Details

Autor(en) / Beteiligte

• Bönnemann, C.G
• Thompson, T.G
• van der Ven, P.F.M
• Goebel, H.H
• Warlo, I
• Vollmers, B
• Reimann, J
• Herms, J
• Gautel, M
• Takada, F
• Beggs, A.H
• Fürst, D.O
• Kunkel, L.M
• Hanefeld, F
• Schröder, R

Titel

Filamin C accumulation is a strong but nonspecific immunohistochemical marker of core formation in muscle

Ist Teil von

• Journal of the neurological sciences, 2003-01, Vol.206 (1), p.71-78

Ort / Verlag

Shannon: Elsevier B.V

Erscheinungsjahr

2003

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Filamin C is the muscle isoform of a group of large actin-crosslinking proteins. On the one hand, filamin C is associated with the Z-disk of the myofibrillar apparatus and binds to myotilin; on the other hand, it interacts with the sarcoglycan complex at the sarcolemma. Filamin C may be involved in reorganizing the cytoskeleton in response to signalling events and in muscle it may, in addition, fulfill structural functions at the Z-disk. An examination of biopsies from patients with multi-minicore myopathy, central core myopathy and neurogenic target fibers with core-like target formations (TF) revealed strong reactivity of all the cores and target formations with two different anti-filamin C antibodies. In all three conditions, the immunoreactivity in the cores for filamin C was considerably stronger than that for desmin. Only for αB-crystallin were comparable levels of immunoreactivity detected. There was no difference in intensity for filamin C between the three pathological conditions. Thus, filamin C along with αB-crystallin is a strong and robust, but nonspecific marker of core formation. The reason why filamin C accumulates in cores is unclear at present, but we postulate that it may be critically involved in the chain of events eventually leading to myofibrillar degeneration.