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  • 1
    Online Resource
    Online Resource
    Personalized nutrition for the diverse needs of infants and children : 62nd Nestlé Nutrition Workshop, Pediatric Program, Helsinki, September 2007 ; from general issues to individual solutions (2008)
    Basel : Karger
    Details Availability
    Keywords: Child Nutritional Physiological Phenomena genetics ; Infant Nutritional Physiological Phenomena genetics ; Genetic Variation physiology ; Nutritional Requirements ; Congresses ; Gastroenterology ; Genetics ; Metabolism ; Nutrition ; Pediatrics
    Description / Table of Contents: Research has shown that humans respond differently to diets and, moreover, that they display varying predispositions to many diet-dependent metabolic and degenerative diseases. The focus of nutritional science is thus shifting from dietary guidelines for populations to individualized foods and diets. It is the aim of nutrigenomics to assign this human diversity in nutritional response to diet - as well as the subsequent consequences to human health - to specific genetic elements. At the same time, evidence suggests that diet itself is a critical determinant of human diversity. This publication focuses on the differences of humans as infants and children with respect to nutritional needs and responses to diet. For this purpose, four main points are discussed, namely 1) How do children differ in view of genetic diversity, environmental inputs, prior imprinting, and resident microflora; 2) What are the immediate and long-term consequences of these differences; 3) Can we accurately assess them; and 4) How can we act on these differences.Supplying answers to some crucial issues, as well as identifying directions for further research and practical applications by the food industry, this publication is an important source of information for all those involved in the subject of diet and individual responses
    Type of Medium: Online Resource
    Pages: XX + 262 S
    Edition: Online-Ausg. Online-Ressource Karger eBooks Collection 1997-2009
    ISBN: 9783805585545
    Series Statement: Nutrition workshop series : Pediatric program 62
    URL: http://dx.doi.org/10.1159/isbn.978-3-8055-8554-5
    URL: https://karger.com/books/book/2618
    DOI: 10.1159/isbn.978-3-8055-8554-5
    DDC: 618.92/39
    RVK:
    YQ 2205
    Language: English
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  • 2
    Electronic Resource
    Electronic Resource
    Whole body protein and amino acid metabolism: relation to protein quality evaluation in human nutrition (1981)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 29 (1981), S. 440-447 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00105a003
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  • 3
    Electronic Resource
    Electronic Resource
    Hepatic ultrastructure in leprechaunism (1982)
    Springer
    Virchows Archiv 397 (1982), S. 121-130 
    Details
    ISSN: 1432-2307
    Keywords: Leprechaunism ; Glycogen ; Liver ; Glucagon ; Hypoglycemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Leprechaunism is a congenital syndrome with characteristic habitus and facies, with fasting hypoglycemia and hyperinsulinism. In response to a glucose challenge there is prolonged severe hyperglycemia with an increased hyperinsulinemia. Our studies on such a patient showed a normal response of the serum glucose to glucagon stimulation in the fed state but no response in the postabsorptive state. Ultrastructural studies on the hepatocytes demonstrated that a lack of hepatic glycogen was not responsible for the biochemical features, since there was abundant normal β-glycogen in both the fed and fasting state, the granules being smaller in the fasted state. We speculate that carbohydrate intolerance in leprechaunism may be due to a relative insulin resistance of cell receptors in the fed state. Reactive hyperinsulinemia persisting into the postabsorptive phase appears to antagonize the usual glycogenolytic response to glucagon during fasting, resulting in hypoglycemia despite the presence of large hepatic glycogen stores.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00442383
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  • 4
    Electronic Resource
    Electronic Resource
    Measurement of muscle protein fractional synthetic rate by capillary gas chromatography/combustion isotope ratio mass spectrometry (1992)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 21 (1992), S. 486-490 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The measurement of skeletal muscle protein fractional synthetic rate using an infusion of (1-13C)leucine and measuring the isotopic abundance of the tracer in skeletal muscle protein by preparative gas chromatography (GC)/ninhydrin isotope ratio mass spectrometry (IRMS) is laborious and subject to errors owing to contamination by 12C. The purpose of this study was to compare muscle (13C)leucine enrichment measured with the conventional preparative GC/ninhydrin IRMS approach to a new, continuous-flow technique using capillary GC/combustion IRMS. Quadriceps muscles were removed from four Sprague-Dawley rats after each was infused at a different rate with (1-13C)leucine for 6-8 h. Muscle leucine enrichment (at.% excess) measured by both methods differed by less than 4%, except at low (13C)leucine enrichments (〈0.03 at.% excess). In addition, capillary GC/combustion IRMS was used to assess muscle (13C)leucine enrichment and fractional muscle protein synthesis rate in ten normal young men and women infused with (1,2-13C2)leucine for 12-14 h. This approach reduced the variability of the isotope abundance measure and gave estimates of muscle protein synthesis rate (0.050 ± 0.011% h-1 (mean ± SEM); range = 0.023-0.147% h-1) that agree with published values determined using the standard analytical approach. The measurement of (13C)leucine enrichment from skeletal muscle protein by capillary GC/combustion IRMS provides a simple, acceptable and practical alternative to preparative GC/ninhydrin IRMS.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200211004
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  • 5
    Electronic Resource
    Electronic Resource
    Glutamine and glutamate nitrogen exchangeable pools in cultured fibroblasts: A stable isotope study (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 134 (1988), S. 143-148 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Glutamine's role as an energetic fuel has been extensively studied in the past using 14C- and 3H-labeled tracers in cultured human cells. Yet another prominent role of glutamine, that of a nitrogen shuttle, cannot be approached without an N-tracer. We therefore used 15N-labeled glutamine and glutamate to address the following questions: (1) is it possible to study the exchangeable pools of intracellular free glutamine and glutamate nitrogen with stable isotope methods? and (2) to what extent is intracellular glutamine pool regulated by extracellular glutamine? We observed that: (1) intracellular [15N]-glutamine enrichment reached a plateau at 80% within 20 min of incubation in a buffer containing 0.7 mM pure 15N-glutamine and no glutamate; in contrast, intracellular 15N-glutamate enrichment rose only to 40% after 4 hours of incubation in a buffer containing 0.5 mM pure 15N-glutamate and no glutamine; (2) the cell-free glutamine content was tightly dependent on extracellular glutamine level, while the cell-free glutamate remained steady irrespective of the extracellular glutamate level; (3) the cells took up glutamine and glutamate against a concentration gradient; the rate of glutamine uptake accounted for 90% of the cell glutamine turnover rate; and (4) when cells were confronted with a glutamine-free medium, only one fourth of intracellular glutamine was derived from the exchangeable glutamate. We conclude that: (1) The size and turnover rate of the intracellular pool of free glutamine nitrogen are measurable using stable isotope methodology; (2) glutamine uptake from the extracellular medium accounts for most of glutamine turnover rate in cultured fibroblasts; and (3) intracellular free glutamate is divided up between several pools in cultured human fibroblasts.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041340118
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