Abstract
Cell growth is regulated by various sets of intranuclear proteins. The oncosuppressor proteins, pRb and p 53 are the most important of the nolecules that inhibit the cell cycle. It has been reported that hsc 73, one of the members of the 70 kDa heat shock protein family, was associated with pRb and p 53. It was suggested that hsp may be important in the cell growth control mechanism. In this paper, we reported that hsp 90 could interact with cdc 2, which is the major cyclin dependent kinase, in the G2/M phase, although hsp 90 could not interact with pRb. Moreover, a human osteosarcoma cell line, HOS, that was transfected with hsp 90-cDNA showed growth inhibition, when obsereed with 3H-thymidine incorporation. These data indicated that hsp 90 might influence cell growth regulation by interacting with cdc2 kinase.
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