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Results 1 - 10 of 13 > >>
EC Number
General Information
Commentary
Reference
evolution
the enzyme belongs to the Ca2+-dependent proprotein convertase family of enzymes
evolution
the enzyme is a serine protease of the proprotein convertase family
malfunction
complete knockout of PC5/6 is lethal between E4.5-7.5
malfunction
enzyme-knockout endometrial epithelial cells show reduced capacity to attach to trophoblast spheroids and bind to fibronectin compared with control. Knockdown of the enzyme decreases cell surface presentation of functional integrins-alpha1, alpha2, alpha5, alphaV and alphaVbeta5
malfunction
gene inactivation of PC5/6 leads to lethality at birth, the lack of PC5/6 in enterocytes results in a significantly higher tumor number in the duodenum, the absence of PC5/6 is also associated with a premature mortality of ApcMin/+ mice that harbor a heterozygote multiple intestinal neoplasia mutation in the adenomatous polyposis coli gene
malfunction
specific lentiviral short hairpin RNA-mediated PC5/6A knockdown decreases bone morphogenetic protein-2 expression and maturation, decreases expression of squamous cell markers, and increases expression of ciliated cell markers. Enzyme inhibition by decanoyl-Arg-Val-Lys-Arg-chloromethylketone and bone morphogenetic protein receptor inhibition by LDN-193189 suppress squamous differentiation, promote mucociliary differentiation, and down-regulate the BMP-2/Smad1/5/8/p38 signaling pathways
metabolism
the enzyme in the human endometrium is tightly regulated during receptivity for embryo implantation
metabolism
the enzyme is the proprotein convertase that is tightly regulated in the uterus during embryo implantation
physiological function
involvement of the enzyme in squamous differentiation of human nasal epithelial cells possibly through up-regulation of the BMP-2/pSmad1/5/8/p38 signaling pathway
physiological function
pro-integrins-alpha in the endometrial epithelium are post-translationally cleaved by the enzyme into functional subunits for the binding of blastocyst and adhesion of extracellular matrix proteins, the enzyme is responsible for the post-translational cleavage of pro-integrin-alpha5 and integrin-alphaV into their heavy and light chains in HEC-1-A cells. The integrins are transmembrane glycoproteins, some of which play an important role in the adhesive interactions between the trophoblast (blastocyst) and uterine epithelium at implantation
Results 1 - 10 of 13 > >>