ISSN:
1573-2657
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Summary The characteristics of the titin filament in the vicinity of the Z-line were investigated using immunoelectron microscopy. We used monoclonal titin antibodies T-11 and T-12 on single fibres of frog skeletal muscle, and on Z-line-extracted fibres. It is well established that the I-band region of titin is elastic. We find, however, that the elastic properties are not uniform. The T-12 epitope, which binds near the Z-line at the N1-line level, hardly changes position relative to the Z-line as the sarcomere is stretched. This demonstrates the functional inextensibility of the N1-Z-line region. After extreme stretch (above 6-μm sarcomere length), this zone finally does elongate; thus, the titin molecule in this region is intrisically elastic. The functional inextensibility seen at shorter sarcomere lengths may, therefore, be a result of binding of titin to the actin filament in the zone near the Z-line. When the Z-line was extracted, the T-12 epitope remained in the same position as in the unextracted fibres; it did not retract from the Z-line. Failure to retract implies that functional anchoring of titin is not exclusive to the Z-line, but includes some site closer to the A-band. Combined with the results of the above-mentioned stretch experiment, this result implies a likely binding of titin to the thin filament either focally at the N1 line or all along the entire N1-Z region. Thus, this region of titin is functionally stiff, but intrinsically elastic.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00121293
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