Myosin-like aggregates in trypsin-treated smooth muscle cells.

Segments of the lower small intestine of the toad Bufo marinus were excised and soaked for approximately 2 hr in Ringer's solution (pH 7.4 or 7.8) containing crystalline trypsin and then fixed for electron microscopy at approximately the same pH. Thin sections of the tunica muscularis of these specimens show smooth muscle cells ranging in appearance from severely damaged at one extreme to apparently unaffected at the other. Among these are cells at intermediate stages, including some which exhibit large and conspicuous populations of thick filaments closely resembling artificially prepared aggregates of smooth muscle myosin. The thick filaments have the form of tactoids approximately 250-300 A in diameter in their middle regions and are approximately 0.5-1.0 micro in length. In some preparations they also display an axial periodicity approximating 143 A. They are usually randomly oriented and segregated from the thin filaments, which tend to form closely packed, virtually crystalline bundles at the periphery of these cells. "Dense bodies" are absent from cells showing these changes. The simplest interpretation of these data is that smooth muscle myosin normally exists among the actin filaments in a relatively disaggregated state and that trypsin induces aggregation by altering the conformation of the myosin molecule. Alternatively, trypsin may act indirectly through an effect on some other smooth muscle protein which normally forms a stable complex with relatively disaggregated myosin.