scholarly journals Stimulation of Protein Synthesis in Mouse Liver by Insect-Moulting Steroids

1968 ◽  
Vol 16 (2) ◽  
pp. 384-387 ◽  
Author(s):  
SEIICHI OKUI ◽  
TADAHIKO OTAKA ◽  
MITSURU UCHIYAMA ◽  
TSUNEMATSU TAKEMOTO ◽  
HIROSHI HIKINO ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Mouse Liver ◽  
Stimulation Of

scholarly journals Stimulation of Protein Synthesis in Mouse Liver by Ecdysterone

1969 ◽  
Vol 17 (1) ◽  
pp. 75-81 ◽  
Author(s):  
TADAHIKO OTAKA ◽  
SEIICHI OKUI ◽  
MITSURU UCHIYAMA
Keyword(s):  
Protein Synthesis ◽  
Mouse Liver ◽  
Stimulation Of

Growth Hormone Stimulation of Protein Synthesis in Isolated Mouse Liver Mitochondria1

Endocrinology ◽  
1967 ◽  
Vol 80 (4) ◽  
pp. 772-774 ◽  
Author(s):  
PATRICK F. DELANEY ◽  
MICHAEL J. KEYES ◽  
THOMAS I. SOULE
Keyword(s):  
Growth Hormone ◽  
Protein Synthesis ◽  
Mouse Liver ◽  
Hormone Stimulation ◽  
Stimulation Of

EFFECT OF ACTINOMYCIN D ON TSH-INDUCED STIMULATION OF THYROIDAL PROTEIN SYNTHESIS IN THE RAT

1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
The Other ◽  
Leucine Incorporation ◽  
Short Term ◽  
Other Hand ◽  
Thyroid Glands ◽  
Translational Level ◽  
Stimulation Of

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.

scholarly journals Stimulation of uracil nucleotide synthesis in mouse liver, intestine and kidney by ammonium chloride infusion

1988 ◽  
Vol 175 (1) ◽  
pp. 193-198 ◽  
Author(s):  
Daniel W. ZAHAREVITZ ◽  
Elizabeth A. NAPIER ◽  
Lawrence W. ANDERSON ◽  
John M. STRONG ◽  
Richard L. CYSYK
Keyword(s):  
Ammonium Chloride ◽  
Mouse Liver ◽  
Nucleotide Synthesis ◽  
Uracil Nucleotide ◽  
Stimulation Of

Role of insulin and IGF-I in activation of muscle protein synthesis after oral feeding

1996 ◽  
Vol 270 (4) ◽  
pp. E614-E620 ◽  
Author(s):  
E. Svanberg ◽  
H. Zachrisson ◽  
C. Ohlsson ◽  
B. M. Iresjo ◽  
K. G. Lundholm
Keyword(s):  
Protein Synthesis ◽  
Skeletal Muscles ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Oral Feeding ◽  
Myofibrillar Proteins ◽  
Diabetic Mice ◽  
Igf I ◽  
Stimulation Of

The aim was to evaluate the role of insulin and insulin-like growth factor I (IGF-I) in activation of muscle protein synthesis after oral feeding. Synthesis rate of globular and myofibrillar proteins in muscle tissue was quantified by a flooding dose of radioactive phenylalanine. Muscle tissue expression of IGF-I mRNA was measured. Normal (C57 Bl) and diabetic mice (type I and type II) were subjected to an overnight fast (18 h) with subsequent refeeding procedures for 3 h with either oral chow intake or provision of insulin, IGF-I, glucose, and amino acids. Anti-insulin and anti-IGF-I were provided intraperitoneally before oral refeeding in some experiments. An overnight fast reduced synthesis of both globular (38 +/- 3%) and myofibrillar proteins (54 +/- 3%) in skeletal muscles, which was reversed by oral refeeding. Muscle protein synthesis, after starvation/ refeeding, was proportional and similar to changes in skeletal muscle IGF-I mRNA expression. Diabetic mice responded quantitatively similarly to starvation/refeeding in muscle protein synthesis compared with normal mice (C57 Bl). Both anti-insulin and anti-IGF-I attenuated significantly the stimulation of muscle protein synthesis in response to oral feeding, whereas exogenous provision of either insulin or IGF-I to overnight-starved and freely fed mice did not clearly stimulate protein synthesis in skeletal muscles. Our results support the suggestion that insulin and IGF-I either induce or facilitate the protein synthesis machinery in skeletal muscles rather than exerting a true stimulation of the biosynthetic process during feeding.

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