Detail of "120054-86-6"

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1,4-dihydropyridines for application in combatting resistance to drugs

1,4-dihydropyridines for application in combatting resistance to drugs. Ulrich, Wolf Ruediger; Flockerzi, Dieter; Klemm, Kurt; Sanders, Karl; Boer, Rainer; Boss, Hildegard; Beller, Klaus Dieter; Eichelbaum, Michel (BYK-Gulden Lomberg Chemische Fabrik G.m.b.H., Germany). PCT Int. Appl. WO 9118599 A2 12 Dec 1991, 26 pp. DESIGNATED STATES: W: AU, CA, DE, FI, HU, JP, KR, NO, PL, SU, US; RW: AT, BE, CH, DE, DK, ES, FR, GB, GR, IT, LU, NL, SE. (World Intellectual Property Organization). CODEN: PIXXD2. CLASS: ICM: A61K031-44. APPLICATION: WO 91-EP957 22 May 1991. PRIORITY: DE 90-4017061 26 May 1990; CH 90-2479 26 Jul 1990. DOCUMENT TYPE: Patent CA Section: 1 (Pharmacology) Known 1,4-dihydropyridines I (R1, R3 = C1-6-alkyl, C1-4-alkoxy, C2-4-alkyl; R2 = H, NH2, R1; R4 = substituted Ph; R5NR6 = ring; E2 = alkylene, alkenylene, alkynylene, oxaalkylene, etc.) and their pharmacol. compatible salts are useful for improving the action of antibiotics and cytostatics and suppressing resistance to these agents. Thus, growth of tumor cell lines resistant to the cytostatics vincristine and daunomycin was tested in the presence of each of these agents alone or combined with 10-6M or 10-7M II-HCl. In each case a marked enhancement of cytotoxic activity of the drugs was obsd. II-HCl alone had cytotoxic activity, but to a lesser extent than when combined with the cytostatics.Except for chemicals metioned above, 23214-92-8 and 120054-86-6 are also used. I act similarly with all classes of cytostatics, and also exhibit synergism with and reverse the resistance to the antimalarial drug chloroquine. .

Subtype-specific dimerization of a1-adrenoceptors: Effects on receptor expression and pharmacological properties

Subtype-specific dimerization of a1-adrenoceptors: Effects on receptor expression and pharmacological properties. Uberti, Michelle A.; Hall, Randy A.; Minneman, Kenneth P. (Department of Pharmacology, Emory University School of Medicine, Atlanta, GA, USA). Molecular Pharmacology, 64(6), 1379-1390 (English) 2003 American Society for Pharmacology and Experimental Therapeutics. CODEN: MOPMA3. ISSN: 0026-895X. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) The potential role of dimerization in controlling the expression and pharmacol. properties of a1-adrenoceptor subtypes was examd.Some commonly used reagents like 51-41-2 and 120054-86-6 are used in this experiment. using coimmunopptn. of epitope-tagged receptors. Human a1-adrenoceptor subtypes (a1A, a1B, a1D) were tagged at their N-termini with Flag or hemagglutinin epitopes and transfected into human embryonic kidney 293 cells. Homodimerization of all three subtypes was obsd. by coimmunopptn. of receptors with different tags and was not altered by norepinephrine treatment. Heterodimer formation between hemagglutinin-tagged a1B-adrenoceptors and Flag-tagged a1A- or a1D-adrenoceptors was also obsd. However, no a1A/a1D-adrenoceptor heterodimers were obsd., suggesting that dimerization is subtype-specific. The extent of heterodimerization was also unaltered by norepinephrine treatment. a1-Adrenoceptor truncation mutants lacking carboxyl or N-terminal sequences formed homo- and heterodimers similarly to full-length receptors, suggesting that these domains play little or no role in dimerization. Biotinylation with a membrane-impermeable agent showed that monomers and homo- and hetero-oligomers of all three subtypes are expressed on the cell surface. Radioligand binding studies showed that heterodimerization did not alter the affinity of a1-adrenoceptors for norepinephrine, prazosin, or subtype-selective antagonists, suggesting that dimerization does not result in pharmacol. distinct subtypes. However, coexpression of a1B-adrenoceptors significantly increased both binding site d. and protein expression of a1A- and a1D-adrenoceptors, and increased cell surface expression of a1D-adrenoceptors, suggesting a functional role for heterodimerization. Conversely, coexpression of a1A-with a1D-adrenoceptors, which did not heterodimerize, had no effect on receptor d. or protein. These studies demonstrate subtype-selective heterodimerization of a1-adrenoceptors, which does not change their pharmacol. properties but seems to have functional consequences in regulating receptor expression and trafficking. .