Young weanling albino rats were pair fed with control and thiamine deficient diets for five weeks. The analyses of skins and granulomas showed that, compared with the control, the thiamine deficient group had a decrease in the neutral salt soluble, insoluble, and total collagen con tents. The incorporation of glycine-1-14C into the skin collagen and the free glycine content of skins were also decreased. There was no change in the RNA and DNA contents of skins and granulomas. The urinary excretion of hydroxyproline or plasma hydroxyproline was not affected. The results suggest that there is a reduction of collagen synthesis in thiamine deficiency.In several skin diseases the metabolism of thiamine is disturbed (1-4). Thiamine was shown to accelerate wound healing (5). GOULD (6) suggested a potential role for B-complex vitamins in collagen metabolism. NATARAJAN and BOSE (7) reported a decrease of total hydroxyproline content of skins in thiamine deficient rats. In the present investigation the effect of thiamine defici ency on the metabolism of collagen has been studied.
MATERIALS AND METHODS.Twenty-one-day-old weanling albino rats were fed with a basal diet for five days and then divided into two groups of thirty-six each. The first group was fed a thiamine deficient diet (Nutritional Biochemicals, Cleavland, Ohio), while the second group was fed with the same diet, but with a supplement of thiamine hydrochloride (0.5mg/100g diet) and also the other required vitamins. The first group was given all the required vitamins except thiamine. The control animals were pair fed with thiamine deficient rats. Water was supplied ad lib. Daily records for food consumption were kept and the body weights were taken weekly. On the last day of the experimental period of five weeks, the urine from each rat was collected under toluene for a period of 24 hr. Glycine-1-14C was then injected into each rat intraperitoneally in 0.9% NaCl, the dose being 97
Rat pituitary extracts catalyze methylation of phosphatidylethanolamine to phosphatidylcholine using S-adenosyl-L-methionine as the methyl donor. In vitro incubation of hemipituitaries with 1 mM 2-methylaminoethanol led to a dose dependent decrease in phosphatidylethanolamine methyltransferase activity as well as the incorporation of the radioactivity from [3H-methyl]-L-methionine into phosphatidyl-choline. The inhibitory effect of 2-methylaminoethanol was selective for phospholipids methylation since protein carboxymethyltransferase and catechol-o-methyltransferase activities were not affected.
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