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Human PTPN11 Protein expressed in Wheat germ - ABIN1316822
Jo, Park, Lee, Ahn, Kim, Park, Choi: SHP-2 binds to caveolin-1 and regulates Src activity via competitive inhibition of CSK in response to H2O2 in astrocytes. in PLoS ONE 2014
Proliferation and soft agar assays were used to demonstrate the functional contribution of SHP2 to cell growth and transformation. SHP2 expression correlated with SOX2 expression in glioma stem cell (GSC) lines and was decreased in differentiated cells. Forced differentiation of GSCs by removal of growth factors, as confirmed by loss of SOX2 expression, also resulted in decreased SHP2 expression.
PTPN11 plays a role in regulating neurotrophin (show BDNF Proteins) protective signaling in neuronal cells; PTPN11 dysregulation promotes apoptotic activation.
This study provides information on phenotypes observed in Noonan syndrome patients with different PTPN11 mutations and defines two novel mutations.
SHP-2 protein may become a new target for anti-malignant transformation of glioma.
High SHP2 expression is associated with colorectal tumors.
SHP2 expression was activated by the HBx-NF-kappaB (show NFKB1 Proteins) pathway. In patients with HCC (show FAM126A Proteins), a loss of SHP2 expression was associated with suppressed NF-kappaB (show NFKB1 Proteins)-SHP2-ERK (show EPHB2 Proteins) pathway activity and accelerated HCC (show FAM126A Proteins) development, whereas SHP2 overexpression in parallel with increased STAT3 (show STAT3 Proteins) activity was associated with fibrosis promotion during the early stages of HCC (show FAM126A Proteins) development.
The inhibitory action of cryptotanshinone is largely attributed to the inhibition of STAT3 Tyr705 phosphorylation with a novel mechanism of upregulating the tyrosine phosphatase activity of SHP-2 protein.
Studies indicate that multiple classes of PTPN11 mutations with a distinct perturbing effect on SHP2's function.
Mutational status of NRAS (show NRAS Proteins), KRAS, and PTPN11 genes is associated with genetic/cytogenetic features in children with B-precursor acute lymphoblastic leukemia.
Studied mutations of PTPN11 in a cohort of Noonan Syndrome patients. Mutational analysis was performed and PTPN11 mutations were detected in 11 out of 17 (64.7%) patients with Noonan syndrome; 72% had mutation in exon 3 and 27 % had mutation in exon 13.
SHP2 supports basal pulmonary endothelial barrier function by coordinating the tyrosine phosphorylation profile of VE-cadherin (show CDH5 Proteins), beta-catenin (show CTNNB1 Proteins), and p190RhoGAP (show GRLF1 Proteins) and the activity of RhoA (show RHOA Proteins).
These findings identify Shp2 in podocytes as a significant contributor to the signaling events following LPS challenge and suggest that inhibition of Shp2 in podocytes may present a potential therapeutic target for podocytopathies.
Loss of Shp2 within radial glia resulted in cortical dysplasia with decreased ERK (show EPHB2 Proteins) signaling and was associated with glial defects and impaired sensorymotor development of newborn mice.
yolk sac (show ADCY10 Proteins) erythromyeloid progenitors expressing mutant PTPN11 demonstrate functional and molecular features of juvenile myelomonocytic leukemia but do not cause disease following transplantation nor following unperturbed development.
nuclear Shp2, rather than cytosolic Shp2, promotes the ERalpha (show ESR1 Proteins) transcription activity. This function is achieved by enhancing the Src kinase (show CSK Proteins)-mediated ERalpha (show ESR1 Proteins) tyrosine phosphorylation, which facilitates ERalpha (show ESR1 Proteins) binding to Pgr (show PGR Proteins) promoter in an ERK (show EPHB2 Proteins)-independent manner in periimplantation uteri.
HIF1A dependent wound healing angiogenesis in vivo can be controlled by site-specific lentiviral magnetic targeting of SHP2.
High SHP2 expression prevents colitis-associated cancer development.
T lymphocyte SHP2-deficiency triggers anti-tumor immunity to inhibit colitis-associated colonic cancer in mice.
Here the authors demonstrate a central role of Ptpn11 in postnatal myogenesis of mice. Loss of Ptpn11 drove muscle stem cells out of the proliferative and into a resting state during muscle growth. This Ptpn11 function was observed in postnatal but not fetal myogenic stem cells. Furthermore, muscle repair was severely perturbed when Ptpn11 was ablated in stem cells due to a deficit in stem cell proliferation and survival.
S-nitrosylation of endogenous SHP2 Phosphatase and PTP1B (show PTPN1 Proteins) in endothelial insulin (show INS Proteins) signaling has been demonstrated.
a method that allows the localized visualization of oxidized intermediates of SHP-2 protein-tyrosine phosphatase (show ACP1 Proteins) inside cells during signaling.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. 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 contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia. Two transcript variants encoding different isoforms have been found for this gene.
, protein-tyrosine phosphatase 1D
, protein-tyrosine phosphatase 2C
, tyrosine-protein phosphatase non-receptor type 11
, SH2 domain-containing protein tyrosine phosphatase-2
, protein-tyrosine phosphatase SYP
, SH-PTP2 protein tyrosine phosphatase non-receptor type 11
, SH-PTP2 protein tyrosine phosphatase, non-receptor type 11
, encodes catalytic domain
, protein tyrosine phosphatase SH-PTP2
, protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)
, non-receptor type protein tyrosine phosphatase SHP2