Albumin synthesis in regenerating rat liver cells

Riassunto Gli autori hanno studiatoin vitro il problema della sintesi dell'albumina in sezioni di fegato normale e rigenerante di ratto. La quantità di albumina prodotta durante l'incubazione non presenta notevoli variazioni nelle due situazioni studiate. Al contrario l'incorporazione di glicina marcata nella albumina del fegato rigenerante risulta nettamente aumentata rispetto a quella del fegato normale. Tale comportamento viene interpretato come espressione di un ricambio albuminico più elevato nel fegato rigenerante che nel normale.

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This investigation was aided by a grant from C.N.R., Roma, and was made during a tenure by one of us (G. G.) of a Scholarship from C.N.R., Roma.     

Depressed synthesis of DNA in regenerating rat liver after spinal cord (C7) transection

Zusammenfassung Nachweis, dass Querschnittläsion des Rückenmarkes in der Höhe C₇ bei Ratten nach partieller Hepatektomie zu bedeutender Hemmung der Auswertung von Thymidin für die DNS-Synthese in der regenerierenden Leber führt.     

Inhibition of protein synthesis in ischaemic liver from phenobarbitone-treated rat.

Both ribosomal factors and cytosolic inhibitors are involved in the reduction of the rate of protein synthesis which occurs in the ischaemic hepatocyte from control and phenobarbitone-treated livers. Of these 2 factors it is the latter which seems to play a major role in determining the irreversible impairment of protein synthesis. Phenobarbitone administration has no effect on the rate of protein synthesis of ischaemic and post-ischaemic hepatocyte.     

Inhibition of rat liver transglutaminase by nucleotides

Summary Tissue-type transglutaminase (TGase) was purified from rat liver, and the effects of nucleotides on its activity were examined. The enzyme activity is inhibited by ATP in a concentration-dependent way, with complete inhibition by 3 mM ATP. Partially-purified TGase from human brain was inhibited by ATP in a manner similar to that observed with the rat liver enzyme. This suggests that the inhibition is a common phenomenon for tissue-type TGase in all species and tissues. The inhibition is reversible since full activity is restored by lowering the ATP concentration. CTP has a TGase-inhibitory potency equivalent to that of ATP, whereas GTP and UTP possess about 50% of the inhibitory activity of ATP. ADP inhibits TGase activity to the same extent as ATP, but AMP causes much less inhibition, and there is no inhibition by adenosine or adenine. The inhibition by ATP is insensitive to ionic strength and is non-competitive with the substrate putrescine. Since ATP levels in cells are of mM order, these results suggest that TGase activity is controlled by ATP in vivo.     

Inhibition by carbaryl of DNA,RNA and protein synthesis in cultured rat lung cells

Summary The carbamate pesticide carbaryl rapidly inhibited DNA, RNA and protein synthesis in L-2 cells from rat lung. the inhibiton was partly reversible and was not accompanied by inhibiton of transport of tritiated precursors into intracellular pools or destruction of the integrity of the cell membrane.We thank W. H. J. Douglas for his gift of L-2 cells.This work was supported by contract 22140 of the Kentucky Tobacco Research Board.     

Inhibition of DNA synthesis by lidocaine and procaine

Zusammenfassung Nachweis, dass in Ehrlich-Ascites-Zellen die DNS-Synthese durch Lokalanaesthetika stärker gehemmt wird als die RNS- und die Proteinsynthese.     

Effects of cycloheximide on protein synthesis in human lung tumors,regenerating rat liver and hepatomas

Summary 10^–4 M cycloheximide (CHM) inhibits leucine incorporation to about the same degree in slices of human lung tumors, rat hepatomas, regenerating livers and normal tissues. At 10^–6 M, CHM has a more pronounced effect on tumor tissue and regenerating liver than on normal tissues. 10^–8 M CHM stimulates protein synthesis in normal rat liver slices.     

Effects of cycloheximide on protein synthesis in human lung tumors, regenerating rat liver and hepatomas

10(-4) M cycloheximide (CHM) inhibits leucine incorporation to about the same degree in slices of human lung tumors, rat hepatomas, regenerating livers and normal tissues. At 10(-6) M, CHM has a more pronounced effect on tumor tissue and regenerating liver than on normal tissues. 10(-8) M CHM stimulates protein synthesis in normal rat liver slices.     

Inhibition of rat liver transglutaminase by nucleotides.

Tissue-type transglutaminase (TGase) was purified from rat liver, and the effects of nucleotides on its activity were examined. The enzyme activity is inhibited by ATP in a concentration-dependent way, with complete inhibition by 3 mM ATP. Partially-purified TGase from human brain was inhibited by ATP in a manner similar to that observed with the rat liver enzyme. This suggests that the inhibition is a common phenomenon for tissue-type TGase in all species and tissues. The inhibition is reversible since full activity is restored by lowering the ATP concentration. CTP has a TGase-inhibitory potency equivalent to that of ATP, whereas GTP and UTP possess about 50% of the inhibitory activity of ATP. ADP inhibits TGase activity to the same extent as ATP, but AMP causes much less inhibition, and there is no inhibition by adenosine or adenine. The inhibition by ATP is insensitive to ionic strength and is non-competitive with the substrate putrescine. Since ATP levels in cells are of mM order, these results suggest that TGase activity is controlled by ATP in vivo.