Oncogenic proteins as tumor antigens

doi:10.1016/S0952-7915(96)80079-3

Current Opinion in Immunology

Volume 8, Issue 5, October 1996, Pages 637-642

https://doi.org/10.1016/S0952-7915(96)80079-3 Get rights and content

Abstract

Human immune responses to oncogenic proteins have been reported and are continuing to be defined. Immunity to nonmutated overexpressed oncoproteins as well as to mutated or unique cancer-specific oncoproteins has been identified. Immune system based treatments targeting oncogenic proteins have shown therapeutic efficacy in animals models and are currently being translated into human clinical trials

References (42)

AF Tilkin et al.
Primary proliferative T cell response to wild-type p53 protein in patients with breast cancer
Eur J Immunol
(1995)
M Theobald et al.
Targeting p53 as a general tumor antigen
Proc Natl Acad Sci USA
(1995)
GJ Ten-Bosch et al.
Recognition of peptides corresponding to the joining region of p210BCR-ABL protein by human T cells
Leukemia
(1995)
B Fisk et al.
Identification of an immunodominat peptide of HER-2/neu protooncogene recognized by ovarian tumor-specific cytotoxic T lymphocyte lines
J Exp Med
(1995)
GE Peoples et al.
Breast and ovarian cancer-specific cytotoxic T lymphocytes recognize the same HER2/neu-derived peptide
Proc Natl Acad Sci USA
(1995)
LM Weiner et al.
Phase I trial of 2B1, a bispecific monoclonal antibody targeting c-erbB-2 and Fc gamma RIII
Cancer Res
(1995)
J Baselga et al.
The epidermal growth factor receptor as a target for therapy in breast carcinoma
Breast Cancer Res Treat
(1994)
M Yanuck et al.
A mutant p53 tumor suppressor protein is a target for peptide-induced CD8⁺ cytotoxic T cells
Cancer Res
(1993)
SF Winter et al.
Development of antibodies against p53 in lung cancer patients appears to be dependent on the type of p53 mutation
Cancer Res
(1992)
B Schlichtholz et al.
The immune response to p53 in breast cancer patients is directed against immunodominant epitopes unrelated to the mutational hot spot
Cancer Res
(1992)

JG Houbiers et al.

Antibodies against p53 are associated with poor prognosis of colorectal cancer

Br J Cancer

(1995)

R Lubin et al.

Serum p53 antibodies as early markers of lung cancer

Nat Med

(1995)

JA Green et al.

Serum p53 auto-antibodies: incidence in familial breast cancer

Eur J Cancer

(1994)

Y Noguchi et al.

Influence of interleukin 12 on p53 peptide vaccination against established Meth A sarcoma

Proc Natl Acad Sci USA

(1995)

HW Nijman et al.

p53, a potential target for tumor-directed T cells

Immunol Lett

(1994)

M Ropke et al.

T cell-mediated cytotoxicity against p53-protein derived peptides in bulk and limiting dilution cultures of healthy donors

Scand J Immunol

(1995)

MA Cheever et al.

Immunity to oncogenic proteins

Immunol Rev

(1995)

SI Abrams et al.

Peptide-specific activiation of cytolytic CD4⁺ T lymphocytes against tumor cells bearing mutated epitopes of K-ras p21

Eur J Immunol

(1995)

RG Fenton et al.

Induction of T-cell immunity against Ras oncoproteins by soluble protein or Ras-expressing Escherichie coll

J Natl Cancer Inst

(1995)

M Takahashi et al.

Antibody responses to ras proteins in patients with colon cancer

Clin Cancer Res

(1995)

B Fossum et al.

p21-ras-peptide-specific T-cell responses in a patient with colorectal cancer. CD4⁺ and CD8⁺ T cells recognize a peptide corresponding to a common mutation (13Gly→Asp)

Int J Cancer

(1994)

Cited by (118)

A novel fluorescent detection for PDGF-BB based on dsDNA-templated copper nanoparticles
2014, Chinese Chemical Letters
A novel method for the detection of PDGF-BB has been developed using double-strand DNA-copper nanoparticles (dsDNA-CuNPs) as fluorescent markers. This assay relies on the premise that the aptamer-based probe undergoes a conformational change upon binding with target protein, and subsequently triggers polymerization reaction to generate dsDNA. Then, the resultant dsDNA can be used as a template for the formation of CuNPs with high fluorescence. Under the optimized conditions, the proposed assay allowed sensitive and selective detection of PDGF-BB with a detection limit of 4 nmol/L. This possibly makes it an attractive platform for the detection of a variety of biomolecules whose aptamers undergo similar conformational change.
Differential methylation of TSP50 and mTSP50 genes in different types of human tissues and mouse spermatic cells
2008, Biochemical and Biophysical Research Communications
Earlier studies identified human TSP50 as a testis-specific gene that encoded a threonine protease. Most importantly, TSP50 could be a cancer/testis antigen since there was a high frequency of reactivation in breast cancer biopsies. It was also found to be negatively regulated by the p53 gene. To further characterize this gene, we recently examined the DNA methylation patterns of the TSP50 gene promoter in normal human testis, as well as breast tissue and a testicular embryonic carcinoma cell line (HTECCL). Bisulfite genomic sequencing results demonstrated that the promoter exhibited mixed DNA methylation patterns in normal human testis, mainly non-methylation versus slight methylation, which could be attributed to the different stages spermatic cells go through during spermatogenesis. In contrast, it was methylated to a much greater extent in both breast tissue and HTECCL. To find out whether DNA methylation status was related to spermatogenesis stages, we analyzed DNA methylation patterns of the mTSP50 (the mouse ortholog of TSP50) promoter in spermatocytes and spermatozoa isolated from sexually mature mice. The results clearly demonstrated that each group of cells exhibited its preferential DNA methylation pattern that apparently was consistent with the gene expression status observed before. Taken together, our findings suggested that DNA methylation might regulate the TSP50 and mTSP50 gene expressions in different types of tissues and spermatic cells.
Cancer vaccines: Accomplishments and challenges
2008, Critical Reviews in Oncology/Hematology
Citation Excerpt :
A very large number of tumor antigens have been characterized to date (reviewed in [8]). Some of the most studied in animal models as well as in early phase clinical trials include melanocyte differentiation antigens (MART-1 [27], gp100 [25], tyrosinase [51], Melan A [52], TRP-1 [53]), tumor-specific mutated gene products (CDK-4 [54], β-catenin [55], MUM-1 [56], oncogenes p53 [57,58] and ras (K- and H-ras) [59]), cancer testes antigens (MAGE antigens, GAGE and NY-ESO1), over-expressed or widely expressed self-antigens (MUC-1 [60], Her2-neu (reviewed in [61]), CEA [62], WT p53 [63], cyclin B1 [29], SART-1 [64], PRAME [65,66], p15 [67]),viral antigens (HPV E7 [68], EBV-derived antigens (reviewed in [69]), and telomerase (reviewed in [70]) [71–76]. Vaccination with monoclonal antibodies specific for a tumor-associated antigen results in the formation of autologous antibodies against the vaccine (reviewed in [32]).
Advancements in knowledge in diverse fields of science, including genetics, cell biology, molecular biology and biochemistry, have shed light on the origins of cancer and cell intrinsic properties that allow it to grow, invade and metastasize. Many therapies currently in use or under development are based on this knowledge. Advances in immunology, on the other hand, have shed light on how the host responds to these malignant properties of cancer. Based on that knowledge, immunotherapy, in particular vaccines directed at improving the host response against cancer, is being developed as an alternative therapeutic approach. In this review, we address main issues that have driven development of cancer vaccines and the challenges that have been met and/or are anticipated.
A Colorimetric Biosensing Platform with Aptamers, Rolling Circle Amplification and Urease-Mediated Litmus Test
2023, Angewandte Chemie - International Edition
Enzyme-Instructed Peptide Assembly Favored by Preorganization for Cancer Cell Membrane Engineering
2023, Journal of the American Chemical Society
Cancer-Specific Delivery of Proteolysis-Targeting Chimeras (PROTACs) and Their Application to Cancer Immunotherapy
2023, Pharmaceutics

View all citing articles on Scopus

View full text

Oncogenic proteins as tumor antigens

Abstract

Eur J Immunol

Proc Natl Acad Sci USA

Leukemia

J Exp Med

Proc Natl Acad Sci USA

Cancer Res

Breast Cancer Res Treat

A mutant p53 tumor suppressor protein is a target for peptide-induced CD8+ cytotoxic T cells

Cancer Res

Development of antibodies against p53 in lung cancer patients appears to be dependent on the type of p53 mutation

Cancer Res

The immune response to p53 in breast cancer patients is directed against immunodominant epitopes unrelated to the mutational hot spot

Cancer Res

Antibodies against p53 are associated with poor prognosis of colorectal cancer

Br J Cancer

Serum p53 antibodies as early markers of lung cancer

Nat Med

Serum p53 auto-antibodies: incidence in familial breast cancer

Eur J Cancer

Influence of interleukin 12 on p53 peptide vaccination against established Meth A sarcoma

Proc Natl Acad Sci USA

p53, a potential target for tumor-directed T cells

Immunol Lett

T cell-mediated cytotoxicity against p53-protein derived peptides in bulk and limiting dilution cultures of healthy donors

Scand J Immunol

Immunity to oncogenic proteins

Immunol Rev

Peptide-specific activiation of cytolytic CD4+ T lymphocytes against tumor cells bearing mutated epitopes of K-ras p21

Eur J Immunol

Induction of T-cell immunity against Ras oncoproteins by soluble protein or Ras-expressing Escherichie coll

J Natl Cancer Inst

Antibody responses to ras proteins in patients with colon cancer

Clin Cancer Res

p21-ras-peptide-specific T-cell responses in a patient with colorectal cancer. CD4+ and CD8+ T cells recognize a peptide corresponding to a common mutation (13Gly→Asp)

Int J Cancer

A mutant p53 tumor suppressor protein is a target for peptide-induced CD8⁺ cytotoxic T cells

Peptide-specific activiation of cytolytic CD4⁺ T lymphocytes against tumor cells bearing mutated epitopes of K-ras p21

p21-ras-peptide-specific T-cell responses in a patient with colorectal cancer. CD4⁺ and CD8⁺ T cells recognize a peptide corresponding to a common mutation (13Gly→Asp)