{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,4,2]],"date-time":"2022-04-02T03:07:13Z","timestamp":1648868833899},"reference-count":0,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Gastrointestinal and Liver Physiology"],"published-print":{"date-parts":[[1992,7,1]]},"abstract":"<jats:p> The influence of adenine and guanine nucleotides on cholecystokinin (CCK) receptor binding was examined in streptolysin O-permeabilized rat pancreatic acini. Specific binding of tracer to intact acini was 12.1 +\/- 0.4% per milligram protein, while permeabilized acini bound 34.6 +\/- 2.9% (n = 7). The increase in binding was also seen when normalized to DNA. Binding to permeabilized acini was reduced by the presence of 1 mM ATP to 23.0 +\/- 1.3%. Analysis of competitive inhibition of tracer binding by unlabeled CCK-8 was consistent with binding to two affinity states on intact acini, with the equilibrium dissociation constants for the high (KdH)- and low (KdL)-affinity states equal to 41 +\/- 5 pM and 5.2 +\/- 0.4 nM, respectively; permeabilized acini displayed a single binding site with Kd = 598 +\/- 40 pM. In the presence of 1 mM ATP, two states were seen on permeabilized acini with KdH = 85 +\/- 11 pM and KdL = 2.7 +\/- 0.6 nM. ATP, ATP gamma S, GTP, and GTP gamma S all inhibited binding, with half-maximal inhibition occurring at greater than 1 mM, 21 microM, 5 microM, and 0.4 microM, respectively. GTP gamma S (1 microM) also induced two affinity states with KdH = 112 +\/- 7 pM and KdL = 1.5 +\/- 0.2 nM (n = 3). Binding of CCK to pancreatic membranes was also decreased by ATP, and a similar regeneration of two binding affinity states was observed. ATP also decreased binding of [125I-Tyr4]bombesin to permeabilized acini, but in contrast did not generate two measurable binding affinity states.(ABSTRACT TRUNCATED AT 250 WORDS) <\/jats:p>","DOI":"10.1152\/ajpgi.1992.263.1.g44","type":"journal-article","created":{"date-parts":[[2017,12,24]],"date-time":"2017-12-24T02:41:57Z","timestamp":1514083317000},"page":"G44-G51","source":"Crossref","is-referenced-by-count":0,"title":["ATP induces two cholecystokinin binding affinity states in permeabilized rat pancreatic acini"],"prefix":"10.1152","volume":"263","author":[{"suffix":"Jr","given":"G. T.","family":"Blevins","sequence":"first","affiliation":[{"name":"Department of Physiology, University of Michigan, Ann Arbor48109-0622."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. A.","family":"Williams","sequence":"additional","affiliation":[{"name":"Department of Physiology, University of Michigan, Ann Arbor48109-0622."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"24","container-title":["American Journal of Physiology-Gastrointestinal and Liver Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.physiology.org\/doi\/pdf\/10.1152\/ajpgi.1992.263.1.G44","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,9,8]],"date-time":"2019-09-08T22:42:44Z","timestamp":1567982564000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.physiology.org\/doi\/10.1152\/ajpgi.1992.263.1.G44"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1992,7,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1992,7,1]]}},"alternative-id":["10.1152\/ajpgi.1992.263.1.G44"],"URL":"https:\/\/doi.org\/10.1152\/ajpgi.1992.263.1.g44","relation":{},"ISSN":["0193-1857","1522-1547"],"issn-type":[{"value":"0193-1857","type":"print"},{"value":"1522-1547","type":"electronic"}],"subject":[],"published":{"date-parts":[[1992,7,1]]}}}