Fig. 6From: Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere functionPassive tension of skinned normal and myopathy myofibers in the presence of recombinant sHSPs. (a) and (b) Passive sarcomere length-tension relationships of Vastus lateralis muscle fibers from CTRL (left panels) and LGMD2A patients (right panels), before and during incubation with (a) αB-crystallin (αBC) or (b) HSP27 recombinant protein (100 μM). Data points are means ± SEM. The number of fibers measured for each condition (N) is indicated; fibers were obtained from 2 subjects/group. Curves are polynomial fits to the means. *p < 0.05 in Student’s t-test. (c) Localization of endogenous HSP27, αB-crystallin and HSP90 in skinned myofibers after force measurements, monitored by indirect immunofluorescence microscopy. Left panels, CTRL myofibers; right panels, LGMD2A myofibers. (d) Localization of exogenous (6xHIS-tagged) recombinant αB-crystallin, in relation to the PEVK titin epitope (TTN), measured using anti-6xHIS-tag Cy3-conjugated antibodies. Left panels, CTRL myofibers; right panels, LGMD2A myofibers. Insets: Higher-power images of regions-of-interest. Muscle samples were fixed in the stretched state after mechanical measurements and incubated with the respective antibodies. All bars, 5 μmBack to article page