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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1984-7-13
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pubmed:abstractText |
The membrane of chromaffin granule, the secretory vesicle of adrenal medullary cells storing catecholamines, enkephalins, and many other components, interacts with F-actin. Using low shear falling ball viscometry to estimate actin binding to membranes, we demonstrated that mitochondrial and plasma membranes from chromaffin cells also provoked large increases in viscosity of F-actin solutions. Mitochondrial membranes also had the capacity to cause complete gelation of F-actin. In addition, vasopressin-containing granules from neurohypophysial tissue were shown to bind F-actin and to increase the viscosity of F-actin solutions. Using an antibody directed against human erythrocyte spectrin, it was found that a spectrin-like protein was associated with secretory granule membrane, mitochondrial membrane, and plasma membrane. The chromaffin granule membrane-associated spectrin-like protein faces the cytoplasmic side, is composed of two subunits (240 kD and 235kD ), the alpha-subunit (240 kD, pHi5 .5) being recognized by the antibody. Nonionic detergents such as Triton X-100 or Nonidet P40 failed to release fully active spectrin-like protein. In contrast, Kyro EOB , a different nonionic detergent, was found to release spectrin-like protein while keeping intact F-actin binding capacity, at least below 0.5% Kyro EOB concentration. Chromaffin cells in culture were stained with antispectrin antibody, showing the presence of spectrin-like protein in the cell periphery close to the cell membrane but also in the cytoplasm. We conclude that in living cells the interaction of F-actin with chromaffin granule membrane spectrin observed in vitro is important in controlling the potential function of secretory vesicles.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Dopamine beta-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monoamine Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Spectrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1558-69
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6374036-Acetylcholinesterase,
pubmed-meshheading:6374036-Actins,
pubmed-meshheading:6374036-Adrenal Medulla,
pubmed-meshheading:6374036-Animals,
pubmed-meshheading:6374036-Cattle,
pubmed-meshheading:6374036-Cell Fractionation,
pubmed-meshheading:6374036-Chromaffin Granules,
pubmed-meshheading:6374036-Chromaffin System,
pubmed-meshheading:6374036-Dopamine beta-Hydroxylase,
pubmed-meshheading:6374036-Fluorescent Antibody Technique,
pubmed-meshheading:6374036-Intracellular Membranes,
pubmed-meshheading:6374036-Membrane Proteins,
pubmed-meshheading:6374036-Monoamine Oxidase,
pubmed-meshheading:6374036-Protein Binding,
pubmed-meshheading:6374036-Spectrin,
pubmed-meshheading:6374036-Subcellular Fractions
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pubmed:year |
1984
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pubmed:articleTitle |
Chromaffin granule membrane-F-actin interactions and spectrin-like protein of subcellular organelles: a possible relationship.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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