Detail of "1622-62-4"

Reference

Benzodiazepine inhibition of flunitrazepam receptor binding, adenosine uptake, and pentylenetetrazol-induced seizures in mice

Benzodiazepine inhibition of flunitrazepam receptor binding, adenosine uptake, and pentylenetetrazol-induced seizures in mice. Chweh, Andrew Y.; Swinyard, Ewart A.; Wolf, Harold H. (Coll. Pharm., Univ. Utah, Salt Lake City, UT 84112, USA). Can. J. Physiol. Pharmacol. 439-14-5 and 58-61-7 which are cas registry numbers are also used here., 62(1), 132-5 (English) 1984. CODEN: CJPPA3. ISSN: 0008-4212. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) The potencies of 7 benzodiazepines (BDZs) were established by 3 tests: inhibition of flunitrazepam [1622-62-4] receptor binding, inhibition of adenosine [58-61-7] uptake, and prevention of pentylenetetrazol-induced seizures in mice. There was a high correlation between the potency for inhibition of flunitrazepam receptor binding and the anti-pentylenetetrazol potencies of benzodiazepines. The anti-pentylenetetrazol potencies of benzodiazepines correlated well with their ability to inhibit adenosine uptake. However, there was no significant correlation between the potency for the inhibition of flunitrazepam receptor binding and the potency for inhibition of adenosine uptake. In addn., there is a marked difference in BDZ potency as measured by these 2 tests in vitro. Apparently, anti-pentylenetetrazol activity of benzodiazepines results from an interaction between BDZ and nanomolar affinity BDZ receptors. .

Nucleoside transport in heart: species differences in nitrobenzylthioinosine binding, adenosine accumulation, and drug-induced potentiation of adenosine action

Nucleoside transport in heart: species differences in nitrobenzylthioinosine binding, adenosine accumulation, and drug-induced potentiation of adenosine action.Some chemicals with cas registry numbers like 58-61-7 and 38048-32-7 are also used. Williams, Evan F.; Barker, Philip H.; Clanachan, A. S. (Dep. Pharmacol., Univ. Alberta, Edmonton, AB T6G 2H7, Can.). Can. J. Physiol. Pharmacol., 62(1), 31-7 (English) 1984. CODEN: CJPPA3. ISSN: 0008-4212. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 13 The site-specific binding of the potent and selective nucleoside transport inhibitor, nitrobenzylthioinosine (NBMPR) [38048-32-7], to the nucleoside transport system of cardiac membranes of several species was investigated. The concn. of NBMPR at these sites ranged from 0.03 nM in rats to 0.78 nM in dogs. The maximal binding capacity of cardiac membranes for NBMPR was also species-dependent and was greatest in bovine and guinea pig heart and least in rat. The affinities of recognized nucleoside transport inhibitors and benzodiazepines for these transport inhibitory sites in guinea pig and rat heart were estd. by studying the inhibition of the site-specific binding of NBMPR in competition expts. These values were compared with their inhibitory effects on the transporter-dependent accumulation of adenosine in guinea pig and rat cardiac muscle segments and with their ability to potentiate the neg. inotropic action of adenosine [58-61-7] in elec. driven guinea pig and rat left atria. In guinea pig heart, the recognized nucleoside transport inhibitors and benzodiazepines had an order of affinity, dilazep [35898-87-4] > hydroxynitrobenzylthioguanosine [41094-07-9] > dipyridamole [58-32-2] > hexobendine [54-03-5] >> lidoflazine [3416-26-0] >> flunitrazepam [1622-62-4] > diazepam [439-14-5] > lorazepam [846-49-1] > flurazepam [17617-23-1], for the NBMPR site which was similar to those for the inhibition of adenosine accumulation and for potentiation of adenosine action. In contrast, in rat heart, where the maximal binding capacity of NBMPR was lower (8-fold), the nucleoside transporter dependent accumulation of adenosine was also lower (6-fold) and the neg. inotropic action of adenosine was not significantly potentiated. Furthermore, NBMPR sites in rat heart displayed a lower affinity for hexobendine, dipyridamole, and lidoflazine relative to sites in guinea pig hearts. Apparently, differences in cardiac nucloside transport systems exist among species with respect to both membrane d. and drug affinity. Such differences influence the ability of transport inhibitors to modify adenosine action in these tissues. .