Aw. English et al., DIFFERENT PHENOTYPES AMONG SLOW BETA MYOSIN HEAVY CHAIN-CONTAINING FIBERS OF RABBIT MASSETER MUSCLE - A NOVEL TYPE OF DIVERSITY IN ADULT MUSCLE/, Journal of muscle research and cell motility, 19(5), 1998, pp. 525-535
Differences in the phenotype of different mammalian muscle fibres are
usually attributed to differences in the expression of the product of
different myosin heavy chain (MyHC) genes, which are known as isoforms
. We studied differences in phenotype among fibres containing a single
MyHC isoform (slow/beta) of the masseter muscle of adult rabbits. Fou
r different monoclonal antibodies to slow/beta MyHC were used to stain
serial sections from muscles in males and females. All antibodies rec
ognize a single band on immunoblots and stain the same set of fibres i
n rabbit postcranial muscles. However, differential staining was obser
ved in the masseter muscles. Antibody BA-D5 reacts with the most fibre
s, antibody A4.951 reacts with a subset of these fibres, and antibody
A4.840 reacts with a subset of the A4.951-positive fibres. Antibody S5
8 reacts only with an even smaller subset of fibres. Even though diffe
rential staining using four antibodies might allow for the expression
of as many as 15 different staining patterns, or phenotypes, only four
were observed in >99% of over 30 000 fibres studied. In females, near
ly 40% of the fibres stain exclusively with antibody BA-D5, while in m
ales, fewer than 8% of the fibres express this phenotype. The proporti
ons of fibres of the other phenotypes do not differ so strikingly with
gender. We conclude that an epitope diversity exists among muscle fib
res in the adult rabbit masseter and that it is not necessarily a cons
equence of differences in gene expression. We feel that it is a regula
ted process and that, at least for some phenotypes, this regulation ma
y be hormonally influenced. (C) Chapman & Hall Ltd.