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PIM1 destabilization is associated with cancer.
The Ser/Thr-protein kinase-1 (PIM-1) was identified as a direct target of miR (show MLXIP Proteins)-328.
Data show that PIM1 contributes to melanoma cell proliferation and tumor growth in vivo; however, the presence of PIM2 (show PIM2 Proteins) and PIM3 (show PIM3 Proteins) could also influence the outcome.
High expression level of PIM is associated with neoplasms.
This review summarizes effects of PIM kinases and their substrates especially on cancer cell migration, invasion and metastatic growth, based on data from cell-based assays, animal experiments and patients.
Results show that PIM-1 is upregulated in pancreatic cancer tissues and plasma. Its knockdown in pancreatic cancer cells suppressed proliferation, induced cell cycle arrest, enhanced apoptosis, resensitized cells to gemcitabine and erlotinib treatment, and inhibited ABCG2 and EZH2 (show EZH2 Proteins) mRNA expression.
Results show that PIM1 is overexpressed in breast cancer tumors and provide evidence for its role in tumor resistance to PI3K (show PIK3CA Proteins) inhibitors.
These results demonstrate the involvement of PIM kinases in LIF (show LIF Proteins)-induced regulation in different trophoblastic cell lines which may indicate similar functions in primary cells.
Down-regulation of UHRF1 (show UHRF1 Proteins) is an important mechanism of PIM1-mediated cellular senescence.
PIM kinases in classical Hodgkin lymphoma exhibit pleiotropic effects, orchestrating tumor immune escape and supporting Reed-Sternberg cell survival.
this study shows that Pim-1 dysregulation has developmental-stage-specific effects on B lymphopoiesis and early myeloid, but not erythroid progenitors
Results show that elevated miR (show MLXIP Proteins)-15b as an early response to Dicer (show DICER1 Proteins) depletion silenced Pim-1 kinase resulting in mitochondrial dysfunction. Rescue experiments demonstrated that suppression of miRNA-15b induction in Dicer (show DICER1 Proteins)-deleted adult hearts result in marked amelioration of cardiac dysfunction.
Pim-1L protects hepatic ABCA1 (show ABCA1 Proteins) from lysosomal degradation by facilitating the physical interaction between ABCA1 (show ABCA1 Proteins) and liver X receptor beta (show NR1H2 Proteins) and subsequent stabilization of the ABCA1 (show ABCA1 Proteins)-Pim-1L complex and thereby regulates the circulating level of high-density lipoprotein.
Pim1 kinase activity maintains airway epithelial integrity and protects against house dust mite-induced proinflammatory activation of the airway epithelium.
Pim kinases prevent premature cardiac aging and maintain a healthy pool of functional mitochondria leading to efficient cellular energetics.
Pim-1 kinase activity regulates hepatocyte growth factor (show HGF Proteins)-induced tumor cell migration, invasion, and cell scattering.
these results identify Pim1 as a novel effector molecule sufficient to drive CD4 (show CD4 Proteins)( ) alphabeta T-cell development and survival in the absence of gammac cytokine receptor (show LEPR Proteins) signaling.
Our data suggest that Pim1 might contribute to progression rather than initiation in prostate neoplasia.
Loss of PIM1 is associated with abnormal hematopoietic phenotypes.
Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI
Inhibition of the Pim1 oncogene (show RAB1A Proteins) results in diminished visual function.
Pim1 overexpression enhanced the effect of intramyocardial delivery of CSCs to infarcted porcine hearts.
The protein encoded by this gene belongs to the Ser/Thr protein kinase family, and PIM subfamily. This gene is expressed primarily in B-lymphoid and myeloid cell lines, and is overexpressed in hematopoietic malignancies and in prostate cancer. It plays a role in signal transduction in blood cells, contributing to both cell proliferation and survival, and thus provides a selective advantage in tumorigenesis. Both the human and orthologous mouse genes have been reported to encode two isoforms (with preferential cellular localization) resulting from the use of alternative in-frame translation initiation codons, the upstream non-AUG (CUG) and downstream AUG codons (PMIDs:16186805, 1825810).
, pim-1 kinase 44 kDa isoform
, pim-1 oncogene (proviral integration site 1)
, proto-oncogene serine/threonine-protein kinase pim-1
, serine/threonine-protein kinase pim-1
, pim-1 oncogene
, non-specific serine/threonine protein kinase
, proto-oncogene serine/threonine-protein kinase Pim-1
, proviral integration site 1
, kinase pim-1
, proviral integration site 2
, serine/threonine-protein kinase Pim-1
, serine/threonine-protein kinase pim-2