Linked Life Data

3892303

Source:http://linkedlifedata.com/resource/pubmed/id/3892303

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6020
pubmed:dateCreated
1985-8-1
pubmed:abstractText
Spectrin is an ubiquitous protein composed of heterodimers with alpha and beta subunits. It was first described in erythrocyte cell membranes (see ref. 1 for review) and subsequently in brain, intestinal brush borders, kidney, liver and adrenals. Brain spectrin (fodrin) alpha-subunit, responsible for actin binding, has a relative molecular mass (Mr) of 240,000, whereas the beta-subunit, involved in membrane attachment, has an Mr of 235,000 (refs 1, 3, 9-13). The membrane of secretory granules from adrenal chromaffin cells membrane of secretory granules from adrenal chromaffin cells increases the viscosity of F-actin solution, and spectrin-like protein is associated with storage granule and plasma membranes. Here, we report the localization of fodrin in secretory cells using monospecific antibodies against the alpha-subunit of fodrin using indirect immunofluorescence. We find that the alpha-subunit forms an intensely stained continuous ring in the subplasmalemmal region of resting chromaffin cells. On stimulation of the cell with nicotine, high potassium or ionophores in the presence of calcium, fodrin forms patches. This aggregation is inhibited by trifluoperazine, hence the entrance of calcium into cells following cell depolarization seems to be the calmodulin-dependent stimulus initiating patch formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:volume
315
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
589-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Reorganization of alpha-fodrin induced by stimulation in secretory cells.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't