N. Hamalainen et D. Pette, THE HISTOCHEMICAL PROFILES OF FAST FIBER TYPE-IIB, TYPE-IID, AND TYPE-IIA IN SKELETAL-MUSCLES OF MOUSE, RAT, AND RABBIT, The Journal of histochemistry and cytochemistry, 41(5), 1993, pp. 733-743
This study characterized histochemically three fast fiber types (IIB,
IID, IIA) in skeletal muscles of mouse, rat, and rabbit, with special
reference to fiber types IIB and IID. The results are complemented by
biochemical analyses of myosin heavy chain composition in these muscle
s. Fiber type delineation is based on various methods for mATPase stai
ning with preincubations and assays under different conditions. In rat
and mouse, IIB and IID fibers can be best distinguished according to
their different mATPase stabilities towards formaldehyde and alkaline
pH. In rabbit, the method of Matoba and Gollnick using acid pre-incuba
tion provided best and most reproducible results. In addition to their
different mATPase stabilities, the three fast fiber types differ with
regard to their oxidative capacities and cross-sectional fiber areas
in the three species. In general, Type IIB fibers are the largest and
least oxidative, Type IIA fibers the smallest and most oxidative, and
Type IID fibers intermediate. In rabbit, Type IID fibers are the predo
minant fast fiber population in extensor digitorum longus, psoas, and
tibialis anterior muscles. As judged from histochemistry, these muscle
s of rabbit do not contain pure Type IIB fibers. This is in accordance
with biochemical results that show the HCIId to form the majority of
the myosin heavy chain complement expressed in these muscles. On the o
ther hand, IIB fibers are numerous in rabbit adductor magnus, gastrocn
emius, and vastus lateralis muscles. Similarly, appreciable amounts of
myosin heavy chain HCIIb are found in the three latter muscles of rab
bit.