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`Superfast' or masticatory myosin and the evolution of jaw-closing muscles of vertebrates
Department of Physiology and Institute for Biomedical Research, F13, University of Sydney, NSW 2006, Australia
e-mail: joeh{at}physiol.usyd.edu.au
Accepted 13 May 2002
There are four fibre types in mammalian limb muscles, each expressing a
different myosin isoform that finely tunes fibre mechanics and energetics for
locomotion. Functional demands on jaw-closer muscles are complex and varied,
and jaw muscles show considerable phylogenetic plasticity, with a repertoire
for myosin expression that includes limb, developmental, 
-cardiac and
masticatory myosins. Masticatory myosin is a phylogenetically ancient motor
with distinct light chains and heavy chains. It confers high maximal muscle
force and power. It is highly jaw-specific in expression and is found in
several orders of eutherian and marsupial mammals including carnivores,
chiropterans, primates, dasyurids and diprotodonts. In exceptional species
among these orders, masticatory myosin is replaced by some other isoform.
Masticatory myosin is also found in reptiles and fish. It is postulated that
masticatory myosin diverged early during gnathostome evolution and is
expressed in primitive mammals. During mammalian evolution, mastication of
food became important, and in some taxa jaw closers replaced masticatory
myosin with -cardiac, developmental, slow or fast limb myosins to adapt
to the variety of diets and eating habits. This occurred early in some taxa
(rodents, ungulates) and later in others (macropods, lesser panda, humans).
The cellular basis for the uniqueness of jaw-closing muscles lies in their
developmental origin.
Key words: jaw muscle, fibre type, muscle contraction, mastication, myosin isoform, masticatory myosin, evolution, molecular phylogeny
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