Immunocytochemistry of the muscle cell cytoskeleton

Abstract

The muscle cell cytoskeleton is defined for this review as any structure or protein primarily involved in linking or connecting protein filaments to each other or to anchoring sites. In striated muscle, the M line connects thick filaments at their centers to adjacent thick filaments. Titin forms elastic filaments that extend from the M line to the Z line and may contribute to the resting tension properties of striated muscle. Nebulin forms inextensible filaments in skeletal muscle that are closely associated with thin filaments and that may provide a length template for thin filaments. Z lines anchor thin filaments from adjacent sarcomeres via the actin-binding function of alpha-actinin. Other proteins located at the Z line include Cap Z, Z-nin, Z protein, and zeugmatin. Intermediate filaments connect myofibrils to each other at the level of the Z line and to the sarcolemma at the Z- and possibly the M-line levels. Immunolocalization has identified the adhesion plaque proteins spectrin, vinculin, dystrophin, ankyrin, and talin at subsarcolemmal sites where they may be involved with filament attachment. Smooth muscle cell cytoskeletons are believed to include membrane associated dense bodies (MADBs), intermediate filaments, cytoplasmic dense bodies (CDBs), and perhaps a subset of actin filaments. MADBs contain a menu of attachment plaque proteins and anchor both thin filaments and intermediate filaments to the sarcolemma. CDBs are intracellular analogs of striated muscle Z lines and anchor thin filaments and intermediate filaments.