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DEVELOPMENT AND TISSUE PLASTICITY
Departments of 1Orthopaedics, 2Physiology and Biophysics, and 3Otolaryngology, College of Medicine, University of California, Irvine, California 92697
Submitted 21 October 2002 ; accepted in final form 5 May 2003
Previous studies have reported the existence of skeletal muscle fibers that
coexpress multiple myosin heavy chain isoforms. These surveys have usually
been limited to studying the polymorphic profiles of skeletal muscle fibers
from a limited number of muscles (i.e., usually <4). Additionally, few
studies have considered the functional implications of polymorphism. Hence,
the primary objective of this study was to survey a relatively large number of
rat skeletal muscle/muscle regions and muscle fibers (n
5,000) to
test the hypothesis that polymorphic fibers represent a larger fraction of the
total pool of fibers than do so-called monomorphic fibers, which express only
one myosin heavy chain isoform. Additionally, we used Hill's statistical model
of the force-velocity relationship to differentiate the functional
consequences of single-fiber myosin heavy chain isoform distributions found in
these muscles. The results demonstrate that most muscles and regions of rodent
skeletal muscles contain large proportions of polymorphic fibers, with the
exception of muscles such as the slow soleus muscle and white regions of fast
muscles. Several muscles were also found to have polymorphic profiles that are
not consistent with the I
IIAIIXIIB scheme of muscle
plasticity. For instance, it was found that the diaphragm muscle normally
contains I/IIX fibers. Functionally, the high degree of polymorphism may
1) represent a strategy for producing a spectrum of contractile
properties that far exceeds that simply defined by the presence of four myosin
heavy chain isoforms and 2) result in relatively small differences in
function as defined by the force-velocity relationship.
isoform; hybrid fiber; polymorphic fiber; force-velocity relationship; fiber type
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