The time-course of disappearance of slow-cardiac calsequestrin (CS) and that of appearance of the skeletal CS isoform were investigated in developing fast-twitch skeletal muscle of the rabbit between postnatal days 1 and 60, along with changes in density of the ryanodine receptor (RyR)/Ca2+ release channel. Western blot data on skeletal muscle membranes, purification of two CS isoforms by phenyl-Sepharose chromatography, and their immunolocalization in muscle fibres, all show that both CS isoforms are coexpressed in neonatal muscles. Our results, at the protein level, indicate that the turning off of synthesis of cardiac CS and its total disappearance from fast-twitch fibres take place at critical periods between two and four weeks postnata...
Calsequestrin (CS) is the major Ca2+-binding protein in the sarcoplasmic reticulum (SR) with a dual ...
The expression pattern of the RyR3 isoform of Ca2+ release channels was analysed by Western blot in ...
AbstractAlthough all muscle cells generate contractile forces by means of organized filament systems...
The time-course of disappearance of slow-cardiac calsequestrin (CS) and that of appearance of the sk...
The cardiac and fast-twitch skeletal muscle forms of the Ca2+-binding protein calsequestrin (CS) are...
The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+...
AbstractThe cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capac...
The postnatal differentiation of sarcoplasmic reticulum (SR) of rabbit skeletal muscles (the slow-tw...
As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 k...
Calsequestrin (CS), the major Ca(2+)-binding protein in the sarcoplasmic reticulum (SR), is thought ...
Early postnatal changes (4-5 days to 15 days after birth) in the biochemical composition of microsom...
Calsequestrin is glycosylated and phosphorylated during its transit to its final destination in the ...
AbstractLinkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine recep...
We have investigated high-affinity ryanodine-binding sites in membrane preparations from representat...
This study investigates the functional role of calsequestrin 2 (CASQ2) in both fast-twitch and slow-...
Calsequestrin (CS) is the major Ca2+-binding protein in the sarcoplasmic reticulum (SR) with a dual ...
The expression pattern of the RyR3 isoform of Ca2+ release channels was analysed by Western blot in ...
AbstractAlthough all muscle cells generate contractile forces by means of organized filament systems...
The time-course of disappearance of slow-cardiac calsequestrin (CS) and that of appearance of the sk...
The cardiac and fast-twitch skeletal muscle forms of the Ca2+-binding protein calsequestrin (CS) are...
The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+...
AbstractThe cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capac...
The postnatal differentiation of sarcoplasmic reticulum (SR) of rabbit skeletal muscles (the slow-tw...
As recently demonstrated by overlay assays using calsequestrin-peroxidase conjugates, the major 63 k...
Calsequestrin (CS), the major Ca(2+)-binding protein in the sarcoplasmic reticulum (SR), is thought ...
Early postnatal changes (4-5 days to 15 days after birth) in the biochemical composition of microsom...
Calsequestrin is glycosylated and phosphorylated during its transit to its final destination in the ...
AbstractLinkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine recep...
We have investigated high-affinity ryanodine-binding sites in membrane preparations from representat...
This study investigates the functional role of calsequestrin 2 (CASQ2) in both fast-twitch and slow-...
Calsequestrin (CS) is the major Ca2+-binding protein in the sarcoplasmic reticulum (SR) with a dual ...
The expression pattern of the RyR3 isoform of Ca2+ release channels was analysed by Western blot in ...
AbstractAlthough all muscle cells generate contractile forces by means of organized filament systems...