scholarly journals Optimum Amino Acid Complement for Protein Synthesis by Rat Mammary Cells in Tissue Culture

1976 ◽  
Vol 59 (10) ◽  
pp. 1758-1763 ◽  
Author(s):  
C.S. Park ◽  
P.T. Chandler ◽  
R.M. Clark
1952 ◽  
Vol 196 (1) ◽  
pp. 51-68 ◽  
Author(s):  
H.W. Gerarde ◽  
Marion. Jones ◽  
Theodore. Winnick

1958 ◽  
Vol 149 (936) ◽  
pp. 392-400 ◽  

The mammary gland in full lactation had for long been recognized as an ideal system for the study of the biosynthesis of protein. The discoveries during the last 5 years of the incorporation of labelled amino acids into the microsomes of cell homogenates and of other reactions of amino acids which might be on the pathway to protein synthesis, encouraged us to study the fate of amino acids in various systems prepared from mammary cells. De novo protein synthesis had not yet been proved in any system which contained no intact cells. So far no net increase in any defined protein fraction during incubations has been found or indeed looked for in our experiments. Naturally one hopes that such studies of the fate of labelled amino acids in cell-free preparations will reveal the detail of enzymic reactions which will prove to be part of the mechanisms of protein biosynthesis. Three types of reactions of amino acids in cell-free preparations from homogenates of many tissues have been studied most extensively. (1) The acyl activation of amino acids to form amino acid-acid adenylates in the presence of ATP and ‘activating enzymes’. (2) The formation of compounds of cell sap-ribonucleic acid ( SRN A ) with amino acids in the presence of ATP and ‘activating enzymes’. (3) The incorporation of amino acids into intracellular particles either from free amino acid or by transfer from amino-acid- SRN A compounds in the presence of ATP , guanosine triphosphate ( GTP ) and ‘activating enzymes’. In this paper we are giving a survey of the results of studies on these three types of reactions in systems prepared from mammary tissue and we are relating these to results obtained with other systems elsewhere. Some comparative studies of the incorporation of labelled amino acids into protein fractions of intact mammary cells (minced tissue) are also presented. All the original results given here were obtained from experiments with guinea-pig mammary gland preparations from animals 2 to 6 days after parturition. Experimental detail will be reported elsewhere.


Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.


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