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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-8-25
|
| pubmed:abstractText |
Three isoforms of fructose-1,6-bisphosphate aldolase were found to bind specifically to the actin-containing filament of the cytoskeleton and to show tissue-specific binding patterns. Aldolase A (muscle type) bound more tightly to the skeletal muscle cytoskeleton among the three isozymes, while aldolase B (liver type) preferred the liver cytoskeleton to those of other tissues. The specific binding of aldolase A to the skeletal muscle cytoskeleton was inhibited strongly by the substrates fructose 1,6-bisphosphate and fructose 1-phosphate. Several mutant aldolases A were examined to identify the amino acid residues or regions that play a role in specific binding. Among the mutant aldolases tested, A-E34D, A-K41N, and A-Y363S exhibited remarkably reduced binding activities. Experiments using FITC-labeled enzymes and Rh-labeled phalloidin disclosed that aldolase A associated with the cytoskeleton. Specifically, when aldolase A was incubated with human fibroblast MRC-5 permeabilized with Triton X-100, aldolase A bound to the actin filaments in the stress fibers within the cell. Aldolase A reversibly inhibited the contraction of MRC-5 cells which usually occurred in the presence of Mg2(+)-ATP and Ca2+. These results provide direct evidence that aldolase binds specifically to the actin-containing stress fibers and suggest that aldolase may regulate cell contraction through its reversible binding to the filaments in the permeabilized MRC-5 fibroblast.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescein-5-isothiocyanate,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose-Bisphosphate Aldolase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/NAD
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0003-9861
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
344
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
184-93
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9244396-Actin Cytoskeleton,
pubmed-meshheading:9244396-Actins,
pubmed-meshheading:9244396-Adenosine Diphosphate,
pubmed-meshheading:9244396-Adenosine Triphosphate,
pubmed-meshheading:9244396-Animals,
pubmed-meshheading:9244396-Antibodies, Monoclonal,
pubmed-meshheading:9244396-Brain,
pubmed-meshheading:9244396-Cytoskeleton,
pubmed-meshheading:9244396-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9244396-Fluorescein-5-isothiocyanate,
pubmed-meshheading:9244396-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:9244396-Humans,
pubmed-meshheading:9244396-Isoenzymes,
pubmed-meshheading:9244396-Liver,
pubmed-meshheading:9244396-Muscle, Skeletal,
pubmed-meshheading:9244396-Mutation,
pubmed-meshheading:9244396-NAD,
pubmed-meshheading:9244396-Protein Binding,
pubmed-meshheading:9244396-Rats
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Mode of interactions of human aldolase isozymes with cytoskeletons.
|
| pubmed:affiliation |
Department of Biochemistry, Saga Medical School, Nabeshima, Saga, Japan. kusakabe@bcmp.med.harvard.edu
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|