Morphological and functional characterization of the endosarcomeric elastic filament.

The elastic filament was studied in chemically skinned fibers from rabbit psoas muscle by electron microscopy and resting tension measurements. Extraction of skinned fibers with 40 mM sodium pyrophosphate caused a selective removal of about two-thirds of the thick filaments and formed a gap between the remaining portion of the A band and the I band. Very thin filaments were seen in the gap and were decorated by anti-titin antibody. The resting tension of these fibers was comparable to that of unextracted control fibers. When the M band was completely extracted by a solution containing 0.6 M NaCl, the resting tension completely disappeared at sarcomere lengths from 2.8 to approximately 3.4 microns. These results suggest that the elastic force of short sarcomeres is endowed in the titin filaments and that these filaments are anchored to some structures of the Z and M lines. Other filaments were found in the gap between the two I bands of NaCl-extracted sarcomeres. These filaments differed from titin filaments by a larger diameter and the anchoring points. They may represent the sarcomeric structures responsible for the resting tension of extracted fibers stretched at sarcomere lengths longer than 3.4 microns.