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Journal of Neuroscience, Vol 14, 1038-1052, Copyright © 1994 by Society for Neuroscience
Localization and characterization of gelsolin in nervous tissues: gelsolin is specifically enriched in myelin-forming cells
J Tanaka and K Sobue
Department of Neurochemistry and Neuropharmacology, Osaka University Medical School, Japan.
Gelsolin is a Ca(2+)-sensitive actin filament-severing protein. To
elucidate the role of gelsolin in nervous tissues, we have investigated
localization and expression of gelsolin in rat CNS and PNS using
biochemical and morphological methods with a polyclonal antibody against
the COOH-terminal fragment of plasma gelsolin. Immunohistochemical study
showed that gelsolin was specifically enriched in oligodendrocytes and
Schwann cells, and was also detected in myelin sheath, especially around
the Ranvier's nodes. The immunohistochemical stainings using indirect
immunofluorescence, avidin- biotin-peroxidase complex, and immunogold
methods were carefully confirmed by immunoblotting against the tissue
homogenates. The expressional changes of gelsolin in developing brain were
investigated. The protein was detectable in newborn rat brain; however, it
began to increase at 8-10 d after birth and reached maximal at 20-30 d when
myelinogenesis actively occurred. After this period, the protein decreased
gradually, although myelin basic protein was increasing until 6 months
after birth. The immunostaining of gelsolin in Schwann cells was enhanced
upon regeneration of injured sciatic nerves by freezing. Immunoelectron
microscopy revealed that gelsolin was present not only in the cytoplasm but
also in compact myelin. Following solubilization by detergents, gelsolin in
the myelin fraction could be purified using anion exchange and blue
Sepharose column chromatographies. The purified protein possessed a
Ca(2+)-dependent severing activity against actin filaments similar to that
of cytoplasmic and plasma gelsolin. These data strongly suggest that
gelsolin in nervous tissues might be involved in lamellipodial movement to
wrap axons of myelin-forming cells by modulating actin polymerization.
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