High-titer HER-2/neu protein-specific antibody can be detected in patients with early-stage breast cancer.

Disis, Mary L.; Pupa, Serenella M.; Gralow, Julie R.; Dittadi, Ruggero; Ménard, Sylvie; Cheever, Martin A.

doi:10.1200/jco.1997.15.11.3363

Cited by 306 publications

(211 citation statements)

References 11 publications

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“…It is noteworthy that in our study one of 29 human control sera harbored speci®c anti-ErbB2 reactivity. Sporadic anti-ErbB2 immunoreactivity in apparently normal donors was also observed by others (Disis et al, 1994a(Disis et al, , 1997. In the absence of detailed clinical information on normal donors, the reason for such reactivity is currently unknown.…”

Section: Discussionmentioning

confidence: 65%

Immune responses to all ErbB family receptors detectable in serum of cancer patients

et al. 1999

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Employing NIH3T3 transfectants with individual human ErbB receptor coding sequences as recombinant antigen sources, we detected by immunoblot analysis speci®c immunoreactivity against all four ErbB receptors among 13 of 41 sera obtained from patients with di erent types of epithelial malignancies. Overall, serum positivity was most frequently directed against ErbB2 followed by EGFR, ErbB3 and ErbB4. Speci®city patterns comprised tumor patients with unique serum reactivity against ErbB2 or ErbB4. Moreover, approximately half of the positive sera exhibited concomitant reactivity with multiple ErbB receptors including EGFR and ErbB2, EGFR and ErbB4, ErbB2 and ErbB3 or EGFR, ErbB2 and ErbB3. Serum reactivity was con®rmed for the respective ErbB receptors expressed by human tumor cells and corroborated on receptor-speci®c immunoprecipitates. Positive sera contained ErbB-speci®c antibodies of the IgG isotype. Representative immunohistochemical analysis of tumor tissues suggested overexpression of ErbB receptors for which serum antibodies were detectable in ®ve of six patients. These ®ndings implicate multiple ErbB receptors including ErbB3 and ErbB4 in addition to EGFR and ErbB2 in primary human cancer. Heterogeneity of natural ErbB-speci®c responses in cancer patients warrants their evaluation in light of immunotherapeutic approaches targeting these receptors.

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Section: Discussionmentioning

confidence: 65%

Immune responses to all ErbB family receptors detectable in serum of cancer patients

et al. 1999

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“…Thus, we next compared the abilities of our DC populations to stimulate primary MLRs against allogeneic CD8 + T cells. We found that DC HER -2 / TNF -a , which had been coinfected with AdVHER2 / neu and AdVTNF -A, induced stronger DCs were infected with either AdVGFP or AdVTNF -a at MOI of 100 ( 1Â10 7 DCs vs 1Â10 9 pfu of either AdVGFP or AdVTNF -a ), or both of these two adenoviruses at MOI of 100 for each adenovirus ( 1Â10 7 DCs vs 1Â10 9 pfu of AdVGFP and 1Â10 9 pfu of AdVTNF -a ). The infected DCs were stained by PE -conjugated anti -TNF -a antibody as described under Materials and methods.…”

Section: Her -2 / Tnf -A Cells Induce Enhanced T -Cell Proliferatimentioning

confidence: 91%

Enhanced HER-2/neu-specific antitumor immunity by cotransduction of mouse dendritic cells with two genes encoding HER-2/neu and alpha tumor necrosis factor

et al. 2002

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The present study uses an in vivo murine tumor model expressing the human HER -2 / neu antigen to evaluate the potential vaccine using dendritic cells ( DCs ) infected with adenovirus AdVHER -2. We first investigated whether infected DCs ( DC HER -2 ) engineered to express HER -2 / neu could induce HER -2 / neu -specific immune responses. Our data showed that ( i ) AdVHER2 -infected DC HER -2 expressed HER -2 / neu by Western blot and flow cytometric analysis, and ( ii ) vaccination of mice with DC HER -2 induced HER -2 / neu -specific cytotoxic T -lymphocyte ( CTL ) responses, but protected only 25% of vaccinated mice from challenge of 3Â10 5 MCA26 / HER -2 tumor cells. Further, to enhance the efficacy of DC HER -2 vaccine, we coinfected DCs with both AdVHER -2 and AdVTNF -a. The infected DCs ( DC HER -2 / TNF -a ) displayed the expression of both HER -2 / neu and TNF -a by flow cytometric and ELISA analysis. We next investigated whether DC HER -2 / TNF -a could induce stronger HER -2 / neu -specific immune responses. We found that DC HER -2 / TNF -a displayed up -regulation of immunologically important CD40, CD86, and ICAM -I molecules compared with DC HER -2 , indicating that the former ones are more mature forms of DCs. Vaccination of DC HER -2 / TNF -a induced stronger allogeneic T -cell proliferation and 36% enhanced HER -2 / neu -specific T -cell responses in vitro than DC HER -2 cells. More importantly, it stimulated the significant anti -HER -2 / neu immunity in vivo, which protected 8 / 8 mice from challenge of 3Â10 5 MCA26 / HER -2 tumor cells. Therefore, DCs genetically engineered to express both the tumor antigen and cytokines such as TNF -a as an immunoadjuvant are likely to represent a new direction in DC vaccine of cancer.

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“…12,36 -43 For example, anti-p53 antibodies were detected in 3-65% of sera of patients with cancer, 38,39 and anti-HER2/neu antibodies were detected in 11% of patients with breast carcinoma. 40 Also, antibodies reactive with cancer/testis antigen, such as MAGE, GAGE, BAGE, SSX, and NY-ESO-1, were found in 4.2-12.5% of sera of patients with melanoma and carcinoma of the lung, breast, and ovary. 41,42 Antibodies against mucins were elicited in 8.3% of patients with various types of cancer.…”

Section: Anti-m2bp Antibody In Sera From Patients With Lung Carcinomamentioning

confidence: 97%

Expression and immunogenicity of a tumor‐associated antigen, 90K/Mac‐2 binding protein, in lung carcinoma

Ozaki

Kontani

Hanaoka³

et al. 2002

Cancer

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BACKGROUNDThe authors attempted to obtain shared proteins among lung carcinoma cells by column chromatographies. A glycoprotein with approximately 500 kDa isolated from QG56 cells showed an identical amino acid sequence to 90K/Mac‐2 binding protein (M2BP). This protein has been reported to be highly expressed and to modulate the expression of surface molecules involved in immune responses on cultured cancer cells. Therefore, it would be beneficial for M2BP to be targeted in cancer immunotherapy.METHODSThe authors analyzed the expression of M2BP in lung carcinoma cells and M2BP's immunogenicity as a tumor antigen. Eight cultured lung carcinoma cell lines and 28 tumor tissues from patients with lung carcinoma were examined for the expression of M2BP mRNA and protein. Sera from cancer patients (n = 23) and healthy donors (n = 19) were studied for their reactivity to M2BP peptides by enzyme–linked immunosorbent assay.RESULTSSeven of the 8 (87.5%) lung carcinoma cell lines and 17 of the 28 (60.7%) tumor tissues expressed high levels of M2BP mRNA. Most of the M2BP mRNA‐positive cancer cell lines and tumors also showed M2BP protein expression. The serum levels of antibodies to M2BP were elevated in 30.4% of the patients. In addition, M2BP‐specific immunoglobulin G was observed in all patients with anti‐M2BP antibodies.CONCLUSIONSM2BP is highly expressed in lung carcinoma cells and is sufficiently immunogenic to elicit specific immunity to this molecule in patients with lung carcinoma. M2BP is expected to be useful as a tumor marker and a target antigen in cancer immunotherapy. Cancer 2002;95:1954–62. © 2002 American Cancer Society.DOI 10.1002/cncr.10899

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High-titer HER-2/neu protein-specific antibody can be detected in patients with early-stage breast cancer.

Cited by 306 publications

References 11 publications

Immune responses to all ErbB family receptors detectable in serum of cancer patients

Immune responses to all ErbB family receptors detectable in serum of cancer patients

Enhanced HER-2/neu-specific antitumor immunity by cotransduction of mouse dendritic cells with two genes encoding HER-2/neu and alpha tumor necrosis factor

Expression and immunogenicity of a tumor‐associated antigen, 90K/Mac‐2 binding protein, in lung carcinoma

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