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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. dans The Journal of clinical investigation 2003
Show all 4 Pubmed References
increased obesity risk linked to N221D allele may be due in part to PC1/3-induced loss of resilience to stressors rather than strictly to decreased enzymatic activity on peptide precursors
we found eight known variants and two novel heterozygous variants (c.1095 + 1G > A and p.S24C), and identified and functionally characterized two rare novel PCSK1 variants of which c.1095 + 1G > A caused complete loss of protein function. In addition to confirming rs6232 and rs6234 in PCSK1 as polygenic risk variants for childhood obesity, we describe an association of rs725522 with insulin metabolism.
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 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.
conclude that the N309K enzyme is able to cleave its own propeptide but is catalytically inert against in trans substrates, and that this variant accounts for the enteric and systemic endocrinopathies seen in the consanguineous kindred studied
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.
rs6232 associated with body mass index
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
Epistases between single nucleotide polymorphisms within proprotein convertase subtilisin/kexin type 1(PCSK1) and dopamine beta-hydroxylase(DBH) genes are significantly associated with susceptibility or resistance to premature ovarian failure
FTO-rs9939609, TMEM18-rs6548238 and PCSK1-rs6234 polymorphisms are significantly associated with body mass index in a southern Chinese population.
SNPs rs6232, rs6234, and rs6235 associated with obesity in Caucasians [review]
Common genetic variants in PCSK1 are associated with coronary artery disease in Chinese patients with type 2 diabetes.
PC1/3(S357G) exhibited a lower calcium dependence; a higher pH optimum.
PCSK1 is overexpressed in fibrolamellar hepatocellular carcinoma.
pancreatic cancer-derived exosomes (Exo-Mia) suppress the synthesis of GIP and GLP-1 from STC-1cells in vitro by down-regulating the PCSK1/3
Study reveals a significant reduction of tachykinin and opioid neuropeptides level in proprotein convertase 1 and proprotein convertase 2 mutant mouse spinal cords.
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
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
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.
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
Binding of MAGP2 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 as a novel down-regulated target of Pax6
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.
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.
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.
Intraislet production of GLP-1 by activation of prohormone convertase 1/3 in pancreatic alpha-cells in mouse models of ss-cell regeneration.
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.
These results demonstrate a prominent role for cathepsin L, jointly with PC1/3 and PC2, for production of dynorphins in brain.
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
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.
expression pattern of IAPP and prohormone convertase 1/3 reveals a distinctive set of endocrine cells in the embryonic pancreas
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