Recombinant Mouse Neuroendocrine convertase 1 (Pcsk1)

1. Study reveals a significant reduction of tachykinin and opioid neuropeptides level in proprotein convertase 1 and proprotein convertase 2 mutant mouse spinal cords. PMID: 28476408
2. 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 PMID: 29198128
3. 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 PMID: 26786350
4. 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 PMID: 27998058
5. findings suggest that the major neuroendocrine features of Prader-Willi syndrome are due to PC1 deficiency PMID: 27941249
6. 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. PMID: 26778167
7. 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 PMID: 26373413
8. Binding of MAGP2 to microfibrils is regulated by proprotein convertase cleavage. PMID: 25153248
9. 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. PMID: 24828610
10. 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. PMID: 22421509
11. 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. PMID: 22396549
12. 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. PMID: 21935423
13. Intraislet production of GLP-1 by activation of prohormone convertase 1/3 in pancreatic alpha-cells in mouse models of ss-cell regeneration. PMID: 20657753
14. 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. PMID: 20610561
15. These results demonstrate a prominent role for cathepsin L, jointly with PC1/3 and PC2, for production of dynorphins in brain. PMID: 19837164
16. 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 PMID: 20052009
17. 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. PMID: 19628676
18. expression pattern of IAPP and prohormone convertase 1/3 reveals a distinctive set of endocrine cells in the embryonic pancreas PMID: 12049785
19. 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 PMID: 12095256
20. severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3 PMID: 12136131
21. disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects PMID: 12145326
22. Processing of pro-CART revealed that PC2 is more potent than PC1/3 in generating bioactive CART I; bioactive CART II is solely generated by PC2; and PC1/3 is predominantly active in liberating the two intermediate CART fragments, 33-102 and 10-89. PMID: 12584191
23. The Arg617-Arg618 residues were found to play a prominent role in targeting PC1 to secretory granules PMID: 12787078
24. model of the membrane topology of the prohomone convertase PC3, where it is anchored to lipid rafts in secretory granule membranes via the transmembrane domain. PMID: 12950171
25. Prosomatostatin (PC1) is a physiologic substrate of proprotein convertase 2 (PC2) in vivo and is required for the generation of brain somatostatin-14 from precursor. PMID: 14614908
26. PC1 is essential for intestinal proglucagon processing in vivo and, thereby, plays an important role in production of the incretin hormone GLP-1 and the intestinotrophic hormone GLP-2. PMID: 14630721
27. Efficient production of mature GHRH from pro-GHRH is a stepwise process mediated predominantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus. PMID: 14684599
28. PC1/3 is important for processing of proIAPP at the COOH-terminus. PMID: 14693708
29. ProSAAS and prohormone convertase 1 are broadly expressed during mouse development PMID: 15018810
30. This review highlights the decisive role played by prohormone convertase (PC)1 in the maturation of hormonal cholecystokinin in intestinal endocrine cells, compared to PC2, which governs the processing of cholecystokinin precursor in cerebral neurons. PMID: 15075450
31. Prohormone convertase 1 plays a key role in the processing of multiple neuroendocrine peptide precursors. PMID: 15779921
32. an amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward furin PMID: 16407210
33. Prohormone convertase 1/3 is essential for processing of the glucose-dependent insulinotropic polypeptide precursor PMID: 16476726
34. PC1 has a role in obesity, hyperphagia and increased metabolic efficiency PMID: 16644867
35. a Pcsk1 deletion/insertion is associated with homozygous embryo preimplantation lethality, mutant allele preferential transmission and heterozygous female susceptibility to dietary fat PMID: 17490633
36. PC1/3, through its various domains, is capable of controlling its enzymatic activity in all regions of the cell that it encounters PMID: 17565604
37. Analysis of the subcellular distribution of fusion proteins containing the C-terminal domains of PC1/3, PC2 and PC5/6A confirmed that all three domains have the capacity to redirect secreted protein to the granule-containing cytoplasmic extensions. PMID: 17645548
38. Expression of PC1/3 rather than PC2 in alpha-cells induces GLP-1 and GLP-2 production and converts the alpha-cell from a hyperglycemia-promoting cell to one that lowers blood glucose levels and promotes islet survival. PMID: 17698597
39. PC1/3 governs the endocrine and PC2 the neuronal processing of proCCK, whereas PC5/6 contributes only to a modest endocrine synthesis of CCK-22. PMID: 18096669
40. mouse G-cells express PC1/3, 2 and 5/6. The concentration of progastrin in PC1/3-null mice was elevated 3-fold. The complementary cleavages of PC1/3 and 2, however, suffice to explain most of the normal endoproteolysis of progastrin. PMID: 18554181
41. Expression of PCSK1 in mouse small intestine. PMID: 18706454
42. Regulation and role of PC1 by corticotropin-releasing factor in mouse pituitary PMID: 18940205
43. These results provide a structure-function analysis of a dense core secretory granules -sorting domain of PC1/3 protease. PMID: 19376969

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KEGG: mmu:18548

STRING: 10090.ENSMUSP00000022075

UniGene: Mm.1333