Hypoxia increases the association of 4E‐binding protein 1 with the initiation factor 4E in isolated rat hepatocytes

FEBS Letters

Buc-Calderon, Pedro M.¹  Tinton, Sandrine A.¹ 

[1] Unité de Biochimie Toxicologique et Cancérologique, Université Catholique de Louvain, UCL-BCTC 7369, 73 Avenue Mounier, B-1200 Brussels, Belgium

关键词: Hypoxia;    Protein synthesis;    Phosphoprotein heat- and acid-stable induced by insulin;    Eukaryotic initiation factor;    eIF;    eukaryotic initiation factor;    4E-BP;    eIF-4E-binding protein;    PHAS-I;    phosphoprotein heat- and acid-stable induced by insulin;    mTOR;    mammalian target of rapamycin;    BSA;    bovine serum albumin;    PAGE;    polyacrylamide gel electrophoresis;    m7GTP;    7-methylguanosine triphosphate;    PMSF;    phenylmethylsulfonyl fluoride;    p70S6K;    70-kDa S6 protein kinase;   

DOI  :  10.1016/S0014-5793(99)00185-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Incubation of hepatocytes under hypoxia increases binding of translation initiation factor eIF-4E to its inhibitory regulator 4E-BP1, and this correlates with dephosphorylation of 4E-BP1. Rapamycin induced the same effect in aerobic cells but no additive effect was observed when hypoxic cells were treated with rapamycin. This enhanced association of 4E-BP1 with eIF-4E might be mediated by mTOR. Nevertheless, only hypoxia produces a rapid inhibition of protein synthesis. Although hypoxia might be signalling via the rapamycin-sensitive pathway by changing eIF-4E availability, such a pathway is unlikely to be responsible for the depression in overall protein synthesis under hypoxia.

【 授权许可】

Unknown