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    Mdm2 MDM2 proto-oncogene [ Rattus norvegicus (Norway rat) ]

    Gene ID: 314856, updated on 14-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The Expression of MDM2 Gene Promoted Chondrocyte Proliferation in Rats with Osteoarthritis via the Wnt/beta-Catenin Pathway.

    The Expression of MDM2 Gene Promoted Chondrocyte Proliferation in Rats with Osteoarthritis via the Wnt/β-Catenin Pathway.
    Jiang J, Feng S, Li Z, Luo Y, Wang Z, Li M, Wu G.

    07/16/2022
    ZEB2, interacting with MDM2, contributes to the dysfuntion of brain microvascular endothelial cells and brain injury after intracerebral hemorrhage.

    ZEB2, interacting with MDM2, contributes to the dysfuntion of brain microvascular endothelial cells and brain injury after intracerebral hemorrhage.
    Guo Q, Xie M, Guo M, Yan F, Li L, Liu R., Free PMC Article

    04/16/2022
    LncRNA UCA1 protects cardiomyocytes against hypoxia/reoxygenation induced apoptosis through inhibiting miR-143/MDM2/p53 axis.

    LncRNA UCA1 protects cardiomyocytes against hypoxia/reoxygenation induced apoptosis through inhibiting miR-143/MDM2/p53 axis.
    Wang QS, Zhou J, Li X.

    10/3/2020
    Tempo-spatial alternative polyadenylation analysis reveals that 3' UTR lengthening of Mdm2 regulates p53 expression and cellular senescence in aged rat testis.

    Tempo-spatial alternative polyadenylation analysis reveals that 3' UTR lengthening of Mdm2 regulates p53 expression and cellular senescence in aged rat testis.
    Wang L, Chen M, Fu H, Ni T, Wei G.

    09/26/2020
    only MDM2/FRS2 low-grade osteosarcoma was dedifferentiated parosteal osteosarcoma

    Consistent Amplification of FRS2 and MDM2 in Low-grade Osteosarcoma: A Genetic Study of 22 Cases With Clinicopathologic Analysis.
    He X, Pang Z, Zhang X, Lan T, Chen H, Chen M, Yang H, Huang J, Chen Y, Zhang Z, Jing W, Peng R, Zhang H.

    08/31/2019
    Murine double minute-2-forkhead box O1-thrombospondin-1 pathway plays an important role in angio-regulation of the skeletal muscle in the pathophysiological context of type 1 diabetes.

    Hyperglycaemia correlates with skeletal muscle capillary regression and is associated with alterations in the murine double minute-2/forkhead box O1/thrombospondin-1 pathway in type 1 diabetic BioBreeding rats.
    Aiken J, Mandel ER, Riddell MC, Birot O.

    03/16/2019
    The results indicate that the miR-188-3p-MDM2-p53 axis may have a critical role in sevoflurane-induced cognitive dysfunction.

    MicroRNA-188-3p is involved in sevoflurane anesthesia-induced neuroapoptosis by targeting MDM2.
    Wang L, Zheng M, Wu S, Niu Z., Free PMC Article

    08/18/2018
    MDM2 is involved in fibroblast activation, mediating renal tubulointerstitial fibrosis via a p53-independent pathway dependant on Notch1 ubiquitination and proteasome degradation.

    MDM2 mediates fibroblast activation and renal tubulointerstitial fibrosis via a p53-independent pathway.
    Ye C, Tang H, Zhao Z, Lei CT, You CQ, Zhang J, Gao P, He FF, Chen S, Wang YM, Zhang C, Su H.

    07/15/2017
    Study showed that demonstrate that Mdm2 intertwines the mammalian target of RAPA, mTOR, and the receptor kinase GRK2 in regulating the desensitization/inactivation of the GPR17 receptor

    The ubiquitin ligase Mdm2 controls oligodendrocyte maturation by intertwining mTOR with G protein-coupled receptor kinase 2 in the regulation of GPR17 receptor desensitization.
    Fumagalli M, Bonfanti E, Daniele S, Zappelli E, Lecca D, Martini C, Trincavelli ML, Abbracchio MP.

    07/30/2016
    High concentration glucose decrease the mRNA expression and cytosolic concentration of Mdm2.

    Hyperglycemia promotes p53-Mdm2 interaction but reduces p53 ubiquitination in RINm5F cells.
    Barzalobre-Gerónimo R, Flores-López LA, Baiza-Gutman LA, Cruz M, García-Macedo R, Ávalos-Rodríguez A, Contreras-Ramos A, Díaz-Flores A, Ortega-Camarillo C.

    02/20/2016
    Explored expression of MMP-9 and MDM2 in the oncogenesis of lung cancer in rats.

    Expression and significance of MMP-9 and MDM2 in the oncogenesis of lung cancer in rats.
    Zhang DH, Zhang LY, Liu DJ, Yang F, Zhao JZ.

    04/4/2015
    these data strongly suggested that SCYL1BP1 is a novel transcriptional activator in neurite outgrowth by directly modulating the Mdm2/p53-dependent pathway, which might play an important role in CNS development and axonal regeneration after injury.

    SCYL1BP1 modulates neurite outgrowth and regeneration by regulating the Mdm2/p53 pathway.
    Liu Y, Chen Y, Lu X, Wang Y, Duan Y, Cheng C, Shen A., Free PMC Article

    05/25/2013
    These results define Mdm2 as a crucial regulator of capillary maintenance and exercise-induced angiogenesis in skeletal muscle.

    Murine double minute-2 expression is required for capillary maintenance and exercise-induced angiogenesis in skeletal muscle.
    Roudier E, Forn P, Perry ME, Birot O., Free PMC Article

    02/2/2013
    results suggest that under some physiological conditions the oncoprotein MDM2 may cooperate with p53 to regulate the osteocalcin gene during osteoblastic differentiation.

    p53 and MDM2 are involved in the regulation of osteocalcin gene expression.
    Chen H, Kolman K, Lanciloti N, Nerney M, Hays E, Robson C, Chandar N., Free PMC Article

    05/26/2012
    p53 activation by MDM2 inhibition prevented cellular proliferation, migration, and NF-kappaB activation in vascular smooth muscle cells.

    Inhibition of MDM2 attenuates neointimal hyperplasia via suppression of vascular proliferation and inflammation.
    Hashimoto T, Ichiki T, Ikeda J, Narabayashi E, Matsuura H, Miyazaki R, Inanaga K, Takeda K, Sunagawa K.

    12/31/2011
    PKB/Akt activation inhibits p53-mediated HIF1A degradation that is independent of MDM2.

    PKB/Akt activation inhibits p53-mediated HIF1A degradation that is independent of MDM2.
    Choy MK, Movassagh M, Bennett MR, Foo RS.

    01/25/2010
    Increased Mdm2 expression is associated with transactivation at the P2 AP-1 RE (rather than the p53 or Ets REs), and Mdm2 induction potentially represents a cardioprotective response to oxidative stress.

    Regulation of expression of the rat orthologue of mouse double minute 2 (MDM2) by H(2)O(2)-induced oxidative stress in neonatal rat cardiac myocytes.
    Pikkarainen S, Kennedy RA, Marshall AK, Tham el L, Lay K, Kriz TA, Handa BS, Clerk A, Sugden PH., Free PMC Article

    01/21/2010
    CDK inhibitors suppress MDM2 levels and enhance p53 expression that facilitates bile acid-induced, ceramide-dependent CD95 activation to induce both apoptosis and autophagy in primary hepatocytes

    Multiple cyclin kinase inhibitors promote bile acid-induced apoptosis and autophagy in primary hepatocytes via p53-CD95-dependent signaling.
    Zhang G, Park MA, Mitchell C, Walker T, Hamed H, Studer E, Graf M, Rahmani M, Gupta S, Hylemon PB, Fisher PB, Grant S, Dent P., Free PMC Article

    01/21/2010
    survival signals generated by PLD1 suppress DNA damage-induced increases in p53 stabilization and cause increased expression of MDM2 and increased turnover of p53

    Phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increases in p53.
    Hui L, Abbas T, Pielak RM, Joseph T, Bargonetti J, Foster DA., Free PMC Article

    01/21/2010
    Increased expression of MDM2 is associated with mammary tumorigenesis

    Increased expression of MDM2, cyclin D1, and p27Kip1 in carcinogen-induced rat mammary tumors.
    Murray SA, Yang S, Demicco E, Ying H, Sherr DH, Hafer LJ, Rogers AE, Sonenshein GE, Xiao ZX.

    01/21/2010
    MDM2 is an E3 ubiquitin ligase with a role in regulation of cardiomyocyte survival and hypertrophy

    Differential regulation of cardiomyocyte survival and hypertrophy by MDM2, an E3 ubiquitin ligase.
    Toth A, Nickson P, Qin LL, Erhardt P.

    01/21/2010
    We conclude that UPI induces an increase in p53 phosphorylation without a corresponding increase in MDM2 expression, and we speculate that this response may contribute to the increased apoptosis previously described in the IUGR kidney.

    Uteroplacental insufficiency increases p53 phosphorylation without triggering the p53-MDM2 functional circuit response in the IUGR rat kidney.
    Baserga M, Hale MA, Ke X, Wang ZM, Yu X, Callaway CW, McKnight RA, Lane RH.

    01/21/2010
    interaction of free arrestins with JNK3 and Mdm2 and their ability to regulate subcellular localization of these proteins may play an important role in the survival of photoreceptors and other neurons

    Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm.
    Song X, Raman D, Gurevich EV, Vishnivetskiy SA, Gurevich VV., Free PMC Article

    01/21/2010
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