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Human PCSK1 Protein expressed in Human Cells - ABIN2002138
Jackson, Creemers, Farooqi, Raffin-Sanson, Varro, Dockray, Holst, Brubaker, Corvol, Polonsky, Ostrega, Becker, Bertagna, Hutton, White, Dattani, Hussain, Middleton, Nicole, Milla, Lindley, ORahilly: Small-intestinal dysfunction accompanies the complex endocrinopathy of human proprotein convertase 1 deficiency. in The Journal of clinical investigation 2003
Show all 4 Pubmed References
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
PCSK1 deficiency plays a role in human endocrinopathies, obesity, gastrointestinal disorders.
findings suggest that the major neuroendocrine features of Prader-Willi syndrome are due to PC1 deficiency
PCSK1 mutations are associated with Obesity.
PCSK1 expression is significantly upregulated in human masticatory mucosa during wound healing
these common variants in PCSK1 and POMC (show POMC Proteins) were not the major cause of obesity in the Thai subjects sampled. However, variants in PCSK1 did affect cholesterol level, LDL-C level, and waist circumference.
we demonstrate evidence that common gene variation in PCSK1 contributes to BMI variation and susceptibility to common obesity in the largest known meta-analysis published to date in genetic epidemiology.
Data show that prohormone convertase 1/3 (PC1/3) endoplasmic reticulum-retained mutants induce endoplasmic reticulum stress.
Mechanism of Fine-tuning pH Sensors in Proprotein Convertases: IDENTIFICATION OF A pH-SENSING HISTIDINE PAIR IN THE PROPEPTIDE OF PROPROTEIN CONVERTASE 1/3.
We showed for the first time that a nonsense mutation in PCSK1 was likely to cause dominantly inherited human obesity, due to the inhibiting properties of the propeptide fragment encoded by the null allele
Oxygen and glucose deprivation or middle cerebral artery occlusion stress caused substantial cell death in a dose-dependent manner. With the increasing OGD (show FGFR1 Proteins) 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 (show CGA Proteins) or small
These pathways are consistent with previously reported behavioral and biochemical phenotypes that typify mice lacking ENT1 (show SLC29A1 Proteins). Moreover, we validated decreased expression of the SNARE (show VTI1B Proteins) complex protein VAMP1 (synaptobrevin-1 (show VAMP1 Proteins)) in the dHip as well as decreased expression of pro-dynorphin (PDYN (show PDYN Proteins)), neuroendocrine convertase (PCSK1), and Leu-Enkephalin (dynorphin-A (show PDYN Proteins)) in the nucleus accumbens
macrophages from PC1/3 KO mice and rat PC1/3-KD NR8383 macrophages secreted more pro-inflammatory cytokines such as TNF-alpha (show TNF Proteins), IL6 (show IL6 Proteins), IL1alpha (show IL1A Proteins) and CXCL2 (show CXCL2 Proteins).
PC1 and PC2 (show CBX4 Proteins) are involved in the C-terminal processing of protachykinin peptides and suggest a major role in the maturation of the protachykinin-1 (show TAC1 Proteins) protein
Binding of MAGP2 (show MFAP5 Proteins) to microfibrils is regulated by proprotein convertase cleavage.
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.
proSAAS (show PCSK1N Proteins) as a novel down-regulated target of Pax6 (show PAX6 Proteins)
Loss of PC1 in mice showed a dramatic decrease in the biosynthesis of all proTRH-derived peptides analyzed including TRH (show TRH Proteins) and its immediate precursor TRH (show TRH Proteins)-Gly.
Prohormone convertase PC1 expression is up-regulated in a cell-specific manner in bovine neuroendocrine ocular ciliary epithelium.
a 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
Pcsk1 has been sequenced and characterized.
Study identified 14 polymorphisms that were organized in nine haplotypes, clearly distributed in two clades of putative European and Asian origin and showed that the porcine PCSK1 gene is associated with fat deposition.
The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a type I proinsulin-processing enzyme that plays a key role in regulating insulin biosynthesis. It is also known to cleave proopiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and progastrin. Mutations in this gene are thought to cause obesity. This encoded protein is associated with carcinoid tumors. Mutations in this gene have been associated with susceptibility to obesity and proprotein convertase 1/3 deficiency. Multiple transcript variants encoding different isoforms have been found for this gene.
, neuroendocrine convertase 1
, prohormone convertase 1
, prohormone convertase 3
, furin homolog
, prohormone convertase 1/3
, propeptide-processing protease
, proprotein convertase 1
, Protein convertase subtilisin / kexin type I
, Protein convertase subtilisin / kexin, type I
, prohormone convertase