title: Effect of abdominal surgery on the activity of acid and alkaline ribonucleases in rats.
abstract: Ribonucleases (RNases) are a group of enzymes that hydrolyze different classes of RNA. It has been suggested that RNase activity in cells can act to indirectly regulate protein synthesis by controlling RNA degradation. However, little is known about the role of RNases under conditions characterized by a sudden increase of protein synthesis, such as with surgical trauma. The aim of this study was to investigate the effect of abdominal surgery on acid and alkaline RNase activities in rat liver. Acid and alkaline RNase activities decreased significantly at 3 h after surgery, reaching the lowest level at 16 h (63% less than control) for the acid and 6 h (39% less than control) for the alkaline activities. Acid RNase activity returned to its initial values 20 h after surgery, while alkaline RNase activity remained decreased even 24 h after surgery. In order to determine whether the observed decreases in RNase activity were produced by RNase inhibitors (RIs), the enzymatic activities of both RNases were measured after the addition of zinc, to dissociate possible RI/RNase complexes. Zinc addition increased acid RNase activity by 61%, but had no significant effect on alkaline RNase activity. Administration of cycloheximide (an inhibitor of protein synthesis) 2 h before surgery prevented the decrease of acid RNase activity 12 h after surgery, while there was no effect on the decrease in alkaline RNase activity. These results show that surgery produces a decrease in hepatic acid and alkaline RNase activities. The decreased acid RNase activity could be a consequence of the de novo synthesis of RNase inhibitors as a response to surgical trauma, while the mechanism involved in the decrease of alkaline RNase activity is unclear. Under pathophysiological conditions, which induce a high rate of protein synthesis, such as surgical wounding, decreased acid and alkaline RNase activity could provide an important mechanism for enhanced protein synthesis, by prolonging RNA half-life.
authors.affiliation: Facultad de Ciencias Quimicas, Universidad Autonoma de Puebla, Puebla, Mexico. ebrambil@siu.buap.mx
authors.forename: E
authors.initials: E
authors.lastname: Brambila
authors.forename: N
authors.initials: N
authors.lastname: Tenorio
authors.forename: E
authors.initials: E
authors.lastname: Garcia-Luna
authors.forename: M P
authors.initials: MP
authors.lastname: Waalkes
mesh_terms: D000005:Abdomen / Q000601:surgery*; D000818:Animals; D003513:Cycloheximide / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000378:metabolism; D005260:Female; D008099:Liver / Q000201:enzymology*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D012260:Ribonucleases / Q000378:metabolism*; D013997:Time Factors
chemical_list: D004791:Enzyme Inhibitors; D011500:Protein Synthesis Inhibitors; D003513:Cycloheximide; D012260:Ribonucleases