Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structure-inhibitory profiles of nucleosides for the human intestinal N1 and N2Na(+)-nucleoside transporters
Autore:
Patil, SD; Ngo, LY; Unadkat, JD;
Indirizzi:
Univ Washington, Dept Pharmaceut, Seattle, WA 98195 USA Univ Washington Seattle WA USA 98195 pt Pharmaceut, Seattle, WA 98195 USA
Titolo Testata:
CANCER CHEMOTHERAPY AND PHARMACOLOGY
fascicolo: 5, volume: 46, anno: 2000,
pagine: 394 - 402
SICI:
0344-5704(200011)46:5<394:SPONFT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
BORDER MEMBRANE-VESICLES; XENOPUS-LAEVIS OOCYTES; HUMAN KIDNEY; 2',3'-DIDEOXYCYTIDINE; EXPRESSION; ANALOGS; CELLS;
Keywords:
human intestine; hCNT1 and hCNT2-Na+-nucleoside transporters; N1 (cif) and N2 (cit) Na+-nucleoside transporters; nucleoside drugs; antiviral drugs; anticancer drugs; drug absorption;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
15
Recensione:
Indirizzi per estratti:
Indirizzo: Unadkat, JD Univ Washington, Dept Pharmaceut, Box 357610, Seattle, WA 98195 USA Univ Washington Box 357610 Seattle WA USA 98195 , WA 98195 USA
Citazione:
S.D. Patil et al., "Structure-inhibitory profiles of nucleosides for the human intestinal N1 and N2Na(+)-nucleoside transporters", CANC CHEMOT, 46(5), 2000, pp. 394-402

Abstract

Purpose: To determine the structure-inhibitory profiles of nucleosides forthe N1 and N2 Na+-nucleoside transporters of the human intestine, Methods:The uptake of H-3-labeled prototypic substrates of the N1 (inosine) and N2 (thymidine) transporters into human intestinal brush border membrane vesicles was measured by a rapid filtration technique in the presence and absenceof various uridine and adenosine analogs and antiviral and anticancer nucleoside drugs (100 and 1000 muM) Results: In the ribose ring, the 3'-oxygen is required for inhibition of uptake of nucleosides by both the N1 and N2 transporters. The structural requirements for such inhibition differ with respect to modifications on the 5' position of the sugar ring or on the base. The N2 transporter is more tolerant to these substitutions than is the N1 transporter. The 6 position on uracil and the 8 position on adenine are critical for inhibition of uptake of nucleosides by both the N1 and N2 nucleoside transporters. Conclusions: These data are the first evidence that the binding site(s) of the human N1 and N2 transporters differ in their interaction with analogs of their common substrates, uridine and adenosine. Such studies can provide insight into the critical structural determinants of the substrate necessary for recognition by the Na+-nucleoside transporters of the human intestine.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 00:46:23