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  Autoimmune expression of a cytoplasmic protein p60 in mice bearing metastasizing SV40-transformed tumors

Manneck, H., Pfaff, M., & Anderer, F. (1988). Autoimmune expression of a cytoplasmic protein p60 in mice bearing metastasizing SV40-transformed tumors. International Journal of Cancer, 42(6), 906-912. doi:10.1002/ijc.2910420620.

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Manneck, HE1, Author           
Pfaff, M1, Author           
Anderer, FA1, Author           
Affiliations:
1Anderer Group, Friedrich Miescher Laboratory, Max Planck Society, ou_3470951              

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 Abstract: In STU mice bearing metastasizing SV40-transformed 51A-232B-M tumors, an immune response against a cellular 60kDa protein (p60) developed in about 50% of the tumor-bearing animals, in addition to the response against SV40 large T-antigen and cellular protein p53. The anti-p60 auto-immune response could be observed as early as 11 days after tumor challenge and was strictly linked with metastatic spread but was not a prerequisite for metastasis. Anti-p60 antibodies could not be detected in sera of animals bearing metastasizing Rous-sarcoma virus-transformed or methylcholanthrene-induced tumors, or in sera from human cancer patients with clinically confirmed metastatic spread. The anti-p60 auto-antibodies showed a broad cross-reactivity against components of similar size in a great number of cell lines of various species and in normal mouse tissue. The p60 auto-antigen is a cytoplasmic protein which is neither phosphorylated nor glycosylated in vivo. Immunoblotting performed with fresh cell lysates under non-reducing conditions using tumor-bearer sera revealed a diffuse p60 double band, but under reducing conditions only one sharp p60 band was observed. The reaction of p60 with anti-p60 auto-antibodies could be completely blocked by pre-treatment of fresh cell lysates with N-ethylmaleimide or p-chloromercuriphenyl sulfonate, or by oxidation in air prior to immunoblotting, indicating that the anti-p60 autoimmune response was directed against an epitope sensitive to SH-group-blocking reagents. Immunofluorescence studies with tumor-bearer sera showed only a very weak cytoplasmic fluorescence, possibly due to the nature of the p60 SH-groups in situ being masked. Immunoprecipitates with monoclonal antibodies against SV40 large T-antigen and p53 obtained from fresh cell lysates of SV40-transformed tumor cells contained no associated p60 auto-antigen. The p60 auto-antigen was purified from tumor cell homogenates with an enrichment factor of about 2,000; its iso-electric point is at pH 6.8. Determination of the biological half-life of p60 yielded a value of about 28 hr. The p60 auto-antibodies in pools of tumor-bearer sera taken at day 40 after tumor challenge all belonged to the IgG1 subclass.

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 Dates: 1988-12
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1002/ijc.2910420620
PMID: 2461350
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Title: International Journal of Cancer
  Other : Int. J. Cancer
Source Genre: Journal
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Publ. Info: New York, NY [etc.] : Wiley-Liss [etc.]
Pages: - Volume / Issue: 42 (6) Sequence Number: - Start / End Page: 906 - 912 Identifier: ISSN: 0020-7136
CoNE: https://pure.mpg.de/cone/journals/resource/954927701080