Correlation between osmoregulation and cell volume regulation

1987 ◽  
Vol 252 (4) ◽  
pp. R768-R773
Author(s):  
M. A. Lang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Free Amino Acids ◽  
Volume Regulation ◽  
Free Amino ◽  
Cell Volume Regulation

The euryhaline crab, Callinectes sapidus, behaves both as an osmoregulator when equilibrated in salines in the range of 800 mosM and below and an osmoconformer when equilibrated in salines above 800 mosM. There exists a close correlation between osmoregulation seen in the whole animal in vivo and cell volume regulation studied in vitro. Hyperregulation of the hemolymph osmotic pressure and cell volume regulation both occurred in salines at approximately 800 mosM and below. During long-term equilibration of the crabs to a wide range of saline environments, the total concentration of hemolymph amino acids plus taurine remained below 3 mM. During the first 6 h after an acute osmotic stress to the whole animal, the hemolymph osmotic pressure and Na activity gradually decreased, whereas the free amino acids remained below 3 mM. As the hemolymph osmotic pressure decreased below approximately 850 mosM, the amino acid level began to increase to 17-25 mM. This change was primarily due to increases in glycine, proline, taurine, and alanine. The likely source of the increase in hemolymph free amino acids in vivo is the free amino acid loss from muscle cells observed during cell volume regulation in vitro.

The costs of cell volume regulation: protein metabolism during hyperosmotic adjustment

1992 ◽  
Vol 72 (3) ◽  
pp. 569-578 ◽  
Author(s):  
A. J. S. Hawkins ◽  
T. J. Hilbish
Keyword(s):  
Amino Acids ◽  
Cell Volume ◽  
Protein Metabolism ◽  
Free Amino Acids ◽  
Volume Regulation ◽  
Free Amino ◽  
Cell Volume Regulation ◽  
Amino Nitrogen ◽  
Body Protein ◽  
Metabolic Pool

To resolve the sources of amino nitrogen which is accumulated as intracellular solute during hyperosmotic volume regulation, components of protein metabolism were monitored during compensation for a change from 15 to 30% salinity in the blue mussel, Mytilus edulis L. Net solute gain stemmed primarily from a marked reduction in total output from the metabolic pool of free amino acids, most of this ‘saving’ resulting from slower whole-body protein synthesis, and the remainder from lower nitrogenous excretion. Indeed, total inputs to the metabolic pool of free amino acids actually decreased over the period of net solute gain at 30%. Associated contributions from dietary assimilation, de novo synthesis and the direct uptake of dissolved amino acids were each negligible, indicating that breakdown products from endogenous body protein were the only significant source of amino nitrogen accumulated during hyperosmotic regulation. This accumulation represented more than 3% of soft-tissue protein nitrogen within the whole animal. We therefore impress that the excretion, during hyposaline adjustment, of all nitrogen previously accumulated as solute in response to equivalent hypersaline change, represents a major component cost of cell volume regulation, and which helps to explain stress and even mortality consequent upon what may be small but frequent fluctuations of salinity.

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

Effect of hemorrhagic shock on hepatic transmembrane potentials and intracellular electrolytes, in vivo

1981 ◽  
Vol 240 (3) ◽  
pp. R211-R219 ◽  
Author(s):  
M. M. Sayeed ◽  
R. J. Adler ◽  
I. H. Chaudry ◽  
A. E. Baue
Keyword(s):  
Hemorrhagic Shock ◽  
Cell Volume ◽  
Volume Regulation ◽  
Cell Volume Regulation ◽  
Shed Blood ◽  
Average Value ◽  
Transmembrane Potentials ◽  
Relative Membrane Permeability

In this study we investigated in vivo changes in hepatic cellular electrolytes and resting transmembrane potentials (Em) during hemorrhagic shock. Hepatic Na-K transport and cell volume regulation were assessed in vitro. Rats were bled and the ensuing hypotension (40 mmHg) was maintained by returning 25-30% (intermediate-shock, IS) or 55-60% (late-shock, LS) of the shed blood. We resuscitated IS rats by reinfusion of all of the remaining shed blood and Ringer's lactate solution. Hepatic cellular Na and Cl increased and K decreased progressively with shock. Resuscitation of IS rats restored cell K and Cl but not Na to preshock levels. Em decreased from the control average value of -40 (mV) to -31 in IS and -19 in LS. Em was partially restored (-36 mV) after resuscitation. We evaluated changes in relative membrane permeability to Na and K (PNa/PK) with shock by assuming Em either to be a Na-K exchange diffusion potential or due to an unequally coupled movement of Na and K. These evaluations show a lack of effect of shock (IS, with or without resuscitation) on PNa/PK. Our observations are compatible with failure of an electrogenic Na pump in shock. This may be related to loss of hepatic cell volume regulation in shock.

Hemorrhagic shock impairs myocardial cell volume regulation and membrane integrity in dogs

1987 ◽  
Vol 252 (6) ◽  
pp. H1203-H1210
Author(s):  
J. W. Horton
Keyword(s):  
Hemorrhagic Shock ◽  
Cell Volume ◽  
Volume Regulation ◽  
Membrane Integrity ◽  
Cell Volume Regulation ◽  
Calcium Entry ◽  
Tissue Water ◽  
Total Tissue

An in vitro myocardial slice technique was used to quantitate alterations in cell volume regulation and membrane integrity after 2 h of hemorrhagic shock. After in vitro incubation in Krebs-Ringer-phosphate medium containing trace [14C]inulin, values (ml H2O/g dry wt) for control nonshocked myocardial slices were 4.03 +/- 0.11 (SE) for total water, 2.16 +/- 0.07 for inulin impermeable space, and 1.76 +/- 0.15 for inulin diffusible space. Shocked myocardial slices showed impaired response to cold incubation (0 degrees C, 60 min). After 2 h of in vivo shock, total tissue water, inulin diffusible space, and inulin impermeable space increased significantly (+19.2 +/- 2.4, +8.1 +/- 1.9, +34.4 +/- 6.1%, respectively) for subendocardium, whereas changes in subepicardium parameters were minimal. Shock-induced cellular swelling was accompanied by an increased total tissue sodium, but no change in tissue potassium. Calcium entry blockade in vivo (lidoflazine, 20 micrograms X kg-1 X min-1 during the last 60 min of shock) significantly reduced subendocardial total tissue water as compared with shock-untreated dogs. In addition, calcium entry blockade reduced shock-induced increases in inulin impermeable space and inulin diffusible space. In vitro myocardial slice studies confirm alterations in subendocardial membrane integrity after 2 h of in vivo hemorrhagic shock. Shock-induced abnormalities in myocardial cell volume regulation are reduced by calcium entry blockade in vivo.

scholarly journals Free amino acids of testes. Concentrations of free amino acids in the testes of several species and the precursors of glutamate and glutamine in rat testes in vivo

1973 ◽  
Vol 132 (3) ◽  
pp. 353-359 ◽  
Author(s):  
Isa K. Mushahwar ◽  
Roger E. Koeppe
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Free Amino Acids ◽  
Free Amino ◽  
Ammonium Acetate ◽  
Testicular Tissue ◽  
Species Variation

Determination of the free amino acid and lactate content of testicular tissue in rat, guinea pig, rabbit, cat, gerbil, hamster, chicken and bullfrog indicates a substantial species variation. Insulin hypoglycaemia and ammonium acetate toxicity changes the concentration of several free amino acids of rat testes. 14C radioactivity from labelled acetate and ethanol is rapidly incorporated into some of the free amino acids of rat testes in vivo, whereas incorporation from [14C]glucose is relatively slow. These results have been compared with those obtained from similar studies with rat brain. In contrast to brain, there is no evidence for glutamate compartmentation in testes.

scholarly journals Regulation of carbohydrate metabolism in lymphoid tissue. Nature of the endogenous substrates and their contribution to the respiratory fuel of the sliced rat spleen in vitro

1976 ◽  
Vol 156 (1) ◽  
pp. 119-127 ◽  
Author(s):  
D Suter ◽  
M J Weidemann
Keyword(s):  
Amino Acids ◽  
Fatty Acid ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Adenine Nucleotide ◽  
Tricarboxylic Acid Cycle ◽  
Total Ammonia

1. Tissue glycogen contributes, maximally, only 10% of the respiratory fuel of the rat spleen slice in the absence of an added carbon source, and makes no significant contribution when glucose (3mM) is added. 2. The reserves of fatty acid in the form of triglyceride (35.5mumol of fatty acid/g dry wt. of tissue) fall by approx. 25% after incubation of spleen slices with or without added glucose for 2h, and, on this basis, account for 32% of the oxidative fuel. 3. In contrast, the total oxidative contribution of fatty acid reserves to the respiratory fuel, determined on the basis of inhibiton of respiration by 2-bromostearate, is 42-52%. This range includes tissue from both starved and well-fed animals and is not significantly altered by the presence of added glycose (3mM). 4. Large quantities of NH3 (31-35mumol//h per g dry wt. of tissue) are produced by spleen slices incubated in the absence of added substrates, and this value is suppressed by approx. 50% on incubation with glucose (3mM). Adenine nucleotide breakdown can account for only 17% of the total ammonia produced. 5. Individual free amino acid concentrations in spleen were determined, both in vivo and in slices before and after 60 min of incubation. Although the total free amino acid pool size increases by 45% during incubation, owing to protein breakdown, the tissue concentrations of aspartate, glutamate, glutamine and alanine do not increase. It is suggested that these amino acids areoxidized in a net sense to CO2 and water with the liberation of free NH3 via transamination reactions, glutaminase, the purine nucleotide cycle and the tricarboxylic acid cycle. 6. It is concluded that the normal endogenous metabolism of sliced rat spleen (43-52% due to lipids, 30% due to amino acids and 10% due to glycogen) is modified by added glycose only to the extent that glycogen oxidation and 50% of the contribtion made by ino acids are suppressed; endogenous lipid metabolism is unaffected.

Effects in vivo and in vitro of l-glutamic acid-γ-hydrazide on metabolism of some free amino acids in brain and liver

1966 ◽  
Vol 15 (11) ◽  
pp. 1831-1845 ◽  
Author(s):  
Ricardo Tapia ◽  
Herminia Pasantes ◽  
Berta G. Ortega ◽  
Guillermo H. Massieu
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Free Amino Acids ◽  
Free Amino
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