Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines.

摘要: Abstract A rabbit antiserum was prepared against the C-terminal peptide of 21 amino acids from human heat shock protein hsp70. These antibodies were shown to be specific for this highly inducible (72 kilodaltons [kDa] in rat cells), and a moderately inducible, constitutively expressed protein, hsc70 (74 kDa). In six independently derived cell lines transformed by murine cDNA-genomic hybrid clone p53 plus an activated Ha-ras gene, elevated levels detected immunoprecipitation using murine-specific anti-p53 monoclonal antibodies. all cases, hsc70, but not hsp70, coimmunoprecipitated with protein. Similarly, p53. Western blot (immunoblot) analysis demonstrated that proteins did share detectable antigenic epitopes. The results provide clear immunological evidence association single p53-plus-ras-transformed lines. A cDNA clone, p11-4, failed produce clonable foci primary cells transfected p11-4 Ha-ras. mutant SVKH215, yielded 2- 35-fold increase number produced after transfection SVKH215 When cloned, 87.5% these encodes binds preferentially 70 kDa compared binding parental gene product. data suggest p53-hsc70 complex could have functional significance cells.