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   <subfield code="a">Length-dependent effects of osmotic compression on skinned rabbit psoas muscle fibers</subfield>
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   <subfield code="a">The goal of this study was to characterize the interrelationship between sarcomere length and interfilament spacing in the control of Ca2+ sensitivity in skinned rabbit psoas muscle fibers. Measurements were made at sarcomere lengths 2.0, 2.7 and 3.4 μm. At 2.7 μm the fiber width was reduced by 17% relative to that at 2.0 μm and the pCa50 for force development was increased by ∼0.3 pCa units. In the presence of 5% Dextran T-500 the fiber width at sarcomere length 2.0 μm was also decreased by 17% and the Ca2+ sensitivity was increased to the same value as at 2.7 μm. In contrast, at sarcomere length 2.7 μm the addition of as much as 10% Dextran T-500 had no effect on Ca2+ sensitivity. At sarcomere length 3.4 μm there was an additional 7% compression and the Ca2+ sensitivity was increased slightly (∼0.1 pCa units) relative to that at 2.7 μm. However at 3.4 μm the addition of 5% Dextran T-500 caused the Ca2+ sensitivity to decrease to the level seen at 2.0 μm. Given that the skinning process causes a swelling of the filament lattice it is evident that the relationship between sarcomere length and Ca2+ sensitivity observed in skinned fibers may not always be applicable to intact fibers. These data are consistent with measurements of Ca2+ in intact fibers which indicate that there might be a decline in Ca2+ sensitivity at long sarcomere lengths.</subfield>
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   <subfield code="t">Journal of Muscle Research &amp; Cell Motility</subfield>
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