Source:http://linkedlifedata.com/resource/pubmed/id/12947086
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
45
|
| pubmed:dateCreated |
2003-11-3
|
| pubmed:abstractText |
The vacuolar-type H+-ATPases (V-ATPases) are multimeric proton pumps involved in a wide variety of physiological processes. We have identified two alternative splicing variants of C2 subunit isoforms: C2-a, a lung-specific isoform containing a 46-amino acid insertion, and C2-b, a kidney-specific isoform without the insert. Immunohistochemistry with isoform-specific antibodies revealed that V-ATPase with C2-a is localized specifically in lamellar bodies of type II alveolar cells, whereas the C2-b isoform is found in the plasma membranes of renal alpha and beta intercalated cells. Immunoprecipitation combined with immunohistological analysis revealed that C2-b together with other kidney-specific isoforms was selectively assembled to form a unique proton pump in intercalated cells. Furthermore, a chimeric yeast V-ATPase with mouse the C2-a or C2-b isoform showed a lower Km(ATP) and lower proton transport activity than that with C1 or Vma5p (yeast C subunit). These results suggest that V-ATPases with the C2-a and C2-b isoform are involved in luminal acidification of lamellar bodies and regulation of the renal acid-base balance, respectively.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
7
|
| pubmed:volume |
278
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
44843-51
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12947086-Acid-Base Equilibrium,
pubmed-meshheading:12947086-Alternative Splicing,
pubmed-meshheading:12947086-Amino Acid Sequence,
pubmed-meshheading:12947086-Blotting, Northern,
pubmed-meshheading:12947086-Cell Membrane,
pubmed-meshheading:12947086-Conserved Sequence,
pubmed-meshheading:12947086-Gene Expression,
pubmed-meshheading:12947086-Humans,
pubmed-meshheading:12947086-Immunohistochemistry,
pubmed-meshheading:12947086-Immunosorbent Techniques,
pubmed-meshheading:12947086-In Situ Hybridization,
pubmed-meshheading:12947086-Isoenzymes,
pubmed-meshheading:12947086-Kidney,
pubmed-meshheading:12947086-Kinetics,
pubmed-meshheading:12947086-Lung,
pubmed-meshheading:12947086-Microscopy, Immunoelectron,
pubmed-meshheading:12947086-Molecular Sequence Data,
pubmed-meshheading:12947086-Organ Specificity,
pubmed-meshheading:12947086-Proton Pumps,
pubmed-meshheading:12947086-Pulmonary Alveoli,
pubmed-meshheading:12947086-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12947086-Sequence Alignment,
pubmed-meshheading:12947086-Vacuolar Proton-Translocating ATPases
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Mouse proton pump ATPase C subunit isoforms (C2-a and C2-b) specifically expressed in kidney and lung.
|
| pubmed:affiliation |
Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Osaka 567-0047, Japan.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|