Activation of mitogen-activated protein kinase phosphatase-1 (MKP-1), dual-specificity protein phosphatase, set the mitogen-activated protein kinase signaling. C-Jun N-terminal kinase (JNK) and p38 activated cisplatin-induced renal injury. However, changes in the expression of MKP-1 cisplatin-induced kidney injury and the effects of regulation sirtuin 2 (SIRT2), a nicotinamide adenine dinucleotide dependent deacetylase, the MKP-1 remains unknown.
To solve this problem, we use the constitution Sirt2 knockout (KO) mice, transgenic (TG) mice with increased expression of SIRT2 particularly in the proximal tubule epithelial cellsand wild-type (WT) mice. Cisplatin nephrotoxicity induced by intraperitoneal injection of cisplatin.MKP-1 expression in the kidney to decline after cisplatin treatment. Cisplatin-induced downregulation of MKP-1 KO mice Sirt2 reversed in the kidneys and then decreased in TG mice Sirt2 kidney.
We observed a similar phenomenon with SIRT2-knockdown or SIRT2-expressed in tubular epithelial cells. Phosphorylation of p38 and JNK, downstream signaling pathways MKP-1, is increased in WT mice after treatment with cisplatin kidney. Decrease SIRT2 suppressed cisplatin-induced phosphorylation of p38 and JNK in renal and tubular epithelial cells.
Excess of SIRT2 increase phosphorylation of p38 and JNK in renal and tubular epithelial cells. Acetylation of MKP-1 increased significantly in SIRT2-knockdown cells and a decrease in SIRT2-expressed cells after stimulation cisplatin. Sirt2 KO mice and Sirt2 TG mice showed improvement and aggravation of kidney injury, apoptosis, necroptosis and inflammation caused by cisplatin.Our data showed that SIRT2 associated with cisplatin-induced renal injury through regulation MKP-1 expression.
SIRT2 is involved in cisplatin-induced acute kidney injury through regulation of mitogen-activated protein kinase phosphatase–1.
Protein phosphatase one controls the activity of a balance between collective and singular mode of cell migration.
collective cell migration is central to many developmental and pathological processes. However, the collective mechanisms that keep cells together and coordinate the movement of some cells are poorly understood. Using a Drosophila Model border cell migration, we found that cell cohesion protein phosphatase 1 (PP1) activity collective control and migration.
Inhibition of PP1 causes cells to get round the border, which split off, and move it as single cell motility changes. We are proof that PP1 promoting appropriate levels of cadherin-catenin protein-complex at the intersection of the cells in the cluster to keep the cells along the border. Limiting PP1 actomyosin contractility advanced to the outskirts of the cluster rather than on the internal border cell contact that individual. We showed that the myosin phosphatase PP1 complex, which blocks non-muscle myosin II- (Myo-II) activity, cell shape and the boundary coordinates of cluster cohesion.
Given the high conservation of the PP1 complex, this study identifies collective PP1 as the main regulator of the single cell migration. Protein phosphatase methylesterase 1 has been identified as a new gene that is upregulated in skeletal muscle in response to neurogenic atrophy in mice. Western blot analysis confirms that Ppme1 expressed during both muscle cell proliferation and differentiation.
Description: A polyclonal antibody against PPP1R15A. Recognizes PPP1R15A from Human. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1:500-2000, ELISA:1:10000-20000
Description: A polyclonal antibody against PPP1R15A. Recognizes PPP1R15A from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The induction of this gene by ionizing radiation occurs in certain cell lines regardless of p53 status, and its protein response is correlated with apoptosis following ionizing radiation.
Description: Pre-made over-expression lentivirus for expressing human target: h PPP1R15A (protein phosphatase 1, regulatory subunit 15A), [alternative names: GADD34]. The sub-cloned codon sequence is identical (100% match) to CDS region in NCBI ID: NM_014330.3 . It also contains a RFP-Blasticidin dual selection marker.
Description: Description of target: Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'. In case of infection with vesicular stomatitis virus (VSV), impairs viral replication.5 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.6"Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha."_x005F_x005F_x000D_Novoa I., Zeng H., Harding H.P., Ron D._x005F_x005F_x000D_J. Cell Biol. 153:1011-1022(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PP1, MUTAGENESIS OF VAL-549.Ref.8"Stress-induced gene expression requires programmed recovery from translational repression."_x005F_x005F_x000D_Novoa I., Zhang Y., Zeng H., Jungreis R., Harding H.P., Ron D._x005F_x005F_x000D_EMBO J. 22:1180-1187(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION.Ref.9"The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice."_x005F_x005F_x000D_Kojima E., Takeuchi A., Haneda M., Yagi A., Hasegawa T., Yamaki K., Takeda K., Akira S., Shimokata K., Isobe K._x005F_x005F_x000D_FASEB J. 17:1573-1575(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.Ref.10"Gadd34 requirement for normal hemoglobin synthesis."_x005F_x005F_x000D_Patterson A.D., Hollander M.C., Miller G.F., Fornace A.J. Jr._x005F_x005F_x000D_Mol. Cell. Biol. 26:1644-1653(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.Ref.11"Suppression of viral replication by stress-inducible GADD34 protein via the mammalian serine/threonine protein kinase mTOR pathway."_x005F_x005F_x000D_Minami K., Tambe Y., Watanabe R., Isono T., Haneda M., Isobe K., Kobayashi T., Hino O., Okabe H., Chano T., Inoue H._x005F_x005F_x000D_J. Virol. 81:11106-11115(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION. ;Species reactivity: Mouse;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.057 ng/mL
Description: Description of target: Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.6"Potential molecular mechanism for rodent tumorigenesis: mutational generation of Progression Elevated Gene-3 (PEG-3)."_x005F_x005F_x000D_Su Z.-Z., Emdad L., Sarkar D., Randolph A., Valerie K., Yacoub A., Dent P., Fisher P.B._x005F_x005F_x000D_Oncogene 24:2247-2255(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTANT PEG-3. ;Species reactivity: Rat;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 0.118 ng/mL
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Goat Anti-PPP1R15A / GADD34 . This antibody is tested and proven to work in the following applications:
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in tissue homogenates, cell lysates and other biological fluids.
Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in tissue homogenates, cell lysates and other biological fluids.
Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in tissue homogenates, cell lysates and other biological fluids.
Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in tissue homogenates, cell lysates and other biological fluids.
Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in Tissue homogenates, cell lysates and other biological fluids.
Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in Tissue homogenates, cell lysates and other biological fluids.
Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in Tissue homogenates, cell lysates and other biological fluids.
Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in Tissue homogenates, cell lysates and other biological fluids.
Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) ELISA Kit
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Mouse Protein Phosphatase 1, Regulatory Subunit 15A ELISA Kit (PPP1R15A)
Description: A sandwich ELISA kit for detection of Protein Phosphatase 1, Regulatory Subunit 15A from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: A sandwich ELISA kit for detection of Protein Phosphatase 1, Regulatory Subunit 15A from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids.
Description: A Rabbit polyclonal antibody against Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A). This antibody is labeled with Biotin.
Description: A Rabbit polyclonal antibody against Mouse Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A). This antibody is labeled with APC-Cy7.
Description: A Rabbit polyclonal antibody against Rat Protein Phosphatase 1, Regulatory Subunit 15A (PPP1R15A). This antibody is labeled with APC-Cy7.
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In addition, Ppme1 promoter active in muscle cells, while mutation of conserved E-box element prevents full induction Ppme1 reporter gene, suggesting that Ppme1 is transcriptionally regulated by myogenic regulatory factors. Interestingly, immunofluorescence analysis showed that Ppme1 localized to both the cytoplasm and nucleus, whereas cell fractionation showed that Ppme1 only found in the cytoplasm. Functional studies revealed that the inhibition of muscle cell differentiation Ppme1 use AMZ30 ABL127 or attenuates.
