Reptilian skeletal muscle: contractile properties of identified, single fast-twitch and slow fibers from the lizard Dipsosaurus dorsalis

J Exp Zool. 1987 Jun;242(3):283-90. doi: 10.1002/jez.1402420306.

Abstract

Contractile properties and innervation patterns were determined in identified single fibers from the iliofibularis muscle of the desert iguana, Dipsosaurus dorsalis. Single fibers from both the red and white regions of the iliofibularis muscle were dissected along their length under oil and a portion was mounted on transducers for determination of maximum isometric tension (Po) and unloaded shortening velocity (Vmax) using the slack test method. Fibers were chemically skinned and activated by high Ca++. The remaining portion of the muscle fiber was mounted on a glass slide and histochemically treated to demonstrate myosin ATPase activity. Fibers studied functionally could therefore be classified as fast or slow according to their myosin ATPase activity, and they could also be classified metabolically according to the region of the muscle from which they were dissected. Fast-twitch glycolytic (FG) fibers from the white region and fast-twitch oxidative, glycolytic (FOG) and slow fibers from the red region had shortening velocities at 25 degrees C of 7.5, 4.4, and 1.5 l X s-1, respectively. Po did not differ in the three fiber types, averaging 279 kN X m-2. In a second experiment, 10 microns sections were examined every 30 microns through the proximal-most 7.5 mm of the iliofibularis muscle for motor endplates. Sections were stained to demonstrate regions of acetylcholinesterase activity. Fibers with visible endplates were classified in serial sections by histochemical treatment for myosin ATPase and succinic dehydrogenase. All slow fibers examined (n = 22) exhibited multiple endplates, averaging one every 725 microns.(ABSTRACT TRUNCATED AT 250 WORDS)

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / analysis
  • Animals
  • Histocytochemistry
  • Lizards / physiology*
  • Male
  • Muscle Contraction*
  • Muscles / anatomy & histology
  • Muscles / enzymology

Substances

  • Adenosine Triphosphatases