Disease relevance of OSGEP

• Proteolysis of platelet GPIb with Serratia marcescens protease or O-sialoglycoprotein endopeptidase had no effect on alpha-thrombin binding to platelets or their subsequent activation [1].
• The Pasteurella haemolytica O-sialoglycoprotein endopeptidase is inhibited by zinc ions and does not cleave fetuin [2].
• Folate biosynthesis pseudogenes, PsifolP and PsifolK, and an O-sialoglycoprotein endopeptidase gene homolog in the phytoplasma genome [3].

High impact information on OSGEP

• The interaction between L-selectin and leukocytes was protease sensitive and calcium dependent, and abolished by cell treatment with neuraminidase, chlorate, or O-sialoglycoprotein endopeptidase [4].
• Treatment of HL-60 cells with O-sialoglycoprotein endopeptidase inhibited attachment and rolling on L-selectin and P-selectin [5].
• Purification and spectrometric analysis of N-CoR cleaving activity from an APL cell line reveals that it is a glycoprotein endopeptidase known as OSGEP [6].
• This protein was cleaved by O-sialoglycoprotein endopeptidase and required sialic acid for E-selectin binding [7].
• Opticin remains a dimer after removal of the amino-terminal region by O-sialoglycoprotein endopeptidase digestion, suggesting that dimer formation is mediated by the leucine-rich repeats [8].

Biological context of OSGEP

• Furthermore, the cleavage of N-CoR in APL cells could be blocked by the broad-spectrum protease inhibitor AEBSF and by RNA interference-mediated down-regulation of OSGEP expression [6].

Anatomical context of OSGEP

• No interactions were observed on WT E-selectin, whereas S128R supported a transient tethering interaction of K562 cells, which was resistant to digestion with either neuraminidase or O-sialoglycoprotein endopeptidase, and, in turn, could result in firm adhesion in the presence of a beta2-integrin [9].
• Treatment of both neonatal and adult neutrophils with 3RB-PSGL-1 similarly inhibited the interaction with P-selectin monolayers under shear conditions, effects similar to treatment with O-sialoglycoprotein endopeptidase (OSGE) [10].
• Pre-incubation of equine PBMC with neuraminidase or O-sialoglycoprotein endopeptidase (OSGP) reduced ePsel-IgG monocyte binding to 36% or 60%, respectively [11].

Associations of OSGEP with chemical compounds

• Degradation of glycoprotein Ib (GPIb) with an O-sialoglycoprotein endopeptidase did not affect the thrombin-stimulated labeling of inositol phosphates, indicating that binding to GPIb is not involved in the sustained thrombin-induced formation of inositol phosphates [12].
• Carbohydrate analysis shows that the endosialin core protein carries abundantly sialylated, O-linked oligosaccharides and is sensitive to O-sialoglycoprotein endopeptidase, placing it in the group of sialomucin-like molecules [13].

Analytical, diagnostic and therapeutic context of OSGEP

• Similar attachment-assay results were obtained using O-sialoglycoprotein endopeptidase; after treatment, the increase in JAr binding (>50%) was suppressed by the antiepisialin antibody [14].
• The assay of the O-sialoglycoprotein endopeptidase of Pasteurella haemolytica has previously used the cleavage of 125I-labeled glycophorin A, measured by SDS-PAGE, autoradiography, gel-slicing, and scintillation counting [15].

References