title: Calcium sensitivity of residual force enhancement in rabbit skinned fibers.
abstract: Isometric force after active stretch of muscles is higher than the purely isometric force at the corresponding length. This property is termed residual force enhancement. Active force in skeletal muscle depends on calcium attachment characteristics to the regulatory proteins. Passive force has been shown to influence calcium attachment characteristics, specifically the sarcomere length dependence of calcium sensitivity. Since one of the mechanisms proposed to explain residual force enhancement is the increase in passive force that results from engagement of titin upon activation and stretch, our aim was to test if calcium sensitivity of residual force enhancement was different from that of its corresponding purely isometric contraction and if such a difference was related to the molecular spring titin. Force-pCa curves were established in rabbit psoas skinned fibers for reference and residual force-enhanced states at a sarcomere length of 3.0 μm 1) in a titin-intact condition, 2) after treatment with trypsin to partially eliminate titin, and 3) after treatment with trypsin and osmotic compression with dextran T-500 to decrease the lattice spacing in the absence of titin. The force-pCa curves of residual force enhancement were shifted to the left compared with their corresponding controls in titin-intact fibers, indicating increased calcium sensitivity. No difference in calcium sensitivity was observed between reference and residual force-enhanced contractions in trypsin-treated and osmotically compressed trypsin-treated fibers. Furthermore, calcium sensitivity after osmotic compression was lower than that observed for residual force enhancement in titin-intact skinned fibers. These results suggest that titin-based passive force regulates the increase in calcium sensitivity of residual force enhancement by a mechanism other than reduction of the myofilament lattice spacing.
authors: Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Calgary, Alberta, Canada.
authors: V
authors: V
authors: Joumaa
authors: Human Performance Laboratory, Faculty of Kinesiology, University of Calgary, Calgary, Alberta, Canada wherzog@ucalgary.ca.
authors: W
authors: W
authors: Herzog
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D020013:Calcium Signaling / Q000187:drug effects; D064211:Connectin / Q000378:metabolism; D003911:Dextrans / Q000494:pharmacology; D007537:Isometric Contraction / Q000187:drug effects; D018485:Muscle Fibers, Skeletal / Q000187:drug effects / Q000378:metabolism*; D053580:Muscle Strength / Q000187:drug effects; D009210:Myofibrils / Q000378:metabolism; D009997:Osmotic Pressure; D059748:Proteolysis; D016658:Psoas Muscles / Q000187:drug effects / Q000378:metabolism*; D011817:Rabbits; D013997:Time Factors; D014357:Trypsin / Q000494:pharmacology
chemical_list: D064211:Connectin; D003911:Dextrans; D014357:Trypsin; D002118:Calcium
keywords: cross bridges; force-pCa relationship; lattice spacing; pCa50; titin