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The expression of PTP1B in skeletal muscle was increased after caloric restriction and prolonged exercise.
preliminary data show that heterozygous or homozygous deletion of PTPN1 increases the severity of MPN (show PRSS27 Proteins) in Jak2V617F-knock-in mice. Future studies will determine whether loss of PTPN1 cooperates with the JAK2V617F mutation in the pathogenesis of MPN (show PRSS27 Proteins)
we demonstrated a novel oncogenic mechanism of PTP1B on affecting PITX1 (show PITX1 Proteins)/p120RasGAP (show RASA1 Proteins) in colorectal carcinoma(CRC (show CALR Proteins)). Regorafenib inhibited CRC (show CALR Proteins) survival through reserving PTP1B-dependant PITX1 (show PITX1 Proteins)/p120RasGAP (show RASA1 Proteins) downregulation. PTP1B may be a potential biomarker predicting regorafenib effectiveness, and a potential solution for CRC (show CALR Proteins)
this study highlights an important role for Nck1 (show NCK1 Proteins) in fine-tuning IRE1alpha (show ERN1 Proteins) expression and signaling that regulate PTP1B expression and subsequent activation of the PI3K (show PIK3CA Proteins)-Akt (show AKT1 Proteins) pathway in HepG2 cells.
In conclusion, HDAC6 (show HDAC6 Proteins) might enhance aggressive melanoma cells progression via interacting with PTPN1, which was independent of its histone modifying activity.
PTP1B is widely expressed in the human breast gland with highest expression in myoepithelial cells and fibroblasts. Inhibition of PTP1B in D492 and HMLE affects cell-cell adhesion and induces anoikis-like effects.
The results of the present study highlight the expression quantitative trait loci enrichment and pleiotropy in psoriasis and schizophrenia, and also suggest a possible key role of the PTPN1 gene in the etiology of psoriasis
The structural fragments which are important for PTP1B inhibition were identified by naive Bayesian method and can be further exploited to design new molecules around the identified scaffolds. The descriptive and predictive modeling strategy applied in this study is capable of identifying PTP1B inhibitors from the large compound libraries
The gained results are observed not only the unbinding mechanism of IRK (show KCNJ12 Proteins)-PTP1B complexes came from pulling force profile, number of hydrogen bonds, and interaction energy between IRK (show KCNJ12 Proteins) and PTP1Bs but also described PTP1B's point mutations could variably change its binding affinity towards IRK (show KCNJ12 Proteins).
these results suggest that inhibition of PTP1B activity is a promising new target in the treatment of colorectal cancer and the prevention of metastasis
PTP1B gene deletion significantly limited CLP (show HAPLN1 Proteins)-induced insulin (show INS Proteins) resistance, improved AMP-activated protein kinase (show PRKAA2 Proteins) signaling pathway and Glucose Transporter 4 translocation, and decreased inflammation. These effects were associated with a reduction of sepsis-induced endothelial dysfunction/impaired NO production and especially of insulin (show INS Proteins)-mediated dilatation.
Sleep fragmentation induces increased food intake, reduced leptin (show LEP Proteins) signaling in hypothalamus, systemic insulin (show INS Proteins) resistance, and reduced visceral white adipose tissue insulin (show INS Proteins) sensitivity and inflammation that are mediated by increased PTP-1B activity.
S-nitrosylation of endogenous SHP2 (show PTPN11 Proteins) Phosphatase and PTP1B in endothelial insulin (show INS Proteins) signaling has been demonstrated.
The findings show that reduced PTP1B responses contribute to disease symptoms in part by enhancing S100A9 (show S100A9 Proteins) expression during viral-associated chronic obstructive pulmonary disease exacerbations.
Under normoglycemia control and pod-PTP1B KO mice exhibited comparable renal functions. However, podocyte PTP1B disruption attenuated hyperglycemia-induced albuminuria and renal injury and preserved glucose control. Also, podocyte PTP1B disruption was accompanied with improved renal insulin (show INS Proteins) signaling and enhanced autophagy with decreased inflammation and fibrosis.
Endothelial PTP1B deletion improves cardiac VEGF (show VEGFA Proteins) signalling and angiogenesis and protects against chronic afterload-induced heart failure.
PTP1B inhibitors protect against atherosclerotic plaque formation in the LDLR (show LDLR Proteins)(-/-) mouse model of atherosclerosis.
The results suggest a deficiency of PTP1B improves hypothalamic insulin (show INS Proteins) sensitivity resulting in the attenuation of AgRP (show AGRP Proteins) mRNA expression under HFD conditions.
cadherin 2 (CDH2 (show CDH2 Proteins)) and CDH4 (show CDH4 Proteins) cooperate to regulate radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and beta-catenins.
this paper shows that PTP1B specifically regulates IgE-mediated STAT5 (show STAT5A Proteins) pathway, but is redundant in influencing mast cell function in vivo
PTP-1B increased posthypoxia by about 30% and persisted for 2 weeks while Src kinase (show CSK Proteins) inhibition attenuated the expected PTP-1B-increased expression.
data for the first time demonstrate a calpain/PTP1B/VEGFR2 negative feedback loop in the regulation of VEGF-induced angiogenesis. Modulation of local PTP1B and/or calpain activities may prove beneficial in the treatment of impaired wound healing in diabetes.
The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation.
protein tyrosine phosphatase, non-receptor type 1
, tyrosine-protein phosphatase non-receptor type 1
, tyrosine-protein phosphatase non-receptor type 1-like
, protein tyrosine phosphatase, placental
, protein-tyrosine phosphatase 1B
, protein-protein-tyrosine phosphatase HA2
, protein-tyrosine phosphatase HA2
, protein tyrosine phosphatase 1b
, non-receptor protein tyrosine phosphatase
, phosphoprotein phosphatase
, tyrosine phosphatase 1B