0000000001008101

AUTHOR

Mohamad Aljofan

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Cleavage of endometrial α-integrins into their functional forms is mediated by proprotein convertase 5/6.

2012

Background Proprotein convertases (PCs) post-translationally activate a large number of protein precursors through limited cleavage. PC5/6 (PC6) in the human endometrium is tightly regulated during receptivity for embryo implantation. Integrins are transmembrane glycoproteins, some of which play an important role in the adhesive interactions between the trophoblast (blastocyst) and uterine epithelium at implantation. Integrins require PC cleavage for post-translational modification. We hypothesize that pro-integrin-αs in the endometrial epithelium are post-translationally cleaved by PC6 into functional subunits for the binding of blastocyst and adhesion of extracellular matrix proteins. Met…

BiopsyIntegrinCleavage (embryo)Gene Expression Regulation EnzymologicEndometriumPregnancymedicineCell AdhesionHumansBlastocystEmbryo ImplantationCell adhesionCells CulturedGlycoproteinsbiologyRehabilitationObstetrics and GynecologyTrophoblastTransfectionMolecular biologyFibronectinsFibronectinmedicine.anatomical_structureBlastocystReproductive Medicinebiology.proteinProprotein Convertase 5CalciumFemaleProprotein ConvertasesIntegrin alpha ChainsProtein Processing Post-TranslationalHuman reproduction (Oxford, England)
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