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Ferrando, A. A.

Publications and source records attributed to Ferrando, A. A..

7 records
All sourcesNASA NTRSDOE OSTI
NASA NTRS2005

Amino acid supplementation alters bone metabolism during simulated weightlessness

High-protein and acidogenic diets induce hypercalciuria. Foods or supplements with excess sulfur-containing amino acids increase endogenous sulfuric acid production and therefore have the potential to increase calcium excretion and alter bone metabolism. In this study, effects of an amino acid/carbohydrate supplement on bone resorption were examined during bed rest. Thirteen subjects were divided at random into two groups: a control group (Con, n = 6) and an amino acid-supplemented group (AA, n = 7) who consumed an extra 49.5 g essential amino acids and 90 g carbohydrate per day for 28 days. Urine was collected for n-telopeptide (NTX), deoxypyridinoline (DPD), calcium, and pH determinations. Bone mineral content was determined and potential renal acid load was calculated. Bone-specific alkaline phosphatase was measured in serum samples collected on day 1 (immediately before bed rest) and on day 28. Potential renal acid load was higher in the AA group than in the Con group during bed rest (P < 0.05). For all subjects, during bed rest urinary NTX and DPD concentrations were greater than pre-bed rest levels (P < 0.05). Urinary NTX and DPD tended to be higher in the AA group (P = 0.073 and P = 0.056, respectively). During bed rest, urinary calcium was greater than baseline levels (P < 0.05) in the AA group but not the Con group. Total bone mineral content was lower after bed rest than before bed rest in the AA group but not the Con group (P < 0.05). During bed rest, urinary pH decreased (P < 0.05), and it was lower in the AA group than the Con group. These data suggest that bone resorption increased, without changes in bone formation, in the AA group.

Randomized Controlled Trial↗
NASA NTRS1999

Inactivity amplifies the catabolic response of skeletal muscle to cortisol

Severe injury or trauma is accompanied by both hypercortisolemia and prolonged inactivity or bed rest (BR). Trauma and BR alone each result in a loss of muscle nitrogen, albeit through different metabolic alterations. Although BR alone can result in a 2-3% loss of lean body mass, the effects of severe trauma can be 2- to 3-fold greater. We investigated the combined effects of hypercortisolemia and prolonged inactivity on muscle protein metabolism in healthy volunteers. Six males were studied before and after 14 days of strict BR using a model based on arteriovenous sampling and muscle biopsy. Fractional synthesis and breakdown rates of skeletal muscle protein were also directly calculated. Each assessment of protein metabolism was conducted during a 12-h infusion of hydrocortisone sodium succinate (120 microg/kg x h), resulting in blood cortisol concentrations that mimic severe injury (approximately 31 microg/dL). After 14 days of strict BR, hypercortisolemia increased phenylalanine efflux from muscle by 3-fold (P < 0.05). The augmented negative amino acid balance was the result of an increased muscle protein breakdown (P < 0.05) without a concomitant change in muscle protein synthesis. Muscle efflux of glutamine and alanine increased significantly after bed rest due to a significant increase in de novo synthesis (P < 0.05). Thus, inactivity sensitizes skeletal muscle to the catabolic effects of hypercortisolemia. Furthermore, these effects on healthy volunteers are analogous to those seen after severe injury.

Non-NASA Center↗
NASA NTRS1996

Prolonged bed rest decreases skeletal muscle and whole body protein synthesis

We sought to determine the extent to which the loss of lean body mass and nitrogen during inactivity was due to alterations in skeletal muscle protein metabolism. Six male subjects were studied during 7 days of diet stabilization and after 14 days of stimulated microgravity (-6 degrees bed rest). Nitrogen balance became more negative (P < 0.03) during the 2nd wk of bed rest. Leg and whole body lean mass decreased after bed rest (P < 0.05). Serum cortisol, insulin, insulin-like growth factor I, and testosterone values did not change. Arteriovenous model calculations based on the infusion of L-[ring-13C6]-phenylalanine in five subjects revealed a 50% decrease in muscle protein synthesis (PS; P < 0.03). Fractional PS by tracer incorporation into muscle protein also decreased by 46% (P < 0.05). The decrease in PS was related to a corresponding decrease in the sum of intracellular amino acid appearance from protein breakdown and inward transport. Whole body protein synthesis determined by [15N]alanine ingestion on six subjects also revealed a 14% decrease (P < 0.01). Neither model-derived nor whole body values for protein breakdown change significantly. These results indicate that the loss of body protein with inactivity is predominantly due to a decrease in muscle PS and that this decrease is reflected in both whole body and skeletal muscle measures.

Non-NASA Center↗
NASA NTRS1995

Oral branched-chain amino acids decrease whole-body proteolysis

BACKGROUND: This study reports the effects of ingesting branched-chain amino acids (leucine, valine, and isoleucine) on protein metabolism in four men. METHODS: To calculate leg protein synthesis and breakdown, we used a new model that utilized the infusion of L-[ring-13C6]phenylalanine and the sampling of the leg arterial-venous difference and muscle biopsies. In addition, protein-bound enrichments provided for the direct calculation of muscle fractional synthetic rate. Four control subjects ingested an equivalent amount of essential amino acids (threonine, methionine, and histidine) to discern the effects of branched-chain amino acid nitrogen vs the effects of essential amino acid nitrogen. Each drink also included 50 g of carbohydrate. RESULTS: Consumption of the branched-chain and the essential amino acid solutions produced significant threefold and fourfold elevations in their respective arterial concentrations. Protein synthesis and breakdown were unaffected by branched-chain amino acids, but they increased by 43% (p < .05) and 36% (p < .03), respectively, in the group consuming the essential amino acids. However, net leg balance of phenylalanine was unchanged by either drink. Direct measurement of protein synthesis by tracer incorporation into muscle protein (fractional synthetic rate) revealed no changes within or between drinks. Whole-body phenylalanine flux was significantly suppressed by each solution but to a greater extent by the branched-chain amino acids (15% and 20%, respectively) (p < .001). CONCLUSIONS: These results suggest that branched-chain amino acid ingestion suppresses whole-body proteolysis in tissues other than skeletal muscle in normal men.

NASA Discipline Number 18-10↗
NASA NTRS1993

The effect of boron supplementation on lean body mass, plasma testosterone levels, and strength in male bodybuilders

The effect of boron supplementation was investigated in 19 male bodybuilders ages 20-27 years. Ten were given a 2.5-mg boron supplement while 9 were given a placebo every day for 7 weeks. Plasma total and free testosterone, plasma boron, lean body mass, and strength measurements were determined on Days 1 and 49 of the study. Plasma boron values were significantly (p < 0.05) different as the experimental group increased from (+/- SD) 20.1 +/- 7.7 ppb pretest to 32.6 +/- 27.6 ppb posttest, while the control group mean decreased from 15.1 +/- 14.4 ppb pretest to 6.3 +/- 5.5 ppb posttest. Analysis of variance indicated no significant effect of boron supplementation on any of the dependent variables. Both groups demonstrated significant increases in total testosterone, lean body mass, 1-RM squat, and 1-RM bench press. The findings suggest that 7 weeks of bodybuilding can increase total testosterone, lean body mass, and strength in lesser trained bodybuilders, and that boron supplementation had no effect on these measures.

Controlled Clinical Trial↗
NASA NTRS1993

Microwave digestion preparation and ICP determination of boron in human plasma

A microwave digestion procedure, followed by Inductively Coupled Argon Plasma Spectroscopy, is described for the determination of boron (B) in human plasma. The National Institute of Standards and Technology (NIST) currently does not certify the concentration of B in any substance. The NIST citrus leaves 1572 (CL) Standard Reference Material (SRM) and wheat flour 1567a (WF) were chosen to determine the efficacy of digestion. CL and WF values compare favorably to those obtained from an open-vessel, wet digestion followed by ICP, and by neutron activation and mass spectrometric measurements. Plasma samples were oxidized by doubled-distilled ultrapure HNO3 in 120 mL PFA Teflon vessels. An MDS-81D microwave digestion procedure allows for rapid and relatively precise determination of B in human plasma, while limiting handling hazards and sources of contamination.

Ferrando, A. A.↗