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Rat extraocular muscle

Rat extraocular muscle Multiply-innervated fibers from rat superior oblique extraocular muscle were followed in sequential serial sections using histochemistry. Sudan black and adenosine-triphosphase (ATPase) histochemical staining reactions were used to identify these fibers in the muscle's global layer and orbital surface layer. Regional differences in ATPase staining occurred along the length of multiply-innervated fibers from the orbital surface layer. In their middle third where these fibers appear ‘morphologically-fast’ and contain endplatelike endings, they were found to exhibit a dual ATPase activity. In their distal third where they appear ‘morphologically-slow’ and contain simple, superficial endings, they had an alkaline-labile and acid-stabile ATPase activity profile. In contrast, the multiply-innervated fibers of the global layer exhibited a homogeneous ATPase activity, i.e., alkaline-labile and acid-stabile pattern. This histochemical homogeneity parallels their uniform morphologically-slow profile. These fibers contain only multiple superficial endings. It would appear that the histochemical and ultrastructural profile of a fiber is dependent upon the type and location of the motor innervation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Histochemistry and Cell Biology Springer Journals

Rat extraocular muscle

Pachter, B.
Histochemistry and Cell Biology , Volume 80 (6) – Oct 14, 2004
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References (19)

Publisher
Springer Journals
Copyright
Copyright © 1984 by Springer-Verlag
Subject
Biomedicine; Biomedicine, general; Cell Biology; Biochemistry, general; Developmental Biology
ISSN
0948-6143
eISSN
1432-119X
DOI
10.1007/BF00553713
Publisher site
See Article on Publisher Site

Abstract

Multiply-innervated fibers from rat superior oblique extraocular muscle were followed in sequential serial sections using histochemistry. Sudan black and adenosine-triphosphase (ATPase) histochemical staining reactions were used to identify these fibers in the muscle's global layer and orbital surface layer. Regional differences in ATPase staining occurred along the length of multiply-innervated fibers from the orbital surface layer. In their middle third where these fibers appear ‘morphologically-fast’ and contain endplatelike endings, they were found to exhibit a dual ATPase activity. In their distal third where they appear ‘morphologically-slow’ and contain simple, superficial endings, they had an alkaline-labile and acid-stabile ATPase activity profile. In contrast, the multiply-innervated fibers of the global layer exhibited a homogeneous ATPase activity, i.e., alkaline-labile and acid-stabile pattern. This histochemical homogeneity parallels their uniform morphologically-slow profile. These fibers contain only multiple superficial endings. It would appear that the histochemical and ultrastructural profile of a fiber is dependent upon the type and location of the motor innervation.

Journal

Histochemistry and Cell Biology – Springer Journals

Published: Oct 14, 2004

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