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At least 217 records · Page 12Linked to original sources
PubMed1990

Effects of enalapril and neuroendocrine activation on prognosis in severe congestive heart failure (follow-up of the CONSENSUS trial). CONSENSUS Trial Study Group.

This study enrolled 253 patients with severe heart failure (New York Heart Association functional class IV) from 35 centers in Scandinavia, randomly assigned to treatment with placebo or enalapril, in addition to their usual treatment for heart failure. After an initial titration period, the daily doses of enalapril ranged from 2.5 to 40 mg. At the end of the trial, 46% of the placebo-treated patients and 61% of the enalapril-treated patients were alive (p = 0.003); the survival figures at 8 months after completion of the trial were 32 and 48%, respectively (p = 0.001); and 21 and 30%, respectively (p = 0.006) at the 2-year follow-up. In the placebo group, there was a significant positive association between mortality and baseline levels of norepinephrine, epinephrine, angiotensin II, aldosterone and atrial natriuretic peptide; no such association was found in the enalapril-treated patients. The results suggest that the effects of enalapril on mortality are related to a counteraction of the neuroendocrine activation in general and to the renin-angiotensin system in particular.

Enalapril↗
PubMed2003

Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2.

During mitosis, the cyclin-dependent kinase, Cdc2, signals the inactivation of major anabolic processes such as transcription, mRNA processing, translation, and ribosome biogenesis, thereby providing energy needed for the radical and energetically costly structural reorganization of the cell. This is accomplished by phosphorylation and inactivation of several key anabolic elements, including TFIIIB, TFIID, RNA polymerase II, poly(A) polymerase, and translation elongation factor 1gamma. We report here that ribosomal S6 kinase 1 (S6K1), a protein kinase linked to the translation of ribosomal protein mRNAs, is also subject to regulation by Cdc2 in mitosis. In mitotic HeLa cells, when the activity of Cdc2 is high, S6K1 is phosphorylated at multiple Ser/Thr, Pro (S/TP) sites, including Ser(371), Ser(411), Thr(421), and Ser(424). Concomitant with this, the phosphorylation of the hydrophobic motif site, Thr(389), is reduced resulting in a decrease in the specific activity of S6K1. The mitotic S/TP phosphorylation sites are readily phosphorylated by Cdc2.cyclin B in vitro. These proline-directed phosphorylations are sensitive to chemical inhibitors of Cdc2 but not to inhibitors of mammalian target of rapamycin, phosphatidylinositol 3-kinase, MEK1/2, or p38. In murine FT210 cells arrested in mitosis, conditional inactivation of Cdc2 reduces phosphorylation of S6K1 at S/TP sites while simultaneously increasing phosphorylation of Thr(389) and of the S6K1 substrate, RPS6. A physical interaction exists between Cdc2 and S6K1, and this interaction is enhanced in mitotic cells. These results suggest that Cdc2 provides a signal that triggers inactivation of S6K1 in mitosis, presumably serving to spare energy for costly mitotic processes at the expense of ribosomal protein synthesis.

CDC2 Protein Kinase↗