Linked Life Data

2159516

Source:http://linkedlifedata.com/resource/pubmed/id/2159516

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pubmed-article:2159516pubmed:abstractTextIt has been previously recognized that a number of protocols may cause breakage of the triad junction and separation of the constituent organelles of skeletal muscle. We now describe a fraction of triad junctions which is refractory to the known protocols for disruption. Triads were passed through a French press and the dissociated organelles were separated on a sucrose density gradient, which was assayed for PN200-110, ouabain and ryanodine binding. Ryanodine binding showed a single peak at the density of heavy terminal cisternae. On the other hand, the PN200-110 and ouabain, which are external membrane ligands, bound in two peaks: one at the free transverse tubule region and the other at the light terminal cisternae. Similarly, a two peak pattern of PN200-110 and ouabain binding was observed when triad junctions were broken by the Ca2(+)-dependent protease, calpain, which selectively hydrolyzes the junctional foot protein. The light terminal cisternae vesicles were subjected to three different procedures of junctional breakage: French press, hypertonic salt treatment, and protease digestion using calpain or trypsin. The treated membranes were then centrifuged on density gradients. Only extensive trypsin digestion caused a partial shift of ouabain activity into the free transverse tubule region. These observations suggest that the triads are a composite mixture of breakage susceptible, "weak," and breakage resistant, "strong," triads. Scatchard analysis of PN200-110 suggests that the transverse tubules of strong triads contain a relatively high number of dihydropyridine receptors compared to those of weak triads. Thin section electron microscopic images of the strong triads comparable to those of intact muscle are presented.lld:pubmed
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pubmed-article:2159516pubmed:authorpubmed-author:BrandtN RNRlld:pubmed
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pubmed-article:2159516pubmed:pagination221-35lld:pubmed
pubmed-article:2159516pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2159516pubmed:articleTitleIdentification of a new subpopulation of triad junctions isolated from skeletal muscle; morphological correlations with intact muscle.lld:pubmed
pubmed-article:2159516pubmed:affiliationDepartment of Pharmacology, University of Miami, School of Medicine, Florida 33101.lld:pubmed
pubmed-article:2159516pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:2159516pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:2159516pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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