Linked Life Data

10419512

Source:http://linkedlifedata.com/resource/pubmed/id/10419512

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1999-8-19
pubmed:abstractText
The dihydropyridine receptor (DHPR) in the skeletal muscle plasmalemma functions as both voltage-gated Ca(2+) channel and voltage sensor for excitation-contraction (EC) coupling. As voltage sensor, the DHPR regulates intracellular Ca(2+) release via the skeletal isoform of the ryanodine receptor (RyR-1). Interaction with RyR-1 also feeds back to increase the Ca(2+) current mediated by the DHPR. To identify regions of the DHPR important for receiving this signal from RyR-1, we expressed in dysgenic myotubes a chimera (SkLC) having skeletal (Sk) DHPR sequence except for a cardiac (C) II-III loop (L). Tagging with green fluorescent protein (GFP) enabled identification of expressing myotubes. Dysgenic myotubes expressing GFP-SkLC or SkLC lacked EC coupling and had very small Ca(2+) currents. Introducing a short skeletal segment (alpha(1S) residues 720-765) into the cardiac II-III loop (replacing alpha(1C) residues 851-896) of GFP-SkLC restored both EC coupling and Ca(2+) current densities like those of the wild type skeletal DHPR. This 46-amino acid stretch of skeletal sequence was recently shown to be capable of transferring strong, skeletal-type EC coupling to an otherwise cardiac DHPR (Nakai, J., Tanabe, T., Konno, T., Adams, B., and Beam, K.G. (1998) J. Biol. Chem. 273, 24983-24986). Thus, this segment of the skeletal II-III loop contains a motif required for both skeletal-type EC coupling and RyR-1-mediated enhancement of Ca(2+) current.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21913-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10419512-Amino Acid Sequence, pubmed-meshheading:10419512-Animals, pubmed-meshheading:10419512-Animals, Newborn, pubmed-meshheading:10419512-Calcium Channels, pubmed-meshheading:10419512-Calcium Channels, L-Type, pubmed-meshheading:10419512-Cells, Cultured, pubmed-meshheading:10419512-Green Fluorescent Proteins, pubmed-meshheading:10419512-Heart, pubmed-meshheading:10419512-Luminescent Proteins, pubmed-meshheading:10419512-Membrane Potentials, pubmed-meshheading:10419512-Mice, pubmed-meshheading:10419512-Mice, Mutant Strains, pubmed-meshheading:10419512-Molecular Sequence Data, pubmed-meshheading:10419512-Muscle, Skeletal, pubmed-meshheading:10419512-Patch-Clamp Techniques, pubmed-meshheading:10419512-Protein Structure, Secondary, pubmed-meshheading:10419512-Receptor Cross-Talk, pubmed-meshheading:10419512-Recombinant Fusion Proteins, pubmed-meshheading:10419512-Restriction Mapping, pubmed-meshheading:10419512-Ryanodine Receptor Calcium Release Channel, pubmed-meshheading:10419512-Signal Transduction
pubmed:year
1999
pubmed:articleTitle
The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the Bi-directional coupling with the ryanodine receptor.
pubmed:affiliation
Department of Anatomy and Neurobiology College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80523, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't