Linked Life Data

7520707

Source:http://linkedlifedata.com/resource/pubmed/id/7520707

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1994-9-29
pubmed:abstractText
Rabbit gastric glands were treated with alpha-toxin to test for permeabilization of basolateral membrane and retention of functional activity of parietal cells. Treatment with up to 400 U alpha-toxin/mL resulted in a dose-dependent increase in permeabilization, as judged by nuclear uptake of trypan blue (960 daltons), while causing relatively little loss of cytoplasmic macromolecules in the size range of lactate dehydrogenase (134,000 daltons). In the presence of cAMP and ATP, alpha-toxin-permeabilized resting gastric glands were stimulated to accumulate aminopyrine by approximately 10-fold over glands incubated without added nucleotides. Aminopyrine accumulation in stimulated permeabilized glands was inhibited by specific H+,K(+)-ATPase inhibitors, omeprazole and SCH-28080, and by the selective inhibitor of protein kinase A, H-89 (IC50 = 7.17 +/- 2.05 microM; n = 4). Aminopyrine accumulation in the alpha-toxin-treated glands was dependent on both exogenous ATP and cAMP; however, when no exogenous ATP was present, cAMP-activated aminopyrine accumulation reached approximately 50% of maximum, and at levels of ATP > 0.05 mM, maximal aminopyrine accumulation occurred without exogenous cAMP. In the presence of ATP alone, aminopyrine accumulation in permeabilized glands achieved 61.1 +/- 3.2% (n = 10; range, 50-70%) of the values measured on paired samples of intact glands stimulated with histamine plus isobutylmethylxanthine. These results demonstrate the functional responsiveness of alpha-toxin-permeabilized resting gastric glands. The participation of a protein kinase A dependent pathway during activation of permeabilized parietal cell is proposed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-Methyl-3-isobutylxanthine, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Aminopyrine, http://linkedlifedata.com/resource/pubmed/chemical/Bucladesine, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/H( )-K( )-Exchanging ATPase, http://linkedlifedata.com/resource/pubmed/chemical/Histamine, http://linkedlifedata.com/resource/pubmed/chemical/Isoquinolines, http://linkedlifedata.com/resource/pubmed/chemical/N-(2-(4-bromocinnamylamino)ethyl)-5-..., http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
pubmed:status
MEDLINE
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26-35
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:articleTitle
Acid secretion in alpha-toxin-permeabilized gastric glands.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.