EFFECTS OF ANTISENSE HSP27 GENE EXPRESSION IN OSTEOSARCOMA CELLS

摘要

Several lines of evidence support the concept that extracellular signals acting on cell growth and differentiation, including those involving integrin receptors, might be transduced by an organized cy-toskeleton (8,16,17,19,21,22). Among the controlling elements possibly implicated in these coordinated processes, the small heat shock protein hsp 27/28 (and its murine analog hsp25) deserves particular interest, in view of its pivotal position at the point of convergence of the different metabolic andregulatory pathways implicated. A series of data have indeed clearly established that hsp27 plays a role in the control of actin polymerization, binding the unphosphorylated form of hsp27 to actin resulting in an inhibition of actin polymerization that is suppressed when the heat shock protein is phosphor-ylated (1,13,15).