HSP27 regulates fibroblast adhesion, motility, and matrix contraction.
作者： Sahoko Hirano , Eric A. Shelden , Robert R. Gilmont
DOI: 10.1379/471.1
关键词: Extracellular matrix 、 Contraction (grammar) 、 Cell division 、 Cell adhesion 、 Cell biology 、 Transfection 、 Actin 、 Fibroblast 、 Biology 、 Cell culture
摘要: Heat shock protein 27 (HSP27) modulates actin-dependent cell functions in several systems. We hypothesized that HSP27 wound contraction. Stably transfected fibroblast lines overexpress (SS12) or underexpress (AS10) were established, and behaviors related to contraction examined. First, fibroblast-populated collagen lattice (FPCL) was examined because it has been studied as a wound-healing model. In floating FPCL assays, SS12 cells caused increased contraction, whereas AS10 reduced Because matrix is thought be mediated by the tractional force of cells, matrix, elongated faster greater extent contained longer stress fibers than control slower elongate cells. attached dishes more efficiently control, less efficiently. Migration on collagen-coated also enhanced, although did not differ from summary, regulates adhesion, elongation, migration manner dependent level its expression.
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