Dietary protein-induced changes in excretory function: a general animal design feature

Author(s):  
Michael A. Singer
2017 ◽  
Vol 32 (5) ◽  
pp. 1587-1595 ◽  
Author(s):  
Hongwei Wang ◽  
Bianhua Zhou ◽  
Ruiyan Niu ◽  
Jinming Wang ◽  
Jianhai Zhang ◽  
...  

1993 ◽  
Vol 3 (11) ◽  
pp. 1723-1737 ◽  
Author(s):  
A J King ◽  
A S Levey

Protein intake has been recognized as a modulator of renal function for over half a century. This review analyzes the renal response induced by changes in habitual protein intake and with acute amino acid infusion or a meat meal in humans and animals. The pattern and magnitude of changes in GFR and creatinine clearance are examined along with a discussion of the effect of the variability of these measurements among individuals and populations on the interpretation of clinical studies. Potential mechanisms of protein-induced changes in GFR and creatinine clearance are examined, including changes in the hormonal milieu, glomerular hemodynamics, and other intrarenal processes. Habitual dietary protein consumption varies significantly with respect to age, gender, and lean body mass--factors that are well known to influence GFR. This correlation raises the possibility that (1) variation in dietary protein intake may account, at least in part, for the differences in renal function among individuals; and (2) the level of protein intake should be assessed in defining the normal range of renal function.


1998 ◽  
Vol 275 (5) ◽  
pp. E814-E820 ◽  
Author(s):  
Fumiaki Yoshizawa ◽  
Scot R. Kimball ◽  
Thomas C. Vary ◽  
Leonard S. Jefferson

The effect of dietary protein on the initiation of mRNA translation was examined in rats starved for 18 h and then fed isocaloric diets containing either 20% protein (20P) or no added protein (0P). Feeding the 20P diet, but not the 0P diet, stimulated protein synthesis in skeletal muscle and liver by 38 and 41%, respectively. The stimulation was associated with reduced binding of eukaryotic initiation factor (eIF) 4E to the translational repressor 4E-BP1, increased formation of the active eIF4E-eIF4G complex, and increased phosphorylation of 4E-BP1. In contrast, feeding a 0P diet had no effect on any of these parameters. Feeding a 20P diet resulted in partial dephosphorylation of eIF4E in both tissues. In liver, refeeding a 0P diet also resulted in partial eIF4E dephosphorylation, suggesting that the phosphorylation state of eIF4E is not important in the stimulation of protein synthesis under these conditions. Finally, plasma insulin concentrations were the same in rats fed either diet (14.8 ± 4.9 vs. 15.5 ± 4.5 μU/ml for 20P and 0P groups, respectively), suggesting that feeding-induced changes in plasma insulin are not sufficient to stimulate protein synthesis. Instead, a combination of dietary protein and insulin may be required to stimulate translation initiation.


1999 ◽  
Vol 276 (5) ◽  
pp. G1302-G1309 ◽  
Author(s):  
Karen A. Lacourse ◽  
Lisa J. Swanberg ◽  
Patrick J. Gillespie ◽  
Jens F. Rehfeld ◽  
Thomas L. Saunders ◽  
...  

A CCK-deficient mouse mutant generated by gene targeting in embryonic stem cells was analyzed to determine the importance of CCK for growth and function of the exocrine pancreas and for pancreatic adaptation to dietary changes. RIAs confirmed the absence of CCK in mutant mice and demonstrated that tissue concentrations of the related peptide gastrin were normal. CCK-deficient mice are viable and fertile and exhibit normal body weight. Pancreas weight and cellular morphology appeared normal, although pancreatic amylase content was elevated in CCK-deficient mice. We found that a high-protein diet increased pancreatic weight, protein, DNA, and chymotrypsinogen content similarly in CCK-deficient and wild-type mice. This result demonstrates that CCK is not required for protein-induced pancreatic hypertrophy and increased proteolytic enzyme content. This is a novel finding, since CCK has been considered the primary mediator of dietary protein-induced changes in the pancreas. Altered somatostatin concentrations in brain and duodenum of CCK-deficient mice suggest that other regulatory pathways are modified to compensate for the CCK deficiency.


1985 ◽  
Vol 49 (9) ◽  
pp. 2671-2683 ◽  
Author(s):  
Ryuzo SASAKI ◽  
Hideki OHNOTA ◽  
Shin-ichi YANAGAWA ◽  
Hideo CHIBA

1987 ◽  
Vol 58 (1) ◽  
pp. 73-85 ◽  
Author(s):  
Penny A. Coyer ◽  
J. P. W. Rivers ◽  
D. J. Millward

1. The effect of dietary protein and energy restriction on heat production and growth costs has been examined in rats fed on a marginal (MP) or high (HP) protein diet, containing 9.2 % or 22 % respectively of the gross energy content as casein. Diets were given either ad fib. or at approximately 25, 50 or 75 % of the ad lib. intake.2. Heat production (kJ/kg body-weight (W)0.75 per d) was increased by 23% in rats fed on the MP diet ad Lib., as compared with their HP controls (P < 0.01).3. Factorial analysis of the data showed that the overall cost of energy deposition (kJ/kJ; Ee) was elevated on the MP diet (MP 1.7, HP 1.28; P < 0.001). Maintenance requirements (kJ/kg W0.75 per d) for zero energy balance were unchanged (MP 562, HP 573).The partial energy cost of protein deposition (Ep) varied with dietary manipulation. If the partial energy cost of fat deposition (Ef) was assumed constant at 1.25 kJ/kJ, and maintenance requirements were assumed to vary with metabolic body size (W0.75), Ep was elevated on the MP diet. On both diets, Ep was reduced at low energy intakes.5. The significance of these results is discussed in the context of current approaches to the analysis and interpretation of findings describing dietary induced changes in the rate of heat production.


1998 ◽  
Vol 85 (5) ◽  
pp. 1744-1752 ◽  
Author(s):  
J. L. Bowtell ◽  
G. P. Leese ◽  
K. Smith ◽  
P. W. Watt ◽  
A. Nevill ◽  
...  

The aim of this study was to investigate dietary protein-induced changes in whole body leucine turnover and oxidation and in skeletal muscle branched chain 2-oxo acid dehydrogenase (BCOADH) activity, at rest and during exercise. Postabsorptive subjects received a primed constant infusion ofl-[1-13C,15N]leucine for 6 h, after previous consumption of a high- (HP; 1.8 g ⋅ kg−1 ⋅ day−1, n = 8) or a low-protein diet (LP; 0.7 g ⋅ kg−1 ⋅ day−1, n = 8) for 7 days. The subjects were studied at rest for 2 h, during 2-h exercise at 60% maximum oxygen consumption, then again for 2 h at rest. Exercise induced a doubling of both leucine oxidation from 20 μmol ⋅ kg−1 ⋅ h−1and BCOADH percent activation from 7% in all subjects. Leucine oxidation was greater before (+46%) and during (+40%, P < 0.05) the first hour of exercise in subjects consuming the HP rather than the LP diet, but there was no additional change in muscle BCOADH activity. The results suggest that leucine oxidation was increased by previous ingestion of an HP diet, attributable to an increase in leucine availability rather than to a stimulation of the skeletal muscle BCOADH activity.


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