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A Novel Gelsolin Isoform Expressed by Oligodendrocytes in the Central Nervous System
Author(s) -
Vouyiouklis Demetrius A.,
Brophy Peter J.
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.69030995.x
Subject(s) - gelsolin , gene isoform , cytoplasm , biology , microbiology and biotechnology , actin , alternative splicing , actin cytoskeleton , gene , cytoskeleton , biochemistry , cell
Two isoforms of the Ca 2+ ‐sensitive, actin‐binding protein gelsolin have been identified thus far; one is an intracellular protein, cytoplasmic gelsolin, and the other is a secretory protein called plasma gelsolin. Gelsolin expression in the mammalian CNS appears to be localized mainly to oligodendrocytes where it is presumed that the cytoplasmic isoform predominates. Here, we show that oligodendrocytes not only contain cytoplasmic gelsolin, but they also express a novel gelsolin isoform that we have named gelsolin‐3. Cytoplasmic gelsolin, plasma gelsolin, and gelsolin‐3 arise by alternative splicing from the same gene. The N‐terminal amino acid sequence unique to gelsolin‐3 is shown to be encoded by a single exon in a region previously thought to be an intron in the human gelsolin gene. In situ hybridization analysis confirmed that gelsolin‐3 mRNA is localized primarily to oligodendrocytes in rat brain. In other tissues, gelsolin‐3 shows a more restricted pattern of expression than cytoplasmic gelsolin. These data support the view that the gelsolin isoforms have differential roles in the regulation of the actin cytoskeleton.