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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.
Both the rs2904268 C>G CG and GG genotype frequencies were markedly higher in the ESCC group relative to the control group (both p < 0.05). However, the genotype frequencies of rs2230605A>G and rs16995309 C>T were similar between the ESCC and control groups These results indicated that the PTPN1 gene polymorphism rs2904268 is associated with susceptibility to Esophageal Squamous Cell Carcinoma in Inner Mongolia.
Data suggest TrxR1 (show TXNRD1 Proteins) and NADPH (show NQO1 Proteins) directly protect PTP1B from inactivation by oxidation; this protection is independent of TRX1 (show MLL Proteins) and PRX2 (show PRDX2 Proteins); this protection is blocked by auranofin (an inhibitor of TrxR1 (show TXNRD1 Proteins) and requires an intact selenocysteine residue in TrxR1 (show TXNRD1 Proteins). (TrxR1 (show TXNRD1 Proteins) = thioredoxin reductase 1 (show TXNRD1 Proteins); PTP1B = protein tyrosine phosphatase (show ACP1 Proteins), non-receptor type 1; TRX1 (show MLL Proteins) = thioredoxin-1; PRX2 (show PRDX2 Proteins) = paired related homeobox 2 (show PRRX2 Proteins) protein)
Regulation of platelet-activating factor-mediated PTP1B activation by a Janus kinase 2/ calpain pathway has been reported.
PTP1B was overexpressed in over 70% of breast cancer tissues, correlating with patients with estrogen receptor (ER (show ESR1 Proteins))-negative, progesterone receptor (PR (show PGR Proteins))-negative, and human epidermal growth factor receptor (show EGFR Proteins) 2 (HER2 (show ERBB2 Proteins))-positive tumors. The data also showed that both tumor size and lymph node metastasis were significantly higher in patients with a higher level of PTP1B.
PTP1B uses conformational and dynamic allostery to regulate its activity. Both conformational rigidity and dynamics are essential for controlling protein activity.
PTP1BDelta6 is a positive regulator of JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signaling in classical Hodgkin lymphoma cells.(
In PTP1B and VHR (show DUSP3 Proteins), two new allosteric clusters were identified in each enzyme.
PTP1B/RNF213 (show RNF213 Proteins)/alpha-KGDD pathway is critical for survival of HER2 (show ERBB2 Proteins)(+) breast cancer, and possibly other malignancies, in the hypoxic tumour microenvironment
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.
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 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
These findings reveal a novel role for pancreatic PTP1B in cerulein- and arginine-induced acute pancreatitis.
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