Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-5-5
pubmed:abstractText
Mouse T-lymphoma cells contain a unique type of internal vesicle which bands at the relatively light density of 1.07 g/cc. These vesicles do not contain any detectable Golgi, endoplasmic reticulum, plasma membrane, or lysosomal marker protein activities. Binding of [3H]inositol 1,4,5-trisphosphate (IP3) to these internal vesicles reveals the presence of a single, high affinity class of IP3 receptor with a dissociation constant (Kd) of 1.6 +/- 0.3 nM. Using a panel of monoclonal and polyclonal antibodies against IP3 receptor, we have established that the IP3 receptor (approximately 260 kDa) displays immunological cross-reactivity with the rat brain IP3 receptor. Polymerase chain reaction analysis of first-strand cDNAs from both mouse T-lymphoma cells and rat brain tissues reveals that the IP3 receptor transcript in mouse T-lymphoma cells belongs to the short form (non-neuronal form) and not the long form (neuronal form) detected in rat brain tissue. Scatchard plot analysis shows that high affinity binding occurs between ankyrin and the IP3 receptor with a Kd of 0.2 nM. Most importantly, the binding of ankyrin to the light density vesicles significantly inhibits IP3 binding and IP3-induced internal Ca2+ release. These findings suggest that the cytoskeleton plays a pivotal role in the regulation of IP3 receptor-mediated internal Ca2+ release during lymphocyte activation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7290-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8385102-Animals, pubmed-meshheading:8385102-Ankyrins, pubmed-meshheading:8385102-Base Sequence, pubmed-meshheading:8385102-Calcium, pubmed-meshheading:8385102-Calcium Channels, pubmed-meshheading:8385102-Cytoskeleton, pubmed-meshheading:8385102-DNA, Single-Stranded, pubmed-meshheading:8385102-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8385102-Fluorescent Antibody Technique, pubmed-meshheading:8385102-Humans, pubmed-meshheading:8385102-Inositol 1,4,5-Trisphosphate Receptors, pubmed-meshheading:8385102-Inositol Phosphates, pubmed-meshheading:8385102-Lipid Metabolism, pubmed-meshheading:8385102-Lymphoma, T-Cell, pubmed-meshheading:8385102-Mice, pubmed-meshheading:8385102-Molecular Sequence Data, pubmed-meshheading:8385102-Receptors, Cell Surface, pubmed-meshheading:8385102-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:8385102-Transcription, Genetic, pubmed-meshheading:8385102-Tumor Cells, Cultured
pubmed:year
1993
pubmed:articleTitle
The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells.
pubmed:affiliation
Department of Cell Biology and Anatomy, School of Medicine, University of Miami, Florida 33101.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't