Loading…

Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin

Gelsolin, an 82 kDa actin-binding protein, has potent actin filament-severing activity in vitro. To investigate the in vivo function of gelsolin, transgenic gelsolinnull (Gsn−) mice were generated and found to have normal embryonic development and longevity. However, platelet shape changes are decre...

Full description

Saved in:
Bibliographic Details
Published in:Cell 1995-04, Vol.81 (1), p.41-51
Main Authors: Witke, Walter, Sharpe, Arlene H, Hartwig, John H, Azuma, Toshifumi, Stossel, Thomas P, Kwiatkowski, David J
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Gelsolin, an 82 kDa actin-binding protein, has potent actin filament-severing activity in vitro. To investigate the in vivo function of gelsolin, transgenic gelsolinnull (Gsn−) mice were generated and found to have normal embryonic development and longevity. However, platelet shape changes are decreased in Gsn−mice, causing prolonged bleeding times. Neutrophil migration in vivo into peritoneal exudates and in vitro is delayed. Gsn− dermal fibroblasts have excessive actin stress fibers and migrate more slowly than wildtype fibroblasts, but have increased contractility in vitro. These observations establish the requirement of gelsolin for rapid motile responses in cell types involved in stress responses such as hemostasis, inflammation, and wound healing. Neither gelsolin nor other proteins with similar actin filament-severing activity are expressed in early embryonic cells, indicating that this mechanism of actin filament dynamics is not essential for motility during early embryogenesis.
ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(95)90369-0