Rapamycin inhibits poly(ADP-ribosyl)ation in intact cells
نویسندگان
چکیده
منابع مشابه
PolyADP-ribosylation is involved in neurotrophic activity.
PolyADP-ribosylation is a transient posttranslational modification of proteins, mainly catalyzed by poly(ADP-ribose)polymerase-1 (PARP-1). This highly conserved nuclear protein is activated rapidly in response to DNA nick formation and promotes a fast DNA repair. Here, we examine a possible association between polyADP-ribosylation and the activity of neurotrophins and neuroprotective peptides t...
متن کاملRapamycin inhibits poly(ADP-ribosyl)ation in intact cells.
Rapamycin is an immunosuppressive drug, which inhibits the mammalian target of rapamycin (mTOR) kinase activity inducing changes in cell proliferation. Synthesis of poly(ADP-ribose) (PAR) is an immediate cellular response to genotoxic stress catalyzed mostly by poly(ADP-ribose) polymerase 1 (PARP-1), which is also controlled by signaling pathways. Therefore, we investigated whether rapamycin af...
متن کاملPolyADP-Ribosylation in Postfertilization and Genome Reprogramming: Implications for Carcinogenesis
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PolyADP-Ribosylation Is Required for Pronuclear Fusion during Postfertilization in Mice
BACKGROUND During fertilization, pronuclear envelope breakdown (PNEB) is followed by the mingling of male and female genomes. Dynamic chromatin and protein rearrangements require posttranslational modification (PTM) for the postfertilization development. METHODOLOGY/PRINCIPAL FINDINGS Inhibition of poly(ADP-ribose) polymerase activity (PARylation) by either PJ-34 or 5-AIQ resulted in developm...
متن کاملRapamycin allosterically inhibits the proteasome.
Rapamycin is a canonical allosteric inhibitor of the mammalian tarpet of rapamycin (mTOR) kinase with immunosuppressive and proapoptotic activities. We found that in vitro rapamycin also regulates the proteasome, which is an essential intracellular protease of the ubiquitin-proteasome pathway. Rapamycin inhibits proteinase and selected peptidase activities of the catalytic core proteasome at lo...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2009
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2009.06.022