Structural domains of the muscle‐tendon junction. 1. The internal lamina and the connecting domain
- 1 December 1983
- journal article
- research article
- Published by Wiley in The Anatomical Record
- Vol. 207 (4), 573-591
- https://doi.org/10.1002/ar.1092070406
Abstract
The force generated within skeletal muscle fibers of vertebrates is transmitted to the tendon at the muscle-tendon junction. Ultrastructural analysis of the murine muscle-tendon junction following a variety of experimental manipulations has produced evidence that the muscle-tendon junction can be described in terms of four principal domains (Trotter and Eberhard, 1983), two of which are discussed in the present report. Each domain is defined by the shape and orientation of its principal components, and by its position with respect to the plasma membrane. The internal lamina is composed of actin filaments, with a center to center spacing of approximately 12 nm, oriented mainly parallel to the principal vector of contractile force, and to the plasma membrane. These filaments are cross-linked into a structural unit, perhaps by the electron-dense structures which are associated with them. The internal lamina is morphologically connected to the external lamina (lamina densa) by a population of fine filaments oriented approximately perpendicular to the principal vector of contractile force. These filaments which constitute the connecting domain, are approximately 2–8 nm in diameter and are at least 50 nm long. They pass through three separate regions: the sarcoplasm between the internal lamina and the plasma membrane; the plasma membrane proper; and the extracellular space between the plasma membrane and the lamina densa. This third region is often referred to as the lamina lucida. These filaments are composed of at least three separate components in series, linked together by noncovalent interactions. The existence of these discrete structural domains implies that each has a different molecular composition and different mechanical properties.This publication has 13 references indexed in Scilit:
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