抗Human PTEN 抗体:
identified the promotion effect of Dicer1 on liver regeneration by increasing miR-21 expression, which inhibits the expression of two negative cell proliferation regulators, Pten and Rhob
the c-Myc/miR17-92/PTEN axis tunes PI3K activity to control the expression of RAGs in proB cells.
Deletion of Pten resulted in elevated Dvl2, Wnt5a/b, and Naked2, along with decreased GSK3beta hippocampal synaptosome protein expression compared to wild type mice. Aberrations in the canonical Wnt pathway were associated with learning and memory deficits in Pten knockout mice, specifically in novel object recognition and the Lashley maze.
PTENalpha functions as a mitochondrial quality controller that maintains mitochondrial function and cardiac homeostasis.
The study demonstrated that wild-type PTEN can rescue the neuronal hypertrophy, while PTEN H93R, F241S, D252G, W274L, N276S, and D326N failed to rescue this hypertrophy. A subset of these mutations lacked nuclear localization, prompting us to examine the role of nuclear PTEN in regulating neuronal growth.
the mining of an online dataset (The Cancer Genome Atlas) revealed codeletions of PTEN and TP53 and/or CDKN2A/p14ARF in ~25% of human Malignant mesothelioma (MM), indicating that cooperative losses of these genes contribute to the development of a significant proportion of these aggressive neoplasms and suggesting key target pathways for therapeutic intervention.
data support the hypothesis that loss of Pten from the initial segment epithelium alters the luminal fluid microenvironment that is so important for sperm maturation and male fertility
Data indicate a regulatory pathway involving nuclear phosphatase and tensin homolog (PTEN)-mediated miRNA generation that limits the production of myeloid differentiation primary response protein 88 (MyD88) and thereby limits sepsis-associated mortality.
Podocyte-specific knockin of PTEN protected the kidney against hyperglycemia and was partly attributed to an improvement in autophagy and motility and the inhibition of apoptosis.
Deletion of phosphatase and tensin homolog (Pten) and transforming growth factor-beta receptor type 2 (Tgfbr2) may increase prostate epithelial cell reprogramming efficiency in vitro and cause rapid tumor development and early mortality in vivo.
these studies demonstrate altered Kv1.1 protein expression in association with mTOR hyperactivation in NS-Pten KO mice and suggest a role for mTOR signaling in the modulation of voltage-gated ion channel expression in this model.
IL-7R-mTORC1-Myc and PTEN-mediated PI3K suppression as discrete signaling axes driving B cell development.
Inflammatory microenvironments in the periportal area of Mir122a-null mice causes Pten down-regulation and expand tumor-initiating cells, causing hepatocellular carcinoma.
Study findings suggest a novel tumor suppressive role of Pten PDZ-binding domain (PDZ-BD) in a murine model of breast cancer, and the mechanism involves the dysregulation of homeobox genes which may result in defective myoepithelial differentiation in breast cancer cells.
These results suggest that PTEN persistently suppresses OL development in an mTOR-independent manner, and at least in part, via controlling GSK3beta activity. OPC-targeted PTEN-GSK3beta inactivation may benefit facilitated OL regeneration and myelin repair.
our data show that fit T-cell receptor signaling suppresses tumor development mediated by Pten loss-of-function and point towards a role of Pten in positive selection.
These findings suggested that altered tumor-associated gene expression and changed gut microbiota shape a tumor-preventive microenvironment to counteract the tumor-driving potential, leading to the tumor prevention in Pten-deficient(DeltaIEC/DeltaIEC) mice.
our results warrant a mechanistic re-interpretation of the post-transcriptional mechanisms involving Pten mRNAs and raise concerns on how miRNA-binding sites are being validated.
PTEN-deficiency induces cellular senescence that restrains tumor progression, as it involves replication stress, strategies promoting PTEN loss-induced senescence are at risk for cancer prevention and therapy.
the impact of autophagy loss in a different model of PDAC driven by oncogenic KRAS (G12D) combined with deficiency of the tumor suppressor, Phosphatase and Tensin Homolog (PTEN)-a factor lost in pancreatic ductal adenocarcinoma, was examined.
NIS has a role in thyroid cancer cells that involves PTEN signaling
data implicate PTEN in maintaining genomic stability by delaying G2/M-phase progression of damaged cells, thus allowing time for double strand break repair by homologous recombination
Taken together, these findings demonstrate a novel function of PTEN-L as a protein phosphatase for ubiquitin, which counteracts PINK1-mediated ubiquitin phosphorylation leading to blockage of the feedforward mechanisms in mitophagy induction and eventual suppression of mitophagy.
A translational variant of PTEN has been identified and termed PTEN-Long (PTEN-L). The additional 173 amino acids (PTEN-L leader) at the N-terminal constitute a potential signal peptide. Differing from canonical PTEN, PTEN-L is secreted into the extracellular fluid and re-enters recipient cells, playing the similar roles as PTEN in vivo and in vitro.
Circulating exosomal miR-301a-3p levels positively associated with depth of invasion, lymph node metastasis, late TNM stage, and poor prognosis of pancreatic cancer. Hypoxic exosomal miR-301a-3p induced the M2 polarization of macrophages via activation of the PTEN/PI3Kgamma signaling pathway.
A negative correlation between HRD1 and PTEN expression.
PTEN is dispensable for myeloid leukemia cells in response to MAPK inhibitors.
The human PTEN gene encodes a lipid phosphatase with specificity towards phosphatidylinositol (3,4,5) triphosphate (PIP3).
PTEN gene silence disorganizes the PI3K/AKT/ PTEN/mTOR signaling transduction pathway in laryngeal squamous cell carcinoma, affecting potentially the response rates to specific targeted therapeutic agents and the prognosis in those patients
Our study demonstrated that miR-21 could promote proliferation and inhibit apoptosis of hepatic stellate cells, and its mechanism may be related to PTEN/PI3K/AKT pathway.
Nuclear phosphatase and tensin homolog protein (PTEN) expression was observed in approximately half of endometrial adenocarcinoma (EndoCA) patient tumors.
Results provide evidence that PIK3CA mutation and PTEN loss coexist in prostate cancer and can cooperate in vivo to accelerate tumorigenesis and facilitate castration-resistant prostate cancer.
PTEN plays a key role in hepatocarcinogenesis and reduction of PTEN expression is related to increased expression of CD133, EpCAM and CK19 and hepatocellular carcinoma prognosis and recurrence.
PTEN-loss independently conferred higher risk for relapse in Breast Cancer.
MiR-363-3p was significantly highly expressed in osteoporotic samples. Mechanistically, miR-363-3p promotes osteoclastogenesis and inhibits osteogenic differentiation by targeting PTEN and therefore activating PI3K/AKT signaling pathway. MiR-363-3p was activated by its upstream transcription activator MYB
The BRD4-KDM5C-PTEN may be a new oncogenic pathway in CRPC development.
Low PTEN expression is associated with Pulmonary arterial hypertension.
We identified that PTEN loss and increased MET copy number may predict an unfavorable survival in mutated-EGFR non-small-cell lung cancer patients.
PTEN and PMAIP1 are targets of miR-26a-5p and let-7g-5p, respectively.
PTEN/Akt signaling pathway contributes to cardiomyocyte apoptosis after coronary microembolization.
Data suggest the development of phosphatase and tensin homolog deleted on chromosome ten (PTEN)-based anti-inflammatory strategies.
PTEN, FOXO3A and PKB were expressed in a stage- and cell-specific manner during ovarian follicle formation and development in the fetal and neonatal pig.
phosphatase and tensin homolog( PTEN) negatively regulates the enzymes involved in hepatic gluconeogenesis and lipid synthesis
the miR-17-92 cluster is involved in granulosa cell proliferation and differentiation by coordinately targeting the PTEN and BMPR2 genes.
miR-26b participates in the inflammatory response of LPS-stimulated bAMs by modulating the NF-kappaB pathway through targeting PTEN.
Pten expression levels in the mammary glands of dairy cows, was investigated.
These studies identify a key role for PTEN in the modulation of lipid mediators involved in adenosine diphosphate receptor-regulated endothelial signaling pathways involving eNOS activation in vascular endothelial cells.
Overexpressing PTEN enhanced fatty acid oxidation and assembly and secretion of VLDL in cultured hepatocytes.
Inhibition of PTEN activity had no effect on cyclic strain-mediated cell proliferation but inhibited cyclic strain-mediated suppression of apoptosis
PTEN plays an important role in multicilia formation and cilia disassembly by controlling the phosphorylation of Dishevelled.
PTEN negatively regulates growth cone phosphatidylinositol 3,4,5-trisphosphate levels and mediates chemorepulsion, whereas chemoattraction is PTEN-independent.
PTEN-dependent slowing of axonal growth enables the establishment of stable nerve-muscle contacts that develop into neuromuscular junctions.
This gene was identified as a tumor suppressor that is mutated in a large number of cancers at high frequency. The protein encoded this gene is a phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase. It contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Unlike most of the protein tyrosine phosphatases, this protein preferentially dephosphorylates phosphoinositide substrates. It negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating AKT\\/PKB signaling pathway.
mutated in multiple advanced cancers 1
, phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
, protein tyrosine phosphatase and tensin-like protein
, phosphatase and tensin homolog deleted on chromosome ten
, phosphatase and tensin homolog (mutated in multiple advanced cancers 1)
, MMAC1 phosphatase and tensin homolog deleted on chromosome 10
, phosphatase and tensin-like protein
, homolog of human mutated in multiple advanced cancers
, protein/lipid phosphatase Pten