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Example sentences for: ornithine
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The best-characterized example of ubiquitin-independent degradation is the degradation of ornithine decarboxylase (ODC), which is dependent upon ODC interaction with the targeting protein antizyme (Az) [ 18 ] . How ubiquitinated substrates or Az-bound ODC is recognized by the 26S proteasome is not well understood.
Many studies have shown that chronic intravenous infusion of norepinephrine is sufficient to cause hypertrophy, and that various forms of hypertrophy are linked to a decrease in either beta-adrenergic receptor density or a decreased responsiveness to beta-adrenergic stimulation [ 46 48 49 56 57 58 59 60 61 62 63 ] . Barth, for example, showed that norepinephrine infusion induced left ventricular hypertrophy that could be prevented by an adrenergic-receptor blocker [ 58 ] . It has been suggested that ornithine decarboxylase is a link between beta-adrenoreceptors and stimulation of tissue growth factor, which results in hypertrophy [ 64 ] . However, recent studies have focused on alpha-adrenergic reception as a mediator of cardiac hypertrophy [ 35 ] , although some question the role of the alpha-adrenergic receptor as a hypertrophic mediator in vivo [ 34 ] . To date, no published studies of which we are aware have examined alpha-adrenergic reception and the development of cardiac hypertrophy with iron deficiency.
The 26S proteasome is responsible for the bulk turnover of cytoplasmic and nuclear proteins in eukaryotic cells and also plays a key role in the regulation of cell cycle, signal transduction, transcription as well as antigen presentation [ 17 18 19 20 21 ] . Most of the known proteasomal substrates are marked and targeted to proteasome by ubiquitination [ 17 19 20 ] . Ubiquitination, however, is not an obligatory step for substrate targeting to proteasome [ 17 18 20 ] . The degradation of the ornithine decarboxylase (ODC), the rate-limiting enzyme for polyamine synthesis, involves a protein named antizyme (Az), which binds and targets ODC to 26S proteasome for degradation [ 18 ] . However, ODC has remained an "orphan" in Az-dependent proteasomal degradation.
Az was previously identified as a polyamine-inducible factor that binds and targets the ornithine decarboxylase (ODC) to proteasome for degradation [ 18 45 ] . Until now, ODC is the only protein known to be targeted by Az to proteasome, although the existence of additional proteins targeted by Az to proteasome has been suspected [ 20 ] . We now find two new Az interactors: Smad1, the key signal transducer of BMPs, as well as SNIP1, the nuclear repressor of CBP/p300.
The transcript encoding ornithine decar-boxylase (ODC), a known androgen target that catalyzes the rate-limiting step in polyamine biosynthesis [ 26], was induced coordinately with enzymes that catalyze downstream steps in polyamine synthetic pathway (spermine synthase, spermidine/spermine N 1-acetyltransferase, and S-adenosylmethionine decarboxylase) (Figure 5c).
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