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

Ozaki, Yoshitomo; Kontani, Keiichi; Hanaoka, Jun; Chano, Tokuhiro; Teramoto, Koji; Tezuka, Noriaki; Sawai, Satoru; Fujino, Shozo; Tokura, Y.; Okabe, Hidetoshi; Ohkubo, Iwao

doi:10.1002/cncr.10899

Cited by 33 publications

(26 citation statements)

References 38 publications

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“…These results were also shown for breast cancer, where Mac-2BP levels were associated with poor prognosis, presence of metastasis in liver, and shorter disease-free interval (Iacobelli et al, 1994). Elevated levels of this protein have also been shown in lung carcinoma (Ozaki et al, 2002), correlating strongly with clinical staging (Ozaki et al, 2004a).…”

Section: Mac-2 Binding Protein: a Tumor-associated Antigenmentioning

confidence: 55%

The Conserved Scavenger Receptor Cysteine-Rich Superfamily in Therapy and Diagnosis

Moestrup²,

et al. 2011

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Section: Mac-2 Binding Protein: a Tumor-associated Antigenmentioning

confidence: 55%

The Conserved Scavenger Receptor Cysteine-Rich Superfamily in Therapy and Diagnosis

Moestrup²,

et al. 2011

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“…Galectin-3-binding protein is a secreted 90 kDa Nglycosylated protein with affinity for galectins as well as extracellular matrix proteins [12]. Sudden increase in serum galectin-3-binding protein levels have been reported in various infectious and cancerous diseases, including hepatitis C [13][14][15][16][17][18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Galectin-3-binding protein: a serological and histological assessment in accordance with hepatitis C-related liver fibrosis

Cheung

Libbrecht²,

Tilleman³

et al. 2010

European Journal of Gastroenterology & Hepatology

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Objectives. Invasive liver biopsy is the current method for the assessment of liver fibrosis. In search of non-invasive alternatives, galectin-3-binding protein was introduced as a candidate-marker of hepatitis C-related fibrosis based on serum proteomics.We investigated the role of galectin-3-binding protein as a single-marker of significant fibrosis and cirrhosis by means of serology and histology and studied the role of glycosylation on the expression in hepatitis C-and alcohol-related cirrhosis. Methods. Sera and available biopsies of hepatitis C patients with various fibrosis-gradesand patients with alcohol-related cirrhosis were used for galectin-3-binding protein measurements by enzyme-linked immunosorbent assay and immunohistochemistry, respectively. Glycosylation-effect was analyzed by Western blot. Data was analyzed in accordance to fibrosis.Results. Galectin-3-binding protein was increased during cirrhosis (22.7 ± 10.1 µg/mL) in contrast to mild (11.3 ± 6.4 µg/mL) and moderate fibrosis (13.4 ± 8.3 µg/mL) (p < 0.001; p = 0.004, respectively). Receiver operator characteristics curves showed areas under the curve of 0.68 and 0.81 for the detection of respectively significant fibrosis and cirrhosis. Similar findings in hepatic expression were obtained, in which cirrhosis was associated with diffuse, parenchymal expression (p = 0.002). The observed difference between hepatitis C-and alcohol-related cirrhosis (13.5 ± 9.0 µg/mL) (p = 0.009) could not be explained by glycosylation. (mean ± standard deviation) Conclusions. Our recent findings confirm our initial proteome results on serological and histological level as well as the role of galectin-3-binding protein as a marker of 4 4 hepatitis C-related fibrosis, especially cirrhosis. Implication of this protein in future multi-marker study should be considered.

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“…12,13 It has been proposed that the interaction between these proteins may enhance the growth and biological behavior of cancer cells. In cancerous tissues, 90K is expressed at high levels [14][15][16] and is associated with poor prognosis. [16][17][18] Immunohistochemical analyses of 90K expression have revealed weak or no expression in most normal tissues and strong upregulation in tumor cells of human neoplastic tissues, 19 suggesting that 90K can be used as a target antigen in cancer immunotherapy.…”

Section: Introductionmentioning

confidence: 99%

“…In cancerous tissues, 90K is expressed at high levels [14][15][16] and is associated with poor prognosis. [16][17][18] Immunohistochemical analyses of 90K expression have revealed weak or no expression in most normal tissues and strong upregulation in tumor cells of human neoplastic tissues, 19 suggesting that 90K can be used as a target antigen in cancer immunotherapy. Ulmer et al 20 demonstrated that immunohistochemical analyses of colon tumors showed elevated expression of 90K in all tumor samples compared to normal colon samples.…”

Section: Introductionmentioning

confidence: 99%

Dendritic cell-based immunotherapy for colon cancer using an HLA-A*0201-restricted cytotoxic T-lymphocyte epitope from tumor-associated antigen 90K

et al. 2013

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Tumor-associated antigen 90K is implicated in cell-cell and cell-extracellular matrix adhesion through its interaction with galectin-3 and integrin-b1 and is highly expressed in malignant tissues, making it a novel target for the development of new immunotherapies. We investigated a potential immunotherapy treatment for colon cancer using 90K-specific cytotoxic T lymphocytes induced by autologous dendritic cells and pulsed with 90K peptides. We selected three peptides (90K 351 , 90K 5 and 90K 523 ) that bind to HLA-A*0201 molecules on the basis of their binding affinity, as determined by a peptide-T2 binding assay. Dendritic cells pulsed with 90K peptides resulted in the efficient generation of mature dendritic cells and exhibited enhanced T-cell stimulation and polarization of naive T cells toward Th1. Dendritic cells pulsed with 90K peptides generated potent cytotoxic T-lymphocytes that lysed T2 cells loaded with each 90K peptide, and 90K1 /HLA-A2 1 colon cancer cell lines, including HCT116 and SW480, in a dose-dependent and HLA-A*0201-restricted manner. No killing was observed in 90K 1 /HLA-A2 2 DLD1 or 90K 2 /HLA-A2 2 K562 cells. Therefore, we believe that cytotoxic T-lymphocytes stimulated by 90K peptide-pulsed dendritic cells naturally recognize the 90K peptide presented by colon cancer cells in the context of HLA-A2, and kill 90K-positive tumor cells. Dendritic cells pulsed with 90K peptides led to the induction of granzyme B and perforin positive CD8 1 T cells against HCT116 and SW480 cells, but not DLD1 cells. In conclusion, 90K-specific cytotoxic T lymphocytes, generated by stimulating T cells with 90K peptide-pulsed dendritic cells, could be useful effector cells for the immunotherapy treatment of colon cancer.

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

Cited by 33 publications

References 38 publications

The Conserved Scavenger Receptor Cysteine-Rich Superfamily in Therapy and Diagnosis

The Conserved Scavenger Receptor Cysteine-Rich Superfamily in Therapy and Diagnosis

Galectin-3-binding protein: a serological and histological assessment in accordance with hepatitis C-related liver fibrosis

Dendritic cell-based immunotherapy for colon cancer using an HLA-A*0201-restricted cytotoxic T-lymphocyte epitope from tumor-associated antigen 90K

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