Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy
J. Clin. Invest. Joachim Schessl, et al. 118:904 doi:10.1172/JCI34450 [Go to this article.]

Figure 2
FHL1 localization in muscle from RBM patients. (A) Distribution of FHL1 immunoreactivity in normal muscle (B) FHL1 immunoreactivity prominently decorates the intracytoplasmic inclusions, which are more numerous in patient 1 (arrows). (C) Higher magnification of FHL1-labeled inclusions (arrows) in the biopsy from patient 1 demonstrates their often close relationship with myonuclei (blue, star), confirmed on electron microscopy (D) where the inclusions (arrows) abut a myonucleus (patient 1) or are close by (patient 2; star indicates myonucleus). (E and F) Inclusions colabel for FHL1 and the intermediate filament desmin (E) as well as ubiquitin (F) (patient 1). (G) In fibers without prominent inclusions, FHL1 localizes properly to the contractile apparatus, mainly locating to the I-line and Z disk, which is colabeled with α-actinin (arrows). (H) In fibers with prominent inclusions, FHL1 immunoreactivity at the contractile apparatus in the vicinity of the inclusion is severely reduced. Star denotes inclusion, arrows point to the contractile apparatus with Z disks labeled with α-actinin (which is also associated with the inclusion). The fiber architecture is also severely distorted (patient 2). Scale bars: 10 μm.