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D M Robins

Publications and source records attributed to D M Robins.

38 records · Page 3Linked to original sources

Differential effects of estrogen and progesterone on ovalbumin mRNA utilization.

Progesterone treatment of estrogen-primed chicks leads to a shift in the oviduct polysome profile and an increase in the proportion of cytoplasmic RNA which is ovalbumin mRNA. To determine whether the progesterone effect is primarily transcriptional or translational and whether it is separable from estrogen action, rapid estrogen withdrawal by the anti-estrogen tamoxifen was compared in the presence and absence of progesterone. After estrogen stimulation, 24 h of tamoxifen treatment causes ovalbumin synthesis and ovalbumin mRNA levels to fall 10-fold. The proportion of ovalbumin mRNA in the monosome and supernatant fractions of the polysome profile increases; however, these sequences can associate with polysomes if elongation is inhibited by cycloheximide. Progesterone prevents the tamoxifen effects, even if administered 9 h after tamoxifen (at which time ov mRNA has decreased by 30%). The progesterone-induced increase of ovalbumin mRNA (from 0.64% of cytoplasmic RNA to 0.79%) and the increased proportion of ribosomes in polysomes (from 65% to 80%) are thus independent of estrogen action. Twenty-four hours of progesterone plus tamoxifen treatment enhances initiation of translation. However, after prolonged treatments of several days, translation becomes inefficient: ovalbumin synthesis falls by 30% without a coordinate decrease in ovalbumin mRNA, and a significant proportion (15%) of the ovalbumin mRNA becomes localized in monosomes. Thus, optimal maintenance of oviduct mRNA utilization requires the presence of estrogen.

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Regulation of translation of ovalbumin messenger RNA by estrogens and progesterone in oviduct of withdrawn chicks.

In the oviduct of chicks withdrawn from previous treatment with estrogens, no ovalbumin synthesis can be detected, although there are a limited number of ovalbumin mRNA sequences. These sequences are predominately associated with membrane-bound ribosomes. However, the size of the polysomes is small compared to those from the laying hen, suggesting that the inability to detect ovalbumin synthesis is the result of inefficient initiation of ovalbumin synthesis. When the rate of peptide chain elongation is reduced by treatment of chicks with cycloheximide, there is an increase in the average size of polysomes and a shift of ovalbumin mRNA sequences from small to large-sized polysomes. Readministration of estrogen to withdrawn chicks results in a time-dependent shift of monosomes to polysomes and a proportional shift of ovalbumin mRNA sequences between the two fractions, indicating that estrogen stimulates the rate of initiation of all mRNA species in the oviduct to essentially the same extent. In contrast, progesterone administration results in a preferential shift of ovalbumin mRNA relative to total RNA, suggesting a preferential effect of progesterone on initiation of protein synthesis with ovalbumin mRNA.

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