The histochemical profiles of fast fiber types IIB, IID, and IIA in skeletal muscles of mouse, rat, and rabbit.

Abstract

This study characterized histochemically three fast fiber types (IIB, ID, 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 muscles. Fiber type delineation is based on various methods for mATPase staining 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-incubation provided best and most reproducible results. In addition to their different mATPase stabilities, the three fast fiber types M e r with regard to their oxidative capacities and aoss-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 predominant fast fiber popdation in extensor digitorum longus, psoas, and tibialis anterior muscles. As judged from histochemistry, these muscles 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 other hand, IIB fibers are numerous in rabbit adductor magnus, gastrocnemius, and vastus lateralis muscles. Similarly, appreciable amounts of myosin heavy chai n HCIII, are found in the three latter muscles of rabbit.

Evidence for Three Fast Myosin Heavy Chain Isoforms in Type II Skeletal Muscle Fibers in the Adult Llama (Lama glama)

“…Only three major fiber types [one slow-twitch (Type I) and two fast-twitch (Types IIA and IIB)] could be distinguished with these traditional methods in mature skeletal muscle of the majority of mammals (Matoba et al 1985). By applying combined and more refined mATPase histochemical methods, three pure fast Type II fibers can be delineated in skeletal muscle of a number of rodents (Gorza 1990;Rowlerson 1991;Hämäläinen and Pette 1993). The identification of three fast-twitch fiber populations can also be obtained in skeletal muscle of a large mammal such as the llama with the simultaneous application of two different mATPase histochemical stainings ( Figure 2C).…”

“…In adult skeletal muscle of certain small species of mammals (i.e., rat, mouse, and rabbit), three fast MHC isoforms, termed IIA, IIX, or IID (henceforth IIX), and IIB, have been identified (Bär and Pette 1988;Schiaffino et al 1989). The differential distribution of these MHCs defines three pure fast fiber types containing a single MHC isoform (IIA, IIX, and IIB) and some hybrid fiber population containing two or three fast MHCs (Gorza 1990;Hämäläinen and Pette 1993). The relative abundance of the fast MHC IIB isoform decreases among mammals with increasing body size and is not expressed in humans (Smerdu et al 1994), carnivores (Talmadge et al 1996), ruminants (Tanabe et al 1998), and horses .…”

TnIfast IRE enhancer: Multistep developmental regulation during skeletal muscle fiber type differentiation

“…Fibers that did not react with any of the antibodies were typed as IIX. In addition, myosin ATPase histochemistry was performed after preincubation at pH 4.6 according to the method of Brooke and Kaiser (1970), as modified for visualization of IIX fibers in the mouse (Hamalainen and Pette, 1993). This procedure gave a positive signal for IIX fibers and was also useful for interpreting occasional fibers expressing more than one myosin isoform.…”

Cytoarchitectural and metabolic adaptations in muscles with mitochondrial and cytosolic creatine kinase deficiencies

“…Details of procedures used in the morphometric and qualitative aspects of mitochondrial contacts sites will be published elsewhere (Verdoodt et al submitted). For analysis of myosin heavy chain (MHC) composition, crude extracts from individual muscles from a wild-type, ScCKmit [-/-], M-CK [-/-], and CK [-/-] double mutant animals were prepared and electrophoretic profiles on gradient polyacrylamide gels were evaluated as described [68].…”