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Force-calcium relationship depends on myosin heavy chain and troponin isoforms in rat diaphragm muscle fibers
Ist Teil von
Journal of applied physiology (1985), 1999-11, Vol.87 (5), p.1894-1900
Ort / Verlag
Bethesda, MD: Am Physiological Soc
Erscheinungsjahr
1999
Quelle
MEDLINE
Beschreibungen/Notizen
Departments of Anesthesiology and Physiology and Biophysics,
Mayo Clinic and Foundation, Rochester, Minnesota 55905
The present study examined
Ca 2+ sensitivity of diaphragm
muscle (Dia m ) fibers expressing
different myosin heavy chain (MHC) isoforms. We hypothesized that
Dia m fibers expressing the
MHC slow isoform have greater
Ca 2+ sensitivity than fibers
expressing fast MHC isoforms and that this fiber-type difference in
Ca 2+ sensitivity reflects the
isoform composition of the troponin (Tn) complex (TnC, TnT, and TnI).
Studies were performed in single Triton-X-permeabilized
Dia m fibers. The
Ca 2+ concentration at which 50%
maximal force was generated
(pCa 50 ) was determined for each
fiber. SDS-PAGE and Western analyses were used to determine the MHC and
Tn isoform composition of single fibers. The
pCa 50 for
Dia m fibers expressing
MHC slow was significantly greater
than that of fibers expressing fast MHC isoforms, and this greater
Ca 2+ sensitivity was associated
with expression of slow isoforms of the Tn complex. However,
some Dia m fibers expressing
MHC slow contained the
fast TnC isoform. These results suggest that the combination of TnT,
TnI, and TnC isoforms may determine
Ca 2+ sensitivity in
Dia m fibers.
myosin heavy chain; troponin; diaphragm muscle; single fibers; calcium sensitivity; cooperativity