Normal and neoplastic human cells in culture were suspended under isotonic conditions and incubated for one minute with the substrates, including 82P-labelled inorganic phosphate, and cofactors of the glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase reactions (complete medium), a
Wasting of 18 S ribosomal RNA by human myeloma cells cultured in adenosine
β Scribed by John W. Bynum; Elliot Volkin
- Publisher
- John Wiley and Sons
- Year
- 1976
- Tongue
- English
- Weight
- 735 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0021-9541
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
When human myeloma cells are pulsed for one hour with ^3^Hβuridine and chased for six hours in fresh medium containing unlabeled uridine, the processing of 45 S rRNA precursor into the stable 28 S and 18 S rRNA components can be followed. However, when the cells are chased in exogenous adenosine instead of uridine, the accumulation of 18 S rRNA is selectively inhibited. Cells pulsed with ^3^Hβadenosine and chased in the absence of exogenous nucleosides exhibit normal rRNA precursor processing, while cells pulsed simultaneously with ^3^Hβuridine and ^3^Hβadenosine and chased with uridine and adenosine are deficient in labeled 18 S rRNA. Consequently, the inhibition of 18 S rRNA accumulation by adenosine is not an artifact of labeling nor is it relieved by an equal molar concentration of uridine. The wasting of 18 S rRNA in human myeloma cells is similar to that reported to occur in normal lymphocytes during the quiescent state.
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