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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2000-8-15
pubmed:abstractText
To determine whether the concentrations of calcium-binding proteins present in some neurons and sensory cells are sufficient to influence presynaptic calcium signaling, we studied the predominant calcium-binding protein in a class of sensory hair cells in the frog ear. Based on antibody affinity and molecular weight, we identified this protein as calretinin. We measured its cytoplasmic concentration to be approximately 1.2 mM, sufficient to bind approximately 6 mM Ca2+. Calcium signaling was altered when the diffusible cytoplasmic components were replaced by an intracellular solution lacking any fast calcium buffer, and was restored by the addition of 1.2 mM exogenous calretinin to the intracellular solution. We conclude that calretinin, when present at millimolar concentration, can serve as a diffusionally mobile calcium buffer/transporter capable of regulating calcium signaling over nanometer distances at presynaptic sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1097-6256
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
786-90
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Calretinin modifies presynaptic calcium signaling in frog saccular hair cells.
pubmed:affiliation
Institute of Neuroscience, University of Oregon, Eugene, Oregon 97403, USA. edmonds@ucla.edu
pubmed:publicationType
Journal Article