{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,21]],"date-time":"2026-02-21T04:11:44Z","timestamp":1771647104392,"version":"3.50.1"},"reference-count":0,"publisher":"American Physiological Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[1983,11,1]]},"abstract":"<jats:p> Oxidized nicotinamide adenine dinucleotide (NAD+) in cytosol may interact with renal brush-border membranes (BBM) and inhibit BBM phosphate transport. The possible mechanism of interaction was investigated in the present study. Incubation of BBM with [adenine-3H]NAD+ led to acid-stable binding of 3H to the BBM, in contrast there was no binding of 14C when [carbonyl-14C]NAD+ was used. The data are consistent with an ADP-ribosylation mechanism involving transfer of ADP-ribose from NAD+ to BBM. This was confirmed by using [adenylate-32P]NAD+ and by the release of bound 32P in the form of 5'-[32P]AMP when the BBM were treated with snake venom phosphodiesterase. After gradient centrifugation of BBM the ADP-ribosyltransferase was recovered at the same density as known BBM enzymes, indicating that ADP-ribosyltransferase is an intrinsic BBM component and not a contaminant. These findings indicate that cytosolic NAD+ may be used for ADP-ribosylation of BBM proteins and that this may be a mechanism for regulating the BBM phosphate transport system. <\/jats:p>","DOI":"10.1152\/ajpcell.1983.245.5.c449","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T11:32:17Z","timestamp":1514115137000},"page":"C449-C456","source":"Crossref","is-referenced-by-count":33,"title":["NAD+-dependent ADP-ribosyltransferase in renal brush-border membranes"],"prefix":"10.1152","volume":"245","author":[{"given":"S. A.","family":"Kempson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N. P.","family":"Curthoys","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.physiology.org\/doi\/pdf\/10.1152\/ajpcell.1983.245.5.C449","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T19:55:23Z","timestamp":1718654123000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.physiology.org\/doi\/10.1152\/ajpcell.1983.245.5.C449"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1983,11,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1983,11,1]]}},"alternative-id":["10.1152\/ajpcell.1983.245.5.C449"],"URL":"https:\/\/doi.org\/10.1152\/ajpcell.1983.245.5.c449","relation":{},"ISSN":["0363-6143","1522-1563"],"issn-type":[{"value":"0363-6143","type":"print"},{"value":"1522-1563","type":"electronic"}],"subject":[],"published":{"date-parts":[[1983,11,1]]}}}