Demonstration of selective protein complexes of p53 with 73 kDa heat shock cognate protein, but not with 72 kDa heat shock protein in human tumor cells.
It has been demonstrated that p53, especially, mutant p53 (mp53), makes protein complexes with major heat shock proteins hsp72/hsc73. However, there is no direct evidence showing whether hsp72 or hsc73 could bind preferentially to p53. In the present study, using TYKnu human ovarial carcinoma cells and monoclonal antibodies reacting specifically to hsp72/hsc73, we were able to find the selective protein complex formation with p53, presumably mp53, and hsc73, but not in the case of p53 and hsp72. The p53-hsc73 protein complexes dissociate with the addition of ATP, indicating that the dissociation is dependent upon the ATP-hydrolysis. These data suggest that hsc73 rather than hsp72 plays an important role in the yet undefined mechanism of disregulated cell growth control by mp53.
Nihei
T
T
Department of Pathology, Sapporo Medical University School of Medicine, Japan.
Sato
N
N
Takahashi
S
S
Ishikawa
M
M
Sagae
S
S
Kudo
R
R
Kikuchi
K
K
Inoue
A
A
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D002471:Cell Transformation, Neoplastic; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D009363:Neoplasm Proteins / Q000032:analysis / Q000378:metabolism*; D010051:Ovarian Neoplasms / Q000378:metabolism; D011233:Precipitin Tests; D014407:Tumor Cells, Cultured; D016159:Tumor Suppressor Protein p53 / Q000032:analysis / Q000235:genetics / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D006360:Heat-Shock Proteins; D009363:Neoplasm Proteins; D016159:Tumor Suppressor Protein p53; D000255:Adenosine Triphosphate