期刊
BIOPHYSICAL JOURNAL
卷 88, 期 2, 页码 1156-1165出版社
CELL PRESS
DOI: 10.1529/biophysj.104.042630
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Intermediate. laments composed of desmin interlink Z-disks and sarcolemma in skeletal muscle. Depletion of desmin results in lower active stress of smooth, cardiac, and skeletal muscles. Structural functions of intermediate. laments in fast ( psoas) and slow ( soleus) skeletal muscle were examined using x-ray diffraction on permeabilized muscle from desmin-deficient mice ( Des -/-) and controls (Des+/+). To examine lateral compliance of sarcomeres and cells,. lament distances and fiber width were measured during osmotic compression with dextran. Equatorial spacing (x-ray diffraction) of contractile. laments was wider in soleus Des -/- muscle compared to Des+/+, showing that desmin is important for maintaining lattice structure. Osmotic lattice compression was similar in Des -/- and Des+/+. In width measurements of single fibers and bundles, Des -/- soleus were more compressed by dextran compared to Des+/+, showing that intermediate. laments contribute to whole-cell compliance. For psoas fibers, both. lament distance and cell compliance were similar in Des -/- and Des+/+. We conclude that desmin is important for stabilizing sarcomeres and maintaining cell compliance in slow skeletal muscle. Wider. lament spacing in Des -/- soleus cannot, however, explain the lower active stress, but might influence resistance to stretch, possibly minimizing stretch-induced cell injury.
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