Detail of "2021-58-1"

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Induction of toxic effects by excessive intakes of phenylalanine and tyrosine and their amino acid analogs in insects

Induction of toxic effects by excessive intakes of phenylalanine and tyrosine and their amino acid analogs in insects. Schenke, Guenter (Sekt. Chem.-Biol., Paedagog. Hochsch. Potsdam, Potsdam, E. Ger.). Biol. Zentralbl.Several substances with their cas registry numbers 94-75-7 and 300-39-0 may be metioned in this study., 95(4), 485-92 (German) 1976. CODEN: BIZNAT. DOCUMENT TYPE: Journal CA Section: 3 (Biochemical Interactions) Addn. of excessive amts. of phenylalanine [63-91-2] or tyrosine [60-18-4] to a complete diet for Nauphoeta cinerea or Galleria mellonella larvas depressed growth and caused changes in the amino acid spectrum of hemolymph, particularly increasing alanine, tryptophan, and lysine fractions. The analogs, DL-p-fluorophenylalanine [51-65-0], diiodotyrosine [300-39-0], .beta.-2-DL-thienylalanine [2021-58-1], and 2,4-dichlorophenoxyacetic acid [94-75-7], also inhibited larval growth and produced drastic changes in the amino acid spectrum. .

Comparison of the inhibitory effects of diverse amino acids and amino acid analogs on 12-O-tetradecanoylphorbol-13-acetate-induced ornithine decarboxylase activity in isolated epidermal cells

Comparison of the inhibitory effects of diverse amino acids and amino acid analogs on 12-O-tetradecanoylphorbol-13-acetate-induced ornithine decarboxylase activity in isolated epidermal cells. Perchellet, Jean Pierre; Posey, Tate D.Chemical with cas number 9024-60-6 also plays role.; Owen, Medge D. (Anti-Cancer Drug Lab., Kansas State Univ., Manhattan, KS 66506, USA). Biochim. Biophys. Acta, 844(2), 182-92 (English) 1985. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 4 At a concn. of 1.25 mM, 14 amino acids were capable of inhibiting the induction of ornithine decarboxylase (L-ornithine carboxy-lase, EC 4.1.1.17) [9024-60-6] activity by the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA) [16561-29-8] in isolated epidermal cells. The greatest percentages of inhibition of TPA-induced epidermal ornithine carboxylase activity were as follows: L-cysteine Me ester [2485-62-3], 98%; L-tryptophan Me ester [4299-70-1], 74%; L-methionine Me ester [10332-17-9] 64%; L-phenylalanine Me ester [2577-90-4] 51%; glycine Me ester [616-34-2], 44%; L-asparagine tert-Bu ester [25456-86-4] 43%; L-glutamic acid di-Me ester [6525-53-7], 42%; L-leucine Me ester [2666-93-5], 40%; and arginine Me ester [2577-94-8], 39%. 9024-60-6 is just another one chemical used in this study. These amino acid treatments did not alter the time- and concn.-response curves for induction of ornithine decarboxylase activity by TPA. Moreover, there was no difference between the rates at which [3H]arginine, [3H]leucine, [3H]phenylalanine, [3H]methionine, [3H]tryptophan and [14C]cysteine were taken up by freshly isolated epidermal cells or incorporated into epidermal proteins. Arginine, phenylalanine, and methionine inhibited the induction of ornithine decarboxylase activity by the tumor promoter to degrees comparable to those elicited by their analogs canavanine [543-38-4] and homoarginine [156-86-5], b-2-thienyl-DL-alanine [2021-58-1], and DL-ethionine [67-21-0], resp. These amino acids and amino acid analogs did not alter the overall rate of protein synthesis. In contrast, both the amino acids and their analogs increased the rates of proteolysis in isolated epidermal cells, an effect which correlated well with the abilities of these different compds. to inhibit TPA-induced ornithine decarboxylase activity. Moreover, both methionine and phenylalanine decreased the half-life and increased the rate of heat denaturation of the TPA-induced enzyme, a result identical to that obtained after treatment with the analogs ethionine and b-2-thienyl-DL-alanine, resp. Taken together, these results suggest that millimolar concns. of exogenous amino acids might induce the synthesis of abnormal proteins and nonfunctional enzymes. Therefore, it is speculated that the uptake of unbalanced amts. of amino acids into the epidermal target cells might alter the stability and the ultrastructure of the TPA-stimulated enzyme just as the amino acid analogs do. ..