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

TY - JOUR

T1 - Filamin C accumulation is a strong but nonspecific immunohistochemical marker of core formation in muscle

AU - Bonnemann, C G

AU - Thompson, T G

AU - van der Ven, P F M

AU - Goebel, H H

AU - Warlo, I

AU - Vollmers, B

AU - Reimann, J

AU - Herms, J

AU - Gautel, M

AU - Takada, F

AU - Beggs, A H

AU - Furst, D O

AU - Kunkel, L M

AU - Hanefeld, F

AU - Schroder, R

PY - 2003/1/15

Y1 - 2003/1/15

N2 - 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 alphaB-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 alphaB-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. (C) 2002 Elsevier Science B.V All rights reserved.

AB - 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 alphaB-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 alphaB-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. (C) 2002 Elsevier Science B.V All rights reserved.

UR - http://www.scopus.com/inward/record.url?scp=0037437618&partnerID=8YFLogxK

U2 - 10.1016/S0022-510X(02)00341-6

DO - 10.1016/S0022-510X(02)00341-6

M3 - Article

VL - 206

SP - 71

EP - 78

JO - Journal of the Neurological Sciences

JF - Journal of the Neurological Sciences

IS - 1

ER -