Some Relations between Active Transport of Free Amino Acids into Cells and Their Incorporation into Protein

Riggs, Thomas R.; Walker, Lois M.

doi:10.1016/s0021-9258(18)67883-4

Cited by 59 publications

(1 citation statement)

References 22 publications

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“…Exchange of free leucine between cell and medium apparently cocurs by diffusion rather than by a specific energy-requiring mechanism . The rapidity of leucine interchange has also been noted for ascites cells (50), red blood cells, and several other tissues (8) . The rise and fall of label in the intracellular free leucine obtained in the liver slice system is sharper than that obtainable by the administration of the labeled compound in vivo (23) .…”

Section: Incorporation Into Liver Slicesmentioning

confidence: 86%

Electron Microscopic Radioautographic Detection of Sites of Protein Synthesis and Migration in Liver

Ashley

Peters

1969

The Journal of Cell Biology

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The sites of synthesis of proteins and their subsequent migration in rat liver have been studied during a 75 min period after labeling of liver-slice proteins by exposure to leucine-H3 for 2 min. Incorporation of the label into protein began after 1 min and was maximal by 4 min. Electron microscopic radioautography showed that synthesis of proteins in hepatocytes occurs mainly on ribosomes, particularly those in rough endoplasmic reticulum and, to some extent, in nuclei and mitochondria. Most of the newly formed proteins leave the endoplasmic reticulum in the course of 40 min, and concurrently labeled proteins appear in Golgi bodies, smooth membranes, microbodies, and lysosomes. A likely pathway for the secretion of some or all plasma proteins is from typical rough endoplasmic reticulum to a zone of reticulum which is partially coated with ribosomes, to the Golgi apparatus, and thence to the cell periphery. The formation of protein by reticuloendothelial cells was measured and found to be about 5% of the total protein formed by the liver.

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Section: Incorporation Into Liver Slicesmentioning

confidence: 86%

Electron Microscopic Radioautographic Detection of Sites of Protein Synthesis and Migration in Liver

Ashley

Peters

1969

The Journal of Cell Biology

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Transport and Hydrolysis of Peptides by Microorganisms

Payne

1977

Novartis Foundation Symposia

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Analysis of the vegetalizing action of tyrosine on the sea urchin embryo

Mastrangelo

1966

J. Exp. Zool.

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Vegetalization was produced in sea urchin embryos by treatment with D-and L-p-tyrosine, *tyrosine, and m-tyrosine, for 2 to 6 hours during cleavage. Glycine was without effect on development; phenylalanine produced general effects represented by reduction of both animal and vegetal structures. The vegetalizing action of tyrosine was synergistic with that of lithium or dinihophenol. However, unlike the latter compounds, tyrosine had no effect on respiratory rate of the embryos.The uptake and the incorporation of algal hydrolysate-C-14 and leucine-C-14, added to the sea water medium, were lower in sea urchin embryos in the presence of tyrosine or phenylalanine than in untreated control embryos. Inhibition of incorporation caused by phenylalanine was about twice that by tyrosine, and it was postulated that the different effects of these substances on development are related to the degree of inhibition. Neither glycine nor lithium inhibited amino acid uptake.When embryos were treated with tyrosine in the presence of a full complement of those free amino acids normally found in the egg, the vegetalizing effect of tyrosine was annulled. Since the sea urchin depends upon endogenous amino acids for protein synthesis during cleavage, it is suggested that in some way tyrosine limits the endogenous supply of amino acids available for synthesis of the proteins associated with animal structures by inhibiting their release from storage protein.

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Some Relations between Active Transport of Free Amino Acids into Cells and Their Incorporation into Protein

Cited by 59 publications

References 22 publications

Electron Microscopic Radioautographic Detection of Sites of Protein Synthesis and Migration in Liver

Electron Microscopic Radioautographic Detection of Sites of Protein Synthesis and Migration in Liver

Transport and Hydrolysis of Peptides by Microorganisms

Analysis of the vegetalizing action of tyrosine on the sea urchin embryo

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