Calmodulin-binding profiles for nebulin and dystrophin in human skeletal muscle

Nebulin and dystrophin are two high-molecular-mass skeletal muscle proteins that have both been associated with the defective gene in Duchenne muscular dystrophy, although the function of neither protein is known. Other high-molecular-mass, calmodulin-binding proteins have recently been implicated i...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1988-07, Vol.234 (2), p.267-271
Main Authors: Patel, K., Strong, P.N., Dubowitz, V., Dunn, M.J.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Calmodulin
Calmodulin - metabolism
Cell physiology
Duchenne muscular dystrophy
Dystrophin
Fundamental and applied biological sciences. Psychology
Humans
Molecular and cellular biology
Molecular Weight
Muscle contraction
Muscle protein
Muscle Proteins - metabolism
Muscles - metabolism
Muscular Dystrophies - metabolism
Nebulin
PBS, phosphate-buffered saline
PMSF, phenylmethylsulphonyl fluoride
Protein Binding
Reference Values
SDS-PAGE
TCAP buffer, TP buffer containing 1 μM Ca2
TP buffer, PBS containing 0.05% Tween 20
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Nebulin and dystrophin are two high-molecular-mass skeletal muscle proteins that have both been associated with the defective gene in Duchenne muscular dystrophy, although the function of neither protein is known. Other high-molecular-mass, calmodulin-binding proteins have recently been implicated in regulating calcium release from skeletal muscle. Western blots of human skeletal muscle biopsy samples were probed with biotinylated calmodulin; nebulin was identified as a prominent high-molecular-mass calmodulin-binding protein but dystrophin did not bind detectable amounts of biotinylated calmodulin. Dystrophin was absent in a Duchenne muscle biopsy.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80095-4