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Using loss-of-function and gain-of-function approaches, we show that PTPRO promotes the formation of excitatory synapses
PTPROt thus functions as an obligate haploinsufficient TS in CLL, where its expression levels determine its role as a promoter or inhibitor of the tumorigenic process in mice. Partial loss of PTPROt generates the strongest disease phenotype, suggesting that its intermediate expression levels in CLL are selected for.
TLR4 (show TLR4 Proteins) and NF-kappaB (show NFKB1 Proteins)/p65 (show NFkBP65 Proteins) phosphorylation was significantly enhanced in PTPRO over-expressing cells, while significantly down-regulated in PTPRO knockout cells. PTPRO plays ital roles in atherosclerosis (AS) via promoting ox-LDL induced oxidative stress and cell apoptosis through TLR4 (show TLR4 Proteins)/NF-kappaB (show NFKB1 Proteins) pathway.
PTPRO plays an important role in FH by interacting with TLR4 (show TLR4 Proteins).
Study show that EphA4 (show EPHA4 Proteins) is a substrate for PTP-oc in osteoclasts and that the molecular mechanism contributing to the PTP-oc-induced up-regulation of the osteoclast activity in part involves its dephosphorylation and inactivation of the EphA4 (show EPHA4 Proteins) signaling.
PTPRO truncated serves as an important tumor suppressor in hepatocellular carcinoma microenvironment.
The loss of PTPRO in the tumor niche was correlated with larger tumor volume, more metastases, increased number of circulating tumor cells, less apoptosis and reduced necrosis rates in the orthotopic mouse model of breast cancer.
PTPRO regulates insulin (show INS Proteins) and lipid metabolism via the PI3K/Akt (show AKT1 Proteins)/MDM4 (show MDM4 Proteins)/MDM2 (show MDM2 Proteins)/P53 (show TP53 Proteins) axis by affecting autophagy.
Survival and inflammation promotion effect of PTPRO in fulminant hepatitis is associated with NF-kappaB ac (show CTNNB1 Proteins)tivation.
PTPRO deficiency resulted in reduction of NF-kappaB activation in both hepatocytes and macrophages and was correlated to c-Src phosphorylation.
Single nucleotide polymorphism in PTPRO gene is associated with Acute Renal Graft Rejection.
Results provide evidence that PTPRO inhibits ERBB2 (show ERBB2 Proteins)-driven breast cancer through dephosphorylation leading to dual effects of ERBB2 (show ERBB2 Proteins) signaling suppression and endosomal internalization of ERBB2 (show ERBB2 Proteins).
PTPRO is a novel candidate gene in emphysema with severe airflow obstruction.
These observations confirm that PTPRO plays a critical role in liver fibrogenesis by affecting PDGF (show PDGFA Proteins) signaling in HSC (show FUT1 Proteins) activation and might be developed into a feasible therapeutic approach for the treatment of chronic fibrotic liver diseases.
The optimal pH value of PTP-oc is approximately 7.0.
Loss of PTPRO expression is associated with chronic lymphocytic leukemia.
Results highlight the PTPRO contribution in negative regulation of SRC (show SRC Proteins)/EGFR (show EGFR Proteins) signaling in colon cancer.
PTPRO was drastically decreased in fulminant hepatitis, and this was associated with enhanced beta-catenin (show CTNNB1 Proteins) accumulation but reduced IFN-gamma (show IFNG Proteins) secretion.
Our study suggests an interesting PTPRO/TLR4 (show TLR4 Proteins)/NF-kappaB (show NFKB1 Proteins) signaling feedback loop in Hhepatocellular carcinomcarcinogenesis and progression
This gene encodes a member of the R3 subtype family of receptor-type protein tyrosine phosphatases. These proteins are localized to the apical surface of polarized cells and may have tissue-specific functions through activation of Src family kinases. This gene contains two distinct promoters, and alternatively spliced transcript variants encoding multiple isoforms have been observed. The encoded proteins may have multiple isoform-specific and tissue-specific functions, including the regulation of osteoclast production and activity, inhibition of cell proliferation and facilitation of apoptosis. This gene is a candidate tumor suppressor, and decreased expression of this gene has been observed in several types of cancer.
glomerular epithelial protein 1
, osteoclastic phosphotyrosyl phosphatase
, Glomerular epithelial protein 1
, receptor-type protein tyrosine phosphatase D30
, receptor-type tyrosine-protein phosphatase O
, PTPase U2
, protein tyrosine phosphatase U2
, protein tyrosine phosphatase, non-receptor type 15
, receptor protein tyrosine phosphatase RO
, PTP phi
, osteoclastic transmembrane protein-tyrosine phosphatase
, phosphotyrosine phosphatase U2
, protein tyrosine phosphatase PTP-U2