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Decrease of heat shock protein 27/28 with heat stress in HTLV-I-transformed cells
D Sun1, J J Sauk, D W Archibald
1Department of Pathology, School of Dentistry, University of Maryland, Baltimore 21201.
We have previously reported an increase of human T-lymphotropic leukemia/lymphoma virus type I (HTLV-I) replication after heat treatment of MT-2 cells, an HTLV-I-transformed human lymphoid cell line. In this study, we investigated the effect of heat stress on the expression of Hsp27/28 in MT-2 cells. In contrast with previous studies of other cell types, a decrease of Hsp27/28 expression in MT-2 cells and an increase of Hsp70 family proteins in both MT-2 and uninfected lymphoid CEM cells were found following heat treatment at 42 degrees C. Furthermore, heat treatment resulted in an early rapid increase in the phosphorylated form of Hsp27/28 in both MT-2 and CEM cells. The results suggest that early post-translational phosphorylation of HSP27/28 could be a determinant of the ability of MT-2 cells to survive hyperthermia.
We have previously reported an increase of human T-lymphotropic leukemia/lymphoma virus type I (HTLV-I) replication after heat treatment of MT-2 cells, an HTLV-I-transformed human lymphoid cell line. In this study, we investigated the effect of heat stress on the expression of Hsp27/28 in MT-2 cells. In contrast with previous studies of other cell types, a decrease of Hsp27/28 expression in MT-2 cells and an increase of Hsp70 family proteins in both MT-2 and uninfected lymphoid CEM cells were found following heat treatment at 42 degrees C. Furthermore, heat treatment resulted in an early rapid increase in the phosphorylated form of Hsp27/28 in both MT-2 and CEM cells. The results suggest that early post-translational phosphorylation of HSP27/28 could be a determinant of the ability of MT-2 cells to survive hyperthermia.