Abstract
Expression of the p53, the epidermal growth factor receptor (EGFr; c-erbB-1) and c-erbB-2 proteins was studied in 82 patients with primary transitional cell carcinoma of the bladder using an immuno-histochemical method. Strong or moderate staining was found in 18% of tumours for p53 with weaker staining in a further 36% giving a total of 54% of tumours stained for p53. Strong staining was found in 15% of tumours for c-erbB-2 and in 31% for the EGFr. Tumours invading the bladder muscle were significantly more likely to be strongly stained positively for p53 and/or EGFr compared with superficial tumours: only 15% of invasive tumours were stained negatively for both p53 and EGFr. No statistical association was found between p53 and EGFr expression. Weakly positive associations were found between the expression of c-erbB-2 and p53 and between muscle invasive tumours and increased expression of c-erbB-2. Alterations in the expression of p53, c-erbB-1 and c-erbB-2 were found frequently in human transitional cell carcinoma of the urinary bladder and may be of clinical use in defining patient sub-groups of differing prognosis.
Highlights
The protein products of p53, the epidermal growth factor receptor (EGFr) and c-erbB-2 were identified by means of an indirect immunoperoxidase technique using the following monoclonal antibodies
After incubation with primary antibody, sections were washed in tris-phosphate buffered saline (TBS) and covered with peroxidase-conjugated rabbit anti-mouse immuno-globulin (Dakopatts) diluted 1:20 for 30 min
20 further sections were stained with monoclonal antibody PAbi 801 (Oncogene Sciences) which binds to both mutated and normal p53 protein; it is specific for a denaturation resistant epitope between amino acids 32-79
Summary
Frozen sections were cut at 5 ts, air-dried and fixed in acetone for 10 min. The protein products of p53, the EGFr and c-erbB-2 were identified by means of an indirect immunoperoxidase technique using the following monoclonal antibodies. PAb240 recognises an evolutionarily conserved epitope on the p53 protein lying between amino acids 156-214 on murine p53 and it is highly specific for mutated protein as demonstrated by immuno-histochemistry, immuno-precipitation and immuno-blotting techniques (Gannon et al, 1990). It does not bind normal p53 whereas many other monoclonal antibodies to p53 bind both normal and mutated p53. Sections were incubated at room temperature for 30 min with PAb240 as neat supernatant. 20 further sections were stained with monoclonal antibody PAbi 801 (Oncogene Sciences) which binds to both mutated and normal p53 protein; it is specific for a denaturation resistant epitope between amino acids 32-79
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