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B-Crystallin
From the Department of Pathology and the Center for Neurobiology and Behavior, Columbia University College of Physicians and Surgeons, New York, New York
In several neuropathological conditions, 
B-crystallin
and glial fibrillary acidic protein (GFAP) accumulate and form
cytoplasmic inclusions in astrocytes. To explore the pathogenesis of
the inclusions and the possible functions of the accumulated
B-crystallin, GFAP and B-crystallin were overexpressed in
cultured astrocytes by transient transfection. Human GFAP formed
filamentous, cytoplasmic inclusions in mouse
astrocytes, NIH3T3 cells, rat C6 glioma cells,
and human U251 glioma cells. These human GFAP inclusions did not
contain the endogenous vimentin or ß-tubulin, and the
intermediate filament and microtubular networks of the transfected
cells appeared normal. B-crystallin and hsp25 were associated with
the GFAP inclusions. Increasing intracellular B-crystallin levels
using recombinant adenoviruses, either before or after GFAP
inclusions were formed, decreased the number of
inclusion-bearing astrocytes and converted the human GFAP from an
inclusion to a spread, filamentous form. These results suggest
that B-crystallin reorganizes abnormal intermediate filament
aggregates into the normal filamentous network.
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