Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4 Pt 1
|
| pubmed:dateCreated |
1987-5-13
|
| pubmed:abstractText |
The objective of this work is to establish a procedure to study the stimulation-dependent membrane redistribution and properties of H+-K+-ATPase in an in vitro model system, rabbit isolated gastric glands. Stimulated (10(-4) M histamine plus 10(-5) M forskolin) and resting (10(-4) M metiamide) glands were homogenized and fractionated into PO (40 g, 5 min), P1 (400 g, 10 min), P2 (14,500 g, 10 min), P3 (48,200 g, 90 min), and supernatant, S3. Significant changes occurred in the distribution of our marker for H+-K+-ATPase (K+-p-nitrophenyl phosphatase) activity: a reduction in activity of P3 and a compensatory increment in P1. P3 showed valinomycin (Val)-dependent vesicular H+ uptake, while H+ uptake in P1 was Val independent. Direct measurements of ATPase revealed that H+-K+-ATPase activity of P3 was Val dependent and decreased by stimulation; H+-K+-ATPase activity of P1 was Val independent and increased by stimulation. Further density gradient purification of P1 showed that membranes lighter than 17% Ficoll contained higher specific H+-K+-ATPase activity, and the observed increase in H+-K+-ATPase associated with stimulation was more pronounced. Also, the lighter fractions from stimulated P1 had much latent H+-K+-ATPase activity that was unmasked by n-octylglucoside. The properties of membrane fractions from isolated glands were consistent with results obtained in vivo: high H+-K+-ATPase activity of P3 from resting glands corresponds to cytoplasmic tubulovesicles lacking KCl transport pathways; high activity of P1 from stimulated glands corresponds to apical plasma membrane vesicles containing KCl transport in addition to the H+-K+-ATPase, and full competency for the generation of HCl.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Carbachol,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosides,
http://linkedlifedata.com/resource/pubmed/chemical/H( )-K( )-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Histamine,
http://linkedlifedata.com/resource/pubmed/chemical/Metiamide,
http://linkedlifedata.com/resource/pubmed/chemical/Oligomycins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/octyl-beta-D-glucoside
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0002-9513
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
252
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
G458-65
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:3031993-Adenosine Triphosphatases,
pubmed-meshheading:3031993-Animals,
pubmed-meshheading:3031993-Carbachol,
pubmed-meshheading:3031993-Cell Compartmentation,
pubmed-meshheading:3031993-Cyclic AMP,
pubmed-meshheading:3031993-Female,
pubmed-meshheading:3031993-Forskolin,
pubmed-meshheading:3031993-Gastric Juice,
pubmed-meshheading:3031993-Glucosides,
pubmed-meshheading:3031993-H(+)-K(+)-Exchanging ATPase,
pubmed-meshheading:3031993-Histamine,
pubmed-meshheading:3031993-Hydrogen-Ion Concentration,
pubmed-meshheading:3031993-Male,
pubmed-meshheading:3031993-Metiamide,
pubmed-meshheading:3031993-Microsomes,
pubmed-meshheading:3031993-Oligomycins,
pubmed-meshheading:3031993-Potassium,
pubmed-meshheading:3031993-Rabbits,
pubmed-meshheading:3031993-Stomach,
pubmed-meshheading:3031993-Time Factors
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
Stimulation-associated redistribution of H+-K+-ATPase activity in isolated gastric glands.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|