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Biomedical subjects

E Horton

Publications and source records attributed to E Horton.

11 recordsLinked to original sources

Physical activity, nutrition, and chronic disease.

Epidemiologic, animal, clinical, and metabolic studies demonstrate the independent roles of physical activity and nutrition in the prevention and treatment of several chronic diseases. Fewer data are available to describe the synergistic effects of exercise and diet, and questions remain as to whether and how these two lifestyle factors work together to promote health and prevent disease. This paper briefly reviews many of the known effects of physical activity and nutrition on the prevention and treatment of coronary heart disease, non-insulin-dependent diabetes mellitus, obesity, and osteoporosis as well as how exercise and diet may work together. A discussion of how to increase physical activity levels and how to improve dietary intake also is included. Finally, current exercise and dietary recommendations are summarized, as are directions for future research.

Animals↗

alpha-Ketoisocaproate is superior to leucine in sparing glucose utilization in humans.

The present study was designed to examine the glucose-sparing effect of leucine and its keto acid alpha-ketoisocaproate (KIC) in vivo. Two groups of overnight-fasted normal volunteers were studied. In the first group, eight subjects received an intravenous infusion of leucine and six subjects received KIC (2.3 mumol X kg-1 X min-1) for 3 h; on another occasion, all subjects received saline and acted as their own controls. In the second group, 11 subjects received an infusion of 1 mU X kg-1 X min-1 for 3 h with a variable glucose infusion to maintain euglycemia. On another occasion, five subjects received an additional infusion of leucine and six subjects received KIC each at 2.3 mumol X kg-1 X min-1 for 3 h. The amount of exogenous glucose required to maintain euglycemia (M, mg X kg-1 X min-1) was used as an index of total body glucose utilization. Forearm exchange of leucine, KIC, glucose, and lactate was determined in both groups. Both leucine and KIC infusions alone decreased glucose uptake (42 and 40%) and increased lactate release (37 and 116%, respectively). Hyperinsulinemia (6-fold basal) and euglycemia resulted in a fivefold increase in glucose uptake across the human forearm. The amount of exogenous glucose required to maintain euglycemia averaged 7.4 +/- 0.5 mg X kg-1 X min-1. The combination of leucine and insulin infusions did not alter the stimulated forearm glucose uptake nor did it change M (7.25 +/- 0.6 mg X kg-1 X min-1, P = NS).(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗

Processing of tRNA is accomplished by a high-molecular-weight enzyme complex.

An enzyme complex is a multifunctional catalytic unit that efficiently associates substrates with functionally related enzymes. The enzyme complex provides for the cellular regulation of enzymatic activities by physical interaction of the proteins with each other and by prior alteration of one enzyme's substrate by a related enzyme. Such regulatory abilities may go awry in neoplasia. Components of the protein biosynthetic machinery, such as aminoacyl-tRNA synthetases, have been thought to exist freely in the cytoplasm. However, high-molecular-weight enzyme complexes with aminoacyl-tRNA synthetase activities have been found in mammalian cells. We have been the first to report that the mammalian cell enzymes responsible for modification of tRNA occur in enzyme complexes (molecular weight 900000 daltons) associated with aminoacyl-tRNA synthetases and that the activities of these enzymes differ in normal and leukemic cells. Thus the enzymes responsible for the methylation of tRNA occur in enzyme complexes that provide efficient maturation of tRNA and possible regulation of protein synthesis. In FLC cells a unique enzyme complex composed of tRNA-methyltransferase and aminoacyl-tRNA synthetase activities has also been shown to contain a specific ribonuclease activity and a cysteine-tRNA sulfurtransferase activity. Sulfurtransferase activity has been characterized and optimized for its tRNA and cysteine substrates and mercaptoethanol and cation cofactors. Abnormal activity of this enzyme during neoplasia could result in improper acylation of tRNA and/or infidelity of coding by tRNA. Specific RNase is important in the sizing of percursor tRNA into mature tRNA. Results showed that this sizing was dependent upon the presence of the enzyme complex and the length of the incubation time. Many of the 20 aminoacyl-tRNA synthetases are also found in the complex. Electron microscopy has verified the subunit nature of the complex, seen previously by density gradient centrifugation and gel filtration. Three subunits, each of 300 000 daltons, comprise a complex approximately 200 A in diameter.

Amino Acyl-tRNA Synthetases↗