Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-3-21
pubmed:abstractText
We compare the retinal rod photocurrent before and after introduction of an hydrolysis-resistant analog of GTP into the outer segment by the whole-cell patch technique. Others have shown that GTP bound to transducin leads to the hydrolysis of cyclic GMP, causing the response to light--a decrease in dark current. The hydrolysis-resistant GTP analog prolongs the response to a bright flash, which leads us to suggest that prolonged transducin activation by bright light desensitizes the rod by a prolonged decrease in dark current. Recovery from the response to a bright flash does occur after introduction of the analog; that recovery requires acceleration of cyclase activity rather than inhibition of phosphodiesterase. The analog mimics light adaptation by desensitizing the rod and speeding the recovery from a dim flash. The analog plus light or light adaptation prolongs the activities of transducin and phosphodiesterase (oligonucleate 5'-nucleotidohydrolase, EC 3.1.4.1) to mediate desensitization by reducing the dark current. Hence, this faster recovery from a dim flash would be by increased activity of guanylate cyclase [GTP pyrophosphate-lyase (cyclizing), EC 4.6.1.2] rather than by inhibited phosphodiesterase. Accelerated activity of guanylate cyclase may speed recovery by response truncation. We conclude that transducin, activated by photolyzed rhodopsin, may lead to increased activity of both phosphodiesterase and guanylate cyclase to mediate the desensitization and the faster recovery of the light-adapted response.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2417228, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2423011, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2578616, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2578628, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2873060, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-2982108, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3006038, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3018756, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3032080, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3485283, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3920215, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-3981127, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-6288836, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-6307996, http://linkedlifedata.com/resource/pubmed/commentcorrection/2893382-6930647
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1322-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Rod light adaptation may be mediated by acceleration of the phosphodiesterase-guanylate cyclase cycle.
pubmed:affiliation
Department of Ophthalmology and Visual Science, Yale Medical School, New Haven, CT 06510.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't