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J C Waterlow

Publications and source records attributed to J C Waterlow.

At least 109 records · Page 6Linked to original sources
PubMed1977

The relationship between dietary intake, weight change, nitrogen balance, and protein turnover in man.

We have examined the relationships between protein turnover, protein synthesis, and protein breakdown and dietary intake, weight change, and nitrogen balance in children who were recovering and had recovered from severe protein-energy-malnutrition. Protein metabolism was measured by giving [15N]glycine and measuring the enrichment of urinary urea. The level of dietary protein did not affect protein metabolism. There were highly significant correlations between both protein flux and protein synthesis and the ad libitum dietary intake, nitrogen balance, and weight change. Over the range of dietary intake, 60 to 270 cal/kg per day, the protein synthesis rate increased 5-fold. Large changes in dietary intake resulted in small changes in protein breakdown, with breakdown being least on an inadequate intake. Changes in the rate of protein breakdown did not contribute to changes in nitrogen balance or body weight.

Body Weight↗
PubMed1977

The in vivo measurement of protein synthesis.

Methods of measuring in vivo protein synthesis are briefly reviewed. Methods involving incorporation of label into protein are more appropriate for mixed proteins. The major difficulty is the definition of the precursor pool for protein synthesis. The only data available on the effect of infection on protein synthesis are open to criticism on the grounds that the precursor pool was not sampled.

Amino Acids↗
PubMed1977

The presentation and use of height and weight data for comparing the nutritional status of groups of children under the age of 10 years.

This paper presents recommendations for the analysis and presentation of height and weight data from surveillance or surveys involving nutrition and anthropometry in young children up to the age of 10 years. These recommendations are only for the analysis of data collected on a cross-sectional basis. The basic indices recommended are height for age and weight for height, each considered either in terms of centiles or in a cross-classification scheme using standard deviation scores. It is hoped that these methods of analysis and presentation will prove widely acceptable, so that international comparisons will be made easier.

Anthropometry↗
PubMed1976

Measurement of protein turnover in rat liver. Analysis of the complex curve for decay of label in a mixture of proteins.

The curve for decay of 14C in rat liver protein labelled by injection of NaH14CO3 was analysed to obtain the average turnover rate of mixed liver protein. Three different methods of analysis were used. (1) Unlike decay curves from homogeneous proteins, the curve did not fit a single exponential, but a good fit was obtained with three exponentials. By assuming that the mixture contained three major components with different turnover rates, the calculated value for the average turnover rate (k) was close to 40% per day. (2) k was also calculated from the area under the decay curve, a method which makes no assumptions about the number of proteins in the mixture. This method also gave a value close to 40% per day. (3) It was shown empirically, both by simulation of decay of label in model mixtures of protein and with the decay curve measured in vivo, that k can be calculated from the time taken for the specific radioactivity to fall to 10% of its maximum value. This is an advantage, since the other two methods require the decay curve to be measured over a much longer period of time.

Animals↗
PubMed1976

The relative importance of muscle protein synthesis and breakdown in the regulation of muscle mass.

The effects of growth-suppressing and muscle-wasting treatments on muscle protein turnover and amino acid concentrations were determined in vivo. All treatments depressed protein synthesis and some treatments depressed protein breakdown. Only prolonged starvation increased protein breakdown. Muscle protein mass is regulated primarily through alterations in protein synthesis in all except emergency conditions. The increased concentrations of the branched-chain amino acids indicate that they are unlikely to be involved in this regulation.

Animals↗
PubMed1976

Studies of amino acid and protein metabolism in normal man with L-[U-14C]tyrosine.

1. Six men were infused intravenously for 10 h with a tracer amount of L-[U-14C]tyrosine while on a standardized food intake. 2. Measurements of plasma L-[14C]-tyrosine specific radioactivity and the excretion rate of 14CO2 were made at frequent intervals and showed plateau labelling of plasma and expired carbon dioxide within 6-8 h. The tyrosine flux was calculated from the specific radioactivity in plasma at plateau value. 3. The excretion rate of 14CO2, corrected for retention of label within the bicarbonate pool, showed that oxidation accounted for 20% of the tyrosine flux. Urinary excretion of label was negligible. 4. Rates of protein synthesis were calculated from the flux of tyrosine after subtracting the proportion oxidized. Although the mean rate of synthesis was consistent with other measurements of protein turnover, the individual values ranged from 284 to 387 g/day. The variation was not reduced by relating turnover to body weight, lean body mass or energy expenditure. 5. Estimating the rates of protein breakdown from the tyrosine flux involved some assumptions about pathways of phenylalanine metabolism. The use of a labelled essential amino acid would therefore give more accurate values for short-term measurements of whole body protein turnover.

Adult↗
PubMed1976

Energy balance during recovery from malnutrition.

This report presents an account of energy balance of young Jamaican children recovering from protein-energy malnutrition (PEM). This was done in three steps. Initially the true gross energy of a formula used in the treatment of PEM was determined by bomb calorimetry. Then its metabolizable energy content was determined in a group of nine children recovering from PEM. In a similar but different group of eight children total daily metabolizable energy intake (EI), average rate of weight gain (g/kg/day) (WG), and total daily energy expenditure (TDEE) were determined. TDEE was determined by indirect calorimetry using a heart rate counter and is based on the relationship of heart rate to oxygen consumption. In this group, the mean EI was 122.5 kcal, WG was 8.4 g, and TDEE was 92 kcal. The difference between EI and TDEE was 30.7 kcal/kg, or 3.3 kcal/g of weight gain. This difference is presumed to be the stored energy in new tissue and corresponds to a proposed new tissue composition of 31% fat and 14% protein. A regression curve comparison of WG versus EI showed that at zero weight gain EI was 85.5 kcal and each additional gain. The difference of 1.0 kcal between total energy cost and stored energy reflects the energy required to deposit new tissue. Gram weight gain required 4.4 kcal. The latter figure is felt to reflect the total energy cost of weight. From three independent measurements, an estimate of maintenance energy requirements was estimated to be about 82 kcal/kg/day.

Calorimetry↗
PubMed1975

The effect of protein deprivation and starvation on the rate of protein synthesis in tissues of the rat.

1. The fractional rate of protein synthesis was measured in tissues of rats in vivo by continuous infusion of [14C]tyrosine. In growing animals proteins of liver and kidney were renewed at a rate greater than 50% per day, those in skeletal muscle, brain and heart at a rate between 13 and 23% per day. 2. Protein synthesis was also measured in liver, kidney, heart, brain and skeletal muscle of rats either given a protein-free diet for 21 days or starved for 2 days. During the first 2 days no clear differences between the effects of these two regimes could be detected. 3. Gastrocnemius muscle did not lose tissue protein till after 9 days without protein in the diet. The rate of protein synthesis was halved after 1 day and halved again after 21 days without protein. It was deduced that the rate of protein breakdown in muscle had declined also. 4. In liver the loss of protein was immediate without any apparent change in the fractional rate of protein synthesis. Between 2 and 21 days of dietary protein deprivation the liver lost protein slowly but the fractional rate of protein synthesis was increased. It is proposed that lack of protein in the diet also causes an increase in the rate of liver protein breakdown.

Animals↗
PubMed1975

The protein gap.

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Age Factors↗
PubMed1975

Skeletal-muscle growth and protein turnover.

Because of turnover, protein synthesis and breakdown can each be involved in the regulation of the growth of tissue protein. To investigate the regulation of skeletal-muscle-protein growth we measured rates of protein synthesis and breakdown in growing rats during development on a good diet, during development on a marginally low-protein diet and during rehabilitation on a good diet after a period of severe protein deficiency. Rates of protein synthesis were measured in vivo with a constant intravenous infusion of [14C]tyrosine. The growth rate of muscle protein was measured and the rate of breakdown calculated as breakdown rate=synthesis rate-growth rate. These measurements showed that during development on a good diet there was a fall with age in the rate of protein synthesis resulting from a fall in capacity (RNA concentration) and activity (synthesis rate per unit of RNA). There was a fall with age in the breakdown rate so that the rate was highest in the weaning rats, with a half-life of 3 days. There was a direct correlation between the fractional growth and breakdown rates. During rehabilitation on the good diet, rapid growth was also accompanied by high rates of protein breakdown. During growth on the inadequate diet protein synthesis rates were lesss than in controls, but growth occurred because of decreased rates of protein breakdown. This compression was not complete, however, since ultimate muscle size was only one-half that of controls. It is suggested that increased rates of protein breakdown are a necessary accompaniment to muscle growth and may result from the way in which myofibrils proliferate.

Aging↗