scholarly journals An attenuated rate of leg muscle protein depletion and leg free amino acid efflux over time is seen in ICU long-stayers

Critical Care ◽  
2018 ◽  
Vol 22 (1) ◽  
Author(s):  
Lena Gamrin-Gripenberg ◽  
Martin Sundström-Rehal ◽  
Daniel Olsson ◽  
Jonathan Grip ◽  
Jan Wernerman ◽  
...  
2003 ◽  
Vol 35 (5) ◽  
pp. 784-792 ◽  
Author(s):  
HANNU T. PITK??NEN ◽  
TARJA NYK??NEN ◽  
JUHA KNUUTINEN ◽  
KAISA LAHTI ◽  
OLAVI KEIN??NEN ◽  
...  

1977 ◽  
Vol 1 (3) ◽  
pp. 147-151 ◽  
Author(s):  
Kaminski MV ◽  
N. Dunn ◽  
Wannemacher RW ◽  
R. Dinterman ◽  
R DeShazo ◽  
...  

2011 ◽  
Vol 110 (2) ◽  
pp. 480-491 ◽  
Author(s):  
Gordon I. Smith ◽  
Bruce W. Patterson ◽  
Bettina Mittendorfer

We undertook a comprehensive review of the literature to unravel the nature of the variability in the reported rate of human muscle protein synthesis. We analyzed the results from studies that report the protein fractional synthesis rate (FSR) in the vastus lateralis in healthy, nonobese, untrained adults ≤50 yr of age in the postabsorptive state at rest by using the primed, constant tracer amino acid infusion method according to experimental design characteristics. We hypothesized that if the variability is methodological (rather than physiological) in nature, systematic clustering of FSR values would be evident, and outliers would become apparent. Overall, as expected, the mixed muscle protein FSR values were significantly ( P < 0.001) greater when the muscle vs. the plasma free amino acid enrichment is used as the surrogate precursor pool enrichment, and the average mixed muscle protein FSR values were significantly greater ( P = 0.05) than the myofibrillar/myosin heavy chain FSR values. The within-study variability (i.e., population variance) was somewhat smaller in studies that used plasma amino acid/ketoacid enrichments vs. muscle free amino acid enrichment (∼24 vs. ∼31%), but this was not apparent in all circumstances. Furthermore, the between-study consistency of measured FSR values (i.e., interquartile range) was inversely correlated with the average duration between biopsies. Aside from that, the variation in reported FSR values could not be explained by differences in the experimental design and analytical methods, and none of the most commonly used approaches stood out as clearly superior in terms of consistency of results and/or within-study variability. We conclude that the variability in reported values is in part due to 1) differences in experimental design (e.g., choice of precursor pool) and 2) considerable within-subject variability. The summary of the results from our analysis can be used as guidelines for “normal” average basal FSR values at rest in healthy adults.


1977 ◽  
Vol 1 (3) ◽  
pp. 147-151 ◽  
Author(s):  
M.V. Kaminski ◽  
N.P. Dunn ◽  
R.W. Wannemacher ◽  
R.E. Dinterman ◽  
R. DeShazo ◽  
...  

1973 ◽  
Vol 59 (2) ◽  
pp. 435-446
Author(s):  
SIDNEY K. PIERCE ◽  
MICHAEL J. GREENBERG

1. Molluscan cells maintain constant volume in decreasing salinities by releasing intracellular free amino acids as osmotic solute. 2. During a salinity decrease both osmotic pressure and ion concentrations decline simultaneously. Either condition might initiate the amino acid release. 3. Under constant osmotic conditions a decrease in Na+, K+ or Cl- concentration in the medium surrounding the isolated bivalve heart, did not result in an amino acid efflux. 4. On the other hand, removal of Ca2+ and Mg2+ resulted in a vigorous amino acid efflux which continued until the divalent ion concentration was restored. 5. The hypo-osmotically induced amino acid efflux could be partially blocked by raising the external divalent ion concentration. Similarly, lanthanum proved to be an effective blocking agent, both in low osmotic pressures and in Ca2+- and Mg2+-free SW. 6. These results show that salinity-induced free amino acid regulation is initiated by a decrease in external osmotic pressure. The time course of the efflux is dependent on external divalent ion concentration. 7. Finally, the site of divalent ion action is at the external membrane surface. 8. A hypothetical membrane model is proposed.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
EJ Cho ◽  
XL Piao ◽  
MH Jang ◽  
SY Park ◽  
SW Kwon ◽  
...  

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
BM Silva ◽  
AP Oliveira ◽  
DM Pereira ◽  
C Sousa ◽  
RM Seabra ◽  
...  

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