Detail of "13184-27-5"

Reference

Effects of acivicin and dichloroallyl lawsone upon pyrimidine biosynthesis in mouse L1210 leukemia cells

Effects of acivicin and dichloroallyl lawsone upon pyrimidine biosynthesis in mouse L1210 leukemia cells. Kemp, Anthony J.; Lyons, Stephen D.; Christopherson, Richard I. (Russell Grimwade Sch. Biochem., Univ. Melbourne, Parkville 3052, Australia). J. Biol. Chem., 261(32), 14891-5 (English) 1986. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 9 NSC 163501 (acivicin) [42228-92-2] and NSC 126771 (dichloroallyl lawsone) [36417-16-0] are potent inhibitors of nucleotide biosynthesis with consequent anticancer activity against certain exptl. tumors. To det. in detail the metabolic events induced by each inhibitor, a new 2-dimensional chromatog. procedure has been devised for measurement of the concns. of all pyrimidine intermediates and some purine nucleotides from 100 mL of an ext. of cells grown in the presence of [14C]bicarbonate. Addn. of acivicin (25 mM) to mouse L 1210 leukemia cells causes severe depletion in the cellular levels of CTP [65-47-4] and GTP [86-01-1], accumulation of uridine nucleotides, and abrupt but transient increases in the concns. of the early intermediates of both the pyrimidine and purine pathways. Addn. of dichloroallyl lawsone (25 mM) results in a rapid depletion of uridine and cytidine nucleotides; carbamyl aspartate [13184-27-5] and dihydroorotate [155-54-4] accumulate to high levels in an equil. ratio of 20.5:1, and orotate [65-86-1], orotidine [314-50-1], and UMP [58-97-9] increase transiently before decreasing to levels approaching their original steady states. The predominant inhibitory effects of acivicin are upon the reactions UTP [63-39-8] ? CTP and XMP [523-98-8] ? GMP [85-32-5], but there is also an initial transient activation of both the pyrimidine and purine pathways by acivicin. 58-97-9 and 56-65-5 are just another two chemicals used in this study. The data obtained with dichloroallyl lawsone are consistent with inhibition of the conversion of UMP ? UDP [58-98-0] initially followed by potent inhibition of dihydroorotate ? orotate. .

Inhibition by N-acetyl-aspartate of aspartate binding to a proteolipid fraction from rat cerebral cortex

Inhibition by N-acetyl-aspartate of aspartate binding to a proteolipid fraction from rat cerebral cortex. Burgal, M.; Lizondo, J.In this study， 997-55-7 and 56-86-0 are also used.; Jorda, A.; Grisolia, S. (Inst. Invest. Citol. Caja Ahorros Valencia, Valencia, Spain). Neurochem. Res., 9(2), 219-24 (English) 1984. CODEN: NEREDZ. ISSN: 0364-3190. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) N-Acetylaspartate [997-55-7] was bound by a rat brain proteolipid fraction that specifically binds aspartate [56-84-8] and glutamate [56-86-0], and N-acetylaspartate inhibited the binding of aspartate by this fraction. The structural analogs N-carbamylaspartate [13184-27-5] and N-methylaspartate [4226-18-0] also inhibited aspartate binding. Since N-acetylaspartate was previously shown to increase intracellular levels of cyclic nucleotides, this compd. may function in the brain both by blocking the action of aspartate and by producing a physiol. response by itself. It has been reported that N-acetylaspartate does not interfere with glutamate binding to specific synaptosomal receptors. .