This study highlights a connection between the eIF2B body and the regulation of translation initiation as a response to stress in Saccharomyces cerevisiae. Fusel alcohols are involved in signaling nitrogen scarcity to the cell and they inhibit protein synthesis by preventing the movement of the eIF2B body throughout the cell.

1. In the isolated perfused liver from 48h-starved rats, glycogen synthesis was followed by sequential sampling of the two major lobes. 2. The fastest observed rates of glycogen deposition (0.68-0.82mumol of glucose/min per g fresh liver) were obtained in the left lateral lobe, when glucose in the medium was 25-30mm and when gluconeogenic substrates were present (pyruvate, glycerol and serine: each initially 5mm). In this situation there was no net disappearance of glucose from the perfusion medium, although (14)C from [U-(14)C]glucose was incorporated into glycogen. There was no requirement for added hormones. 3. In the absence of gluconeogenic precursors, glycogen synthesis from glucose (30mm) was 0-0.4mumol/min per g. 4. When livers were perfused with gluconeogenic precursors alone, no glycogen was deposited. The total amount of glucose formed was similar to the amount converted into glycogen when 30mm-glucose was also present. 5. The time-course, maximal rates and glucose dependence of hepatic glycogen deposition in the perfused liver resembled those found in vivo in 48h-starved rats, during infusion of glucose. 6. In the perfused liver, added insulin or sodium oleate did not significantly affect glycogen synthesis in optimum conditions. In suboptimum conditions (i.e. glucose less than 25mm, or with gluconeogenic precursors absent) insulin caused a moderate acceleration of glycogen deposition. 7. These results suggest that on re-feeding after starvation in the rat, hepatic glycogen deposition could be initially the result of continued gluconeogenesis, even after the ingestion of glucose. This conclusion is discussed, particularly in connexion with the role of hepatic glucokinase, and the involvement of the liver in the glucose intolerance of starvation.

No abstract

1. Lactation results in decreased glucose and acetate utilization and increased lactate output by sheep adipose tissue. 2. The ability of insulin to stimulate acetate uptake was lost in adipose tissue from lactating sheep, whereas both the response and the sensitivity (ED50) for insulin for stimulation of glucose conversion into products other than lactate were decreased. These impairments were partly restored by prolonged incubation of adipose tissue for 48 h. 3. The ability of insulin to stimulate lactate output was not altered by lactation. 4. Dexamethasone inhibited glucose uptake, lactate output and glycerol output in adipose tissue from both non-lactating and lactating sheep, with an ED50 of about 1 nM. Dexamethasone inhibited acetate uptake by adipose tissue from non-lactating sheep, but this effect was not observed with adipose tissue from lactating sheep. 5. Dexamethasone inhibited the stimulation of glucose uptake at all concentrations of insulin used; the effect varied with insulin concentration and resulted in an accentuation of the insulin dose-response curve. The insulin dose-response curve in the presence of dexamethasone was muted during lactation. 6. The overall effect of these adaptations is to ensure that glucose and acetate utilization by adipose tissue after an insulin surge is diminished during lactation.

The effect of peak lactation on the activities of a number of enzymes of glucose and lipid metabolism of perirenal and subcutaneous adipose tissue, skeletal muscle, liver, kidney cortex and mammary parenchyma of sheep are described. Enzymes studied included hexokinase (glucose utilization), pyruvate carboxylase (gluconeogenesis), pyruvate dehydrogenase (glucose oxidation and production of acetyl CoA for fatty acid synthesis), acetyl CoA carboxylase (fatty acid synthesis) and glycerol-3-phosphate acyltransferase (fatty acid esterification). Major changes that were found include a decrease in activities of enzymes of fatty acid synthesis and esterification in adipose tissues, decreased activity of pyruvate dehydrogenase in muscle and adipose tissues and increased pyruvate carboxylase; there was no change in activities of enzyme of fatty acid esterification in liver. Activities of hexokinase, acetyl CoA carboxylase and glycerol-3-phosphate acyltransferase have been estimated per tissue; this shows the quantitative importance of limiting glucose utilization by muscle and of suppression of fatty acid synthesis in adipose tissue for efficient partitioning of nutrients for milk production.