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Titolo:
Cellular transport processes of aminoguanidine, a nitric oxide synthase inhibitor, in the opossum kidney cell culture line
Autore:
Doan, KMM; Ng, S; Boje, KMK;
Indirizzi:
SUNY Buffalo, Sch Pharm, Dept Pharmaceut, Buffalo, NY 14260 USA SUNY Buffalo Buffalo NY USA 14260 Dept Pharmaceut, Buffalo, NY 14260 USA
Titolo Testata:
INTERNATIONAL JOURNAL OF PHARMACEUTICS
fascicolo: 2, volume: 194, anno: 2000,
pagine: 209 - 220
SICI:
0378-5173(20000125)194:2<209:CTPOAA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
BORDER MEMBRANE-VESICLES; ORGANIC CATION TRANSPORTER; FUNCTIONAL EXPRESSION; AMINO-ACIDS; EXPERIMENTAL MENINGITIS; ADVANCED GLYCOSYLATION; GUANIDINE TRANSPORT; MOUSE BLASTOCYSTS; SYSTEM; MECHANISMS;
Keywords:
aminoguanidine; cell culture; guanidine; organic cation; transport; OK cell culture;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Boje, KMK SUNY Buffalo, Sch Pharm, Dept Pharmaceut, H517 Cooke Hochstetter, Buffalo,NY 14260 USA SUNY Buffalo H517 Cooke Hochstetter Buffalo NY USA 14260 260 USA
Citazione:
K.M.M. Doan et al., "Cellular transport processes of aminoguanidine, a nitric oxide synthase inhibitor, in the opossum kidney cell culture line", INT J PHARM, 194(2), 2000, pp. 209-220

Abstract

Aminoguanidine has potential pharmacologic utility for diabetes and nitricoxide - mediated inflammation. Because aminoguanidine is positively charged at physiologic pH (pK(a) similar to 10), it is unlikely that simple diffusion is a predominant mechanism for cellular penetration. This study soughtto determine the transport processes by which aminoguanidine, a cationic compound, traverses across cellular membranes. In cultured opossum kidney (OK) cell monolayers, aminoguanidine transport involved both saturable and non-saturable diffusion processes. At passage numbers below 67, the observed V-max and K-m for saturable influx were significantly lower than that observed at passages greater than 79 (V-max: low passage, 21.2 +/- 7.8 pmol/(min*mg protein), n = 3; versus high passage, 129.7 +/- 24.3 pmol/(min*mg protein), n = 3, P < 0.05; K-m: low passage, 23.7 +/- 10.8 mu M, n = 3, versus high passage, 101.7 +/- 5.6 mu M, n = 3, P < 0.05; mean +/- S.E.M.). Nonsaturable processes were not statistically different (k(ns): low passage. 1.6 +/- 0.1 pmol/(min*mg protein*mu M), n = 3, high passage, 1.1 +/- 0.2 pmol/(min*mg proteins*mu M) n = 3). Saturable influx was temperature dependent, and independent of ATP energy, sodium gradients or changes in membrane potential. Other organic cations competitively inhibited and trans-stimulated saturable influx. Aminoguanidine influx was increased in the presence of an outwardly-directed proton gradient and was inhibited in the presence of an inwardly-directed proton gradient. Correspondingly, aminoguanidine efflux wastrans-stimulated by aminoguanidine and guanidine. In summary, OK cell cultures at high passage numbers (> 79) express a saturable, bi-directional carrier-mediated process to transport aminoguanidine across cellular membranes. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 04:15:37