serine-type protease inhibitor related to palmitoyltransferase that has an effect on melanogenesis.[5] Among other known serine protease inhibitors (SERPINs), the enhanced stability of PAI-1 might play a role in the development of autoimmune disease and the pathophysiology of vitiligo.
Plasminogen activator inhibitors: hormonally regulated serpins. Molecular and Cellular Endocrinology, 68, 1-19.
MMP-8 can resolve and regulate inflammatory and immunological cascades by processing nonmatrix bioactive substrates such as chemokines, cytokines, serpins, and complement components.
The action of these compounds would be mediated by serpins (antithrombin and heparin II cofactor) (Rodrigues et al., 2013; Wang et al., 2014) because galactose-rich polysaccharides reveal as inhibitors of thrombin (Hayakawa et al., 2000; Ghosh et al., 2004), but the relationship between structure and anticoagulation still lacks in-depth details since the existence of complexity and heterogeneity of the algae glycans make comparison difficult with UHEP at molecular level and bioactivity (Athukorala et al., 2006; Pomin, 2012; Fidelis et al., 2014; Mourao, 2015; Rodrigues et al., 2016).
In blood, thrombin is inhibited by such serpins (serine protease inhibitors) as antithrombin III, heparin cofactor II or protein C inhibitor (21, 25, 26), with antithrombin playing the predominant role.
Interestingly, the plasma contains serine proteinase inhibitors (serpins) that can regulate proteolytic events in tissues [2,49].
Cystatins, thyropins, and serpins prevent cathepsin substrates from binding and are thus endogenous inhibitors of cathepsins [9].
Plants synthesize inhibitory proteins that suppress the extracellular enzyme activities released by pathogenic microorganisms [8,9] These protease inhibitors (PIs) are of common occurrence and some serine PIs (serpins) involved in inhibiting proteases of plant pathogens have been isolated and used for medical treatments.
NON-INHIBITORY SERINE PROTEASE INHIBITORS (SERPINS) IN IMMUNOMODULATION
Many genes, such as serpins, BCL-2 proteins; tumor necrosis factor receptor superfamily, member 11a (TNFRSF11A), unc-13 homolog D (UNC13D), sphingosine, ArfGAP with FG repeats 1 (AGFG1), mitogen-activated protein kinase kinase 4 (MAP2K4), IGFBP7; receptor (TNFRSF)-interacting serine-threonine kinase 1 (R1PK1), were identified.