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Study reveals a significant reduction of tachykinin and opioid neuropeptides level in proprotein convertase 1 and proprotein convertase 2 mutant mouse spinal cords.
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Oxygen and glucose deprivation or middle cerebral artery occlusion stress caused substantial cell death in a dose-dependent manner. With the increasing OGD dose, proPC1 and PC1 proteins gradually increased. In vivo the proPC1 and PC1 expressions presented with a peak at 4-h and then decreased at 24-h reperfusion. The results suggest that the increasing PC1 expression promoted the transformation of proCgA into CgA or small
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investigation of the pathogenesis of obesity in the PC1/3-N222D mouse model and whether this molecular mechanism also applies to common and rare human PCSK1 mutations
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These pathways are consistent with previously reported behavioral and biochemical phenotypes that typify mice lacking ENT1. Moreover, we validated decreased expression of the SNARE complex protein VAMP1 (synaptobrevin-1) in the dHip as well as decreased expression of pro-dynorphin (PDYN), neuroendocrine convertase (PCSK1), and Leu-Enkephalin (dynorphin-A) in the nucleus accumbens
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findings suggest that the major neuroendocrine features of Prader-Willi syndrome are due to PC1 deficiency
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macrophages from PC1/3 KO mice and rat PC1/3-KD NR8383 macrophages secreted more pro-inflammatory cytokines such as TNF-alpha, IL6, IL1alpha and CXCL2.
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PC1 and PC2 are involved in the C-terminal processing of protachykinin peptides and suggest a major role in the maturation of the protachykinin-1 protein
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Binding of MAGP2 to microfibrils is regulated by proprotein convertase cleavage.
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Data indicate that the mutant PC1/3-N222D protein coimmunoprecipitates with wildtype(WT) prohormone convertase 1/3 (PC1/3) and exerts a modest effect on intracellular retention of the WT enzyme.
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proSAAS as a novel down-regulated target of Pax6
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Loss of PC1 in mice showed a dramatic decrease in the biosynthesis of all proTRH-derived peptides analyzed including TRH and its immediate precursor TRH-Gly.
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PC1/3 also has an important role in the regulation of the innate immune system, most likely through the regulation of cytokine secretion in macrophages.
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Reports demonstrate that mouse proprotein convertase 1/3 (mPC1/3) has a lag phase of activation by substrates that can be interpreted as a hysteretic behavior of the enzyme for their hydrolysis.
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Intraislet production of GLP-1 by activation of prohormone convertase 1/3 in pancreatic alpha-cells in mouse models of ss-cell regeneration.
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Data suggest that PC1/3 and many convertase-specific properties are attributable less to convertase-specific catalytic cleft residues than to convertase-specific domain interactions.
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These results demonstrate a prominent role for cathepsin L, jointly with PC1/3 and PC2, for production of dynorphins in brain.
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PC1 expression can promote normal and neoplastic mammary development and growth and suggests that proprotein convertases may be important etiological factors in human breast neoplasia
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The presence of PC and GOAT in the cells, as well as n-octanoic acid in the culture medium, was necessary to produce n-octanoyl ghrelin.
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expression pattern of IAPP and prohormone convertase 1/3 reveals a distinctive set of endocrine cells in the embryonic pancreas
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hydrophobic patch in the PC1 pro-domain is involved in the binding interface with its cognate catalytic domain and also reveals potential mechanisms for the acid-induced dissociation of the complex between pro- and catalytic domains
