The effects of temperature acclimation on protein synthesis rates and nucleic acid content of juvenile cod (Gadus morhua L.)

1992 ◽  
Vol 70 (11) ◽  
pp. 2095-2102 ◽  
Author(s):  
A. R. Foster ◽  
D. F. Houlihan ◽  
S. J. Hall ◽  
L. J. Burren
Keyword(s):  
Growth Rate ◽  
Protein Synthesis ◽  
Gadus Morhua ◽  
Temperature Acclimation ◽  
Nucleic Acid Content ◽  
Translational Efficiency ◽  
Compensatory Mechanism ◽  
Tissue Protein ◽  
Tissue Protein Synthesis ◽  
Rna Concentration

Juvenile cod were acclimated to cold (5 °C) and warm (15 °C) water temperatures and fed sandeel at a similar ration size (3% body weight∙day−1) for at least 40 days. After this acclimation period, there were no significant differences in either weight-specific growth rate or weight-specific tissue protein synthesis rates (ventricle, gill, stomach, and intestine) between the cold- and warm-acclimated fish. However, every cold-acclimated tissue examined had a significantly higher RNA concentration (μg RNA∙g tissue−1) than the respective warm-acclimated tissue. Cold-acclimated ventricle and intestine had significantly reduced RNA activities (i.e., translational efficiency, g protein synthesized∙g RNA−1∙day−1) compared with the warm-acclimated tissues. In contrast, the mean RNA activities of cold-acclimated stomach and gill were not significantly different from those of the same tissues in the warm-acclimated fish. These alterations in RNA activity and RNA concentration with temperature acclimation probably represent a thermal compensatory mechanism for protein synthesis and growth in cod at 5 °C. Positive linear relationships were observed between tissue protein synthesis rates and tissue RNA concentrations (μg RNA∙g tissue−1). RNA/protein ratios (μg RNA∙mg protein−1) gave a positive (but statistically insignificant) trend with protein synthesis rates. In contrast, a negative trend (statistically insignificant) was observed between tissue protein synthesis rates and tissue RNA/DNA ratios (μg RNA∙μg DNA−1). The use of RNA measurements as biochemical correlates of growth rate in juvenile cod is discussed.

Differential effects of insulin on peripheral and visceral tissue protein synthesis in neonatal pigs

2001 ◽  
Vol 280 (5) ◽  
pp. E770-E779 ◽  
Author(s):  
Teresa A. Davis ◽  
Marta L. Fiorotto ◽  
Philip R. Beckett ◽  
Douglas G. Burrin ◽  
Peter J. Reeds ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Translational Efficiency ◽  
Fiber Types ◽  
Peripheral Tissues ◽  
Tissue Protein ◽  
Neonatal Pigs ◽  
Sarcoplasmic Proteins ◽  
Tissue Protein Synthesis ◽  
Stimulation Of

We recently demonstrated in neonatal pigs that, with amino acids and glucose maintained at fasting levels, the stimulation of protein synthesis in longissimus dorsi muscle with feeding can be reproduced by a physiological rise in insulin alone. In the current report, we determine whether the response of protein synthesis to insulin in the neonatal pig is 1) present in muscles of different fiber types, 2) proportional in myofibrillar and sarcoplasmic proteins, 3) associated with increased translational efficiency and ribosome number, and 4) present in other peripheral tissues and in viscera. Hyperinsulinemic-euglycemic-amino acid clamps were performed in 7- and 26-day-old pigs infused with 0, 30, 100, or 1,000 ng · kg−0.66 · min−1 of insulin to reproduce insulin levels present in fasted, fed, refed, and supraphysiological conditions, respectively. Tissue protein synthesis was measured using a flooding dose ofl-[4-3H]phenylalanine. Insulin increased protein synthesis in gastrocnemius muscle and, to a lesser degree, masseter muscle. The degree of stimulation of protein synthesis by insulin was similar in myofibrillar and sarcoplasmic proteins. Insulin increased translational efficiency but had no effect on ribosome number in muscle. All of these insulin-induced changes in muscle protein synthesis decreased with age. Insulin also stimulated protein synthesis in cardiac muscle and skin but not in liver, intestine, spleen, pancreas, or kidney. The results support the hypothesis that insulin mediates the feeding-induced stimulation of myofibrillar and sarcoplasmic protein synthesis in muscles of different fiber types in the neonate by increasing the efficiency of translation. However, insulin does not appear to be involved in the feeding-induced stimulation of protein synthesis in visceral tissues. Thus different mechanisms regulate the growth of peripheral and visceral tissues in the neonate.

scholarly journals Dietary Ornithine Affects the Tissue Protein Synthesis Rate in Young Rats

2012 ◽  
Vol 58 (4) ◽  
pp. 297-302 ◽  
Author(s):  
Kazuyo TUJIOKA ◽  
Takashi YAMADA ◽  
Mami AOKI ◽  
Koji MORISHITA ◽  
Kazutoshi HAYASE ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Young Rats ◽  
Tissue Protein Synthesis

Effects of the Fusarium toxin deoxynivalenol on tissue protein synthesis in pigs

2006 ◽  
Vol 165 (3) ◽  
pp. 297-311 ◽  
Author(s):  
S DANICKE ◽  
T GOYARTS ◽  
S DOLL ◽  
N GROVE ◽  
M SPOLDERS ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Tissue Protein ◽  
Fusarium Toxin ◽  
Tissue Protein Synthesis

Methionine Flux and Tissue Protein Synthesis in Lactating and Dry Goats

1990 ◽  
Vol 120 (9) ◽  
pp. 1006-1015 ◽  
Author(s):  
Claude Champredon ◽  
Elisabeth Debras ◽  
Philippe Patureau Mirand ◽  
Maurice Arnal
Keyword(s):  
Protein Synthesis ◽  
Tissue Protein ◽  
Tissue Protein Synthesis

scholarly journals Acute IGF-I infusion stimulates protein synthesis in skeletal muscle and other tissues of neonatal pigs

2002 ◽  
Vol 283 (4) ◽  
pp. E638-E647 ◽  
Author(s):  
Teresa A. Davis ◽  
Marta L. Fiorotto ◽  
Douglas G. Burrin ◽  
Rhonda C. Vann ◽  
Peter J. Reeds ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Cardiac Muscle ◽  
Liver Protein ◽  
Tissue Protein ◽  
Neonatal Pigs ◽  
Igf I ◽  
Tissue Protein Synthesis ◽  
Insulin Replacement

Studies have shown that protein synthesis in skeletal muscle of neonatal pigs is uniquely sensitive to a physiological rise in both insulin and amino acids. Protein synthesis in cardiac muscle, skin, and spleen is responsive to insulin but not amino acid stimulation, whereas in the liver, protein synthesis responds to amino acids but not insulin. To determine the response of protein synthesis to insulin-like growth factor I (IGF-I) in this model, overnight-fasted 7- and 26-day-old pigs were infused with IGF-I (0, 20, or 50 μg · kg−1 · h−1) to achieve levels within the physiological range, while amino acids and glucose were clamped at fasting levels. Because IGF-I infusion lowers circulating insulin levels, an additional group of high-dose IGF-I-infused pigs was also provided replacement insulin (10 ng · kg−0.66 · min−1). Tissue protein synthesis was measured using a flooding dose ofl-[4-3H]phenylalanine. In 7-day-old pigs, low-dose IGF-I increased protein synthesis by 25–60% in various skeletal muscles as well as in cardiac muscle (+38%), skin (+24%), and spleen (+32%). The higher dose of IGF-I elicited no further increase in protein synthesis above that found with the low IGF-I dose. Insulin replacement did not alter the response of protein synthesis to IGF-I in any tissue. The IGF-I-induced increases in tissue protein synthesis decreased with development. IGF-I infusion, with or without insulin replacement, had no effect on protein synthesis in liver, jejunum, pancreas, or kidney. Thus the magnitude, tissue specificity, and developmental change in the response of protein synthesis to acute physiological increases in plasma IGF-I are similar to those previously observed for insulin. This study provides in vivo data indicating that circulating IGF-I and insulin act on the same signaling components to stimulate protein synthesis and that this response is highly sensitive to stimulation in skeletal muscle of the neonate.

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