Detection in human breast carcinomas of an antigen immunologically related to a group-specific antigen of mouse mammary tumor virus

Mesa-Tejada, Ricardo; Keydar, Iafa; Ramanarayanan, M; Ohno, Tsuneya; Fenoglio, Cecilia M.; Spiegelman, S.

doi:10.1073/pnas.75.3.1529

Cited by 109 publications

(55 citation statements)

References 18 publications

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“…6 by a uniquely informative instance. We have here a section from a case with intraductal and invasive breast carcinoma which shows a nipple duct involved with lobular carcinoma in situ and a nearby duct exhibiting apocrine metaplasia, a benign microscopic component of cystic disease that we have earlier reported (13) to stain with anti-MMTV IgG. This combination of malignant and benign lesions in the same section was of particular interest to us.…”

Section: -I-mentioning

confidence: 99%

“…We now come to the key issue of the present investigation, which centers on the question of whether removal of the sugar residues from gp52 interferes in any way with its ability to block the specific antibody from anti-MMTV IgG responsible for the immunohistochemical staining of human breast cancer sections (13). Four clearly positive tumors were selected for testing and the results with all were satisfyingly clear-cut.…”

Section: -I-mentioning

confidence: 99%

“…Rabbit anti-MMTV (RIII) purified total IgG fraction was prepared and absorbed with the following soluble immunoabsorbants, as described (12,13), by using the indicated quantities per each 0.5 ml contain. (400 ,g) was treated with proteinase K (50 gug) for 16 hr at 370C.…”

Section: Enzymesmentioning

confidence: 99%

“…In any event, this possibility was explored by using antisera raised against the proteins of MMTV as reagents to search for crossreactive components in human breast cancer tissue and this search was crowned with apparent success. An antigen immunologically related to the group-specific antigen, gp52 (a 52,000-dalton glycoprotein) of MMTV was identified (12,13) in paraffin sections of human breast cancers by means of an indirect immunoperoxidase procedure.…”

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confidence: 99%

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Human breast carcinoma antigen is immunologically related to the polypeptide of the group-specific glycoprotein of mouse mammary tumor virus.

Ohno¹,

Mesa-Tejada²,

Keydar³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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We have shown [Mesa-Tejada, R., Keydar, I., Ramanarayanan, M., Ohno, T., Fenoglio (14). Because at most five sections are stained from each breast tumor, the percentage of positives detected must be an underestimate.It was of course gratifying to have extended to the protein level the relationship between human breast cancer and MMTV that was initially discovered in terms of nucleic acid sequence homology. The etiologic implications of these findings are of obvious interest but our immediate concern is the possibility that they might be used to generate clinically useful information. To this end, it was of interest to resolve certain issues regarding the nature of crossreactivity observed between the gp52 and the unique antigen found in the human breast cancers. In particular, it was of some importance to know whether the sugar or the protein moiety of the gp52 glycoprotein was responsible for its ability to block the immunological crossreaction with the antigen found in the breast cancer cells. Aside from its genetic implications, the outcome could materially influence the nature of our attempts to isolate and characterize the human tumorspecific antigen.It is the purpose of the present paper to present data that resolve this issue. The results establish that the antigenic crossreactivity between human breast cancer and gp52 glycoprotein resides in the polypeptide portion and not in the sugar residues of the latter protein. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. MATERIALS AND METHODS Enzymes

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Section: -I-mentioning

confidence: 99%

Section: -I-mentioning

confidence: 99%

Section: Enzymesmentioning

confidence: 99%

mentioning

confidence: 99%

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Human breast carcinoma antigen is immunologically related to the polypeptide of the group-specific glycoprotein of mouse mammary tumor virus.

Ohno¹,

Mesa-Tejada²,

Keydar³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…During the 1970s, MMTV was suggested to play a role in the etiology of human breast cancer when claims were first made that MMTV antigens were involved in this disease (3). A new wave of interest in this issue started in the mid-1990s when MMTV DNA sequences were first identified, using PCR technology, in 38% of human breast cancer samples, but not in healthy tissue (4).…”

Section: Introductionmentioning

confidence: 99%

The Signal Peptide of Mouse Mammary Tumor Virus-Env: A Phosphoprotein Tumor Modulator

Feldman

Roniger

Bar-Sinai

et al. 2012

Molecular Cancer Research

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Mouse mammary tumor virus (MMTV) is associated primarily with mammary carcinomas and lymphomas. The signal peptide of the MMTV envelope precursor is uniquely targeted to nucleoli of cells that harbor the virus, where it can function as a nuclear export factor for intron-containing transcripts. Antibodies to this signal peptide, which we refer to as p14, were previously shown to label nucleoli in a subset of human breast cancers. To look for additional cellular functions of p14, different mutants were ectopically expressed in the MCF-7 human breast cancer cell line. This approach identified motifs responsible for its nucleolar targeting, nucleocytoplasmic shuttling, target protein (B23, nucleophosmin) binding, and phosphorylation at serine 18 and 65 both in situ and in vitro. To test the role of these phosphorylation sites, we carried out in vivo tumorigenesis studies in severe combined immunodeficient mice. The findings show that the p14-Ser65Ala mutation is associated with impaired tumorigenicity, whereas the p14-Ser18Ala mutation is associated with enhanced tumorigenicity. Microarray analysis suggests that phosphorylation at serine 18 or at serine 65 is associated with transcriptional regulation of the L5 nucleolar ribosomal protein (a p14 target) and the Erb-B signal transduction pathway. Taken together, these results show that the phosphorylation status of p14 determines whether it functions as a pro-oncogenic or antioncogenic modulator.

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Prognostic Significance of Cellular Immunity to Autologous Breast Carcinoma and Glycoprotein 55

Black

Zachrau²,

Ashikari³

et al. 1989

Arch Surg

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Detection in human breast carcinomas of an antigen immunologically related to a group-specific antigen of mouse mammary tumor virus

Abstract: Detection in human breast carcinomas of an antigen immunologically related to a group-specific antigen of mouse mammary tumor virus (

Cited by 109 publications

References 18 publications

Human breast carcinoma antigen is immunologically related to the polypeptide of the group-specific glycoprotein of mouse mammary tumor virus.

Human breast carcinoma antigen is immunologically related to the polypeptide of the group-specific glycoprotein of mouse mammary tumor virus.

The Signal Peptide of Mouse Mammary Tumor Virus-Env: A Phosphoprotein Tumor Modulator

Prognostic Significance of Cellular Immunity to Autologous Breast Carcinoma and Glycoprotein 55

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