Stimulation by N6,O2′-dibutyryl adenosine 3′,5′-cyclic-phosphate of amino acid transport, protein synthesis, and chondroitin sulfate synthesis in embryonic bone in vitro, contrasted with the effects of thyroid hormones

1970 ◽  
Vol 201 (3) ◽  
pp. 446-452 ◽  
Author(s):  
Lucile F. Adamson
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Thyroid Hormones ◽  
Chondroitin Sulfate ◽  
Amino Acid Transport ◽  
Transport Protein ◽  
Acid Transport ◽  
Cyclic Phosphate ◽  
Embryonic Bone

Effect of Carbachol on Amino Acid Incorporation into Protein of Rat Pancreas In Vitro

1974 ◽  
Vol 52 (3) ◽  
pp. 632-640 ◽  
Author(s):  
C. Irwin ◽  
A. Tenenhouse
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Secretion ◽  
Amino Acid Transport ◽  
Acid Transport ◽  
Amino Acid Incorporation ◽  
Rat Pancreas ◽  
Acid Incorporation ◽  
Muscarinic Agents

The effect of various cholinergic drugs on incorporation of 3H-leucine into protein of rat pancreas in vitro was studied. It was found that carbachol and bethanechol, but not pilocarpine, inhibited incorporation 70–80%. Even in the continued presence of carbachol, the rate of incorporation is depressed only 40–60 min. It recovers and eventually exceeds that seen in untreated tissue. After 4 h incubation the amount of 3H-leucine incorporated into protein is the same in carbachol-treated and untreated tissue. The alteration of amino acid incorporation can be dissociated from the effect of the drug on secretion in several ways: (1) calcium deprivation abolishes carbachol-stimulated secretion but not the inhibition of amino acid incorporation; (2) atropine, 10−8 M, totally abolishes the effect of carbachol on amino acid incorporation without affecting secretion (10−5 M atropine is needed to abolish carbachol stimulated secretion); (3) pilocarpine stimulates secretion but has no effect on amino acid incorporation. The inhibition of amino acid incorporation is not due to inhibition of amino acid transport nor to a decrease in tissue ATP concentration. It is concluded that there is no clear relationship between protein secretion and synthesis. Muscarinic agents, which stimulate secretion of protein, may also cause changes in the rate of amino acid incorporation into protein; however, the change one measures will depend on when, after administration of the secretagogue, protein synthesis is measured.

scholarly journals Protein turnover, growth and proliferation in CHO cells. Variation within and between mutant classes for salvage pathway enzymes

1992 ◽  
Vol 282 (1) ◽  
pp. 49-57 ◽  
Author(s):  
J M Gunn ◽  
M R Brancheau
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Amino Acid Transport ◽  
Cho Cells ◽  
Protein Turnover ◽  
Transport Protein ◽  
Clonal Variation ◽  
Acid Transport ◽  
Salvage Pathways

We have examined the clonal variation in rates of amino acid transport, protein synthesis, protein degradation, growth and proliferation for CHO cells with mutations in the purine and pyrimidine salvage pathways. First we compared three clonal cell lines, each with a different mutation, with the heterozygous parental line AT3-2. Overall, the correlation between rates of protein turnover, growth and proliferation was excellent. The slower growth and proliferation of one mutant, AB3 (TK-, APRT-), is explained by a low intrinsic rate of protein synthesis coupled with a smaller response in rates of amino acid transport, protein synthesis and protein degradation to insulin, serum and dexamethasone. Secondly, we compared seven aza-adenine-resistant and 14 thioguanine-resistant mutants of AT3-2 and found significant differences in control and insulin-stimulated rates of protein turnover both within and between mutant populations. A significant difference between the populations was unexpected because each individual cell line was cloned from a spontaneous pre-existing mutation in AT3-2, and each population should have the same average rate. Remarkably, all 24 mutants had lower rates of protein synthesis than AT3-2. We cannot explain the data solely in terms of mutations in the salvage pathways. Rather, we propose that the mutant survivors have randomly down-regulated the intrinsically fixed growth factor-regulated pathways of protein turnover, resulting in a broad spectrum of lower metabolic rates.

Ceramide down‐regulates System A amino acid transport and protein synthesis in rat skeletal muscle cells

2004 ◽  
Vol 19 (3) ◽  
pp. 1-24 ◽  
Author(s):  
Russell Hyde ◽  
Eric Hajduch ◽  
Darren J. Powell ◽  
Peter M. Taylor ◽  
Harinder S. Hundal
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Acid Transport ◽  
Rat Skeletal Muscle ◽  
System A

Stimulation of transport of alpha-aminoisobutyric acid into the testes of immature mice in vivo by follicle-stimulating hormone

1982 ◽  
Vol 100 (1) ◽  
pp. 137-142
Author(s):  
Nila Oza ◽  
Sarah J. Meanock ◽  
A. G. Davies
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Specific Activity ◽  
Follicle Stimulating Hormone ◽  
Acid Transport ◽  
Aminoisobutyric Acid ◽  
Old Mice ◽  
Stimulation Of

Abstract. Groups of immature mice were injected sc with radiocarbon-labelled alpha-aminoisobutyric acid (AIB) after being given a single sc injection of hFSH or of 0.9% saline. As an index of the transport of AIB, the specific activity of isotope was measured in homogenates of testis and of liver. FSH treatment caused statistically significant increases in the specific activity of isotope in the testes and in the ratio of testicular to liver specific activity. The effect was greatest in 9-day-old mice injected with FSH 16 h before removal of the testes. Uptake of labelled AIB was not stimulated after administration of hCG or testosterone. Doses of cycloheximide sufficient to reduce the rate of protein synthesis by over 99% did not impair testicular uptake of labelled AIB or the influence of FSH on AIB uptake. These results suggest that FSH stimulates amino acid transport into cells of the immature testis and that this action is independent of the stimulatory effect of FSH on testicular protein synthesis.

Interaction between growth hormone and rat muscle in vitro

1961 ◽  
Vol 200 (4) ◽  
pp. 675-678 ◽  
Author(s):  
J. L. Kostyo ◽  
J. E. Schmidt
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Growth Hormones ◽  
Hormone Concentration ◽  
Acid Transport ◽  
Rat Muscle ◽  
Resultant Effect ◽  
Initial Interaction

Hypophysectomized rat diaphragms, which were immersed briefly in dilute solutions of growth hormone and then washed thoroughly, subsequently transported α-aminoisobutyric acid-1-C14 at a greater rate than the controls. Growth hormones of bovine, porcine, simian and human origins were all effective. Increasing either the hormone concentration or the length of time that the diaphragms were immersed in growth hormone solutions increased the effect on amino acid transport. Prolonged washing of the diaphragms following exposure to growth hormone did not reduce the magnitude of the effect on amino acid transport. Moreover, reducing the temperature of the growth hormone solutions did not diminish the resultant effect on amino acid transport. From these results, it was concluded that the initial interaction between growth hormone and rat muscle in vitro occurs rapidly and the modification produced by this interaction is relatively stable.

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