1999
DOI: 10.3892/ijo.14.5.991
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Regulation of human head and neck squamous cell carcinoma growth in tissue culture by opioid growth factor.

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Cited by 39 publications
(81 citation statements)
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“…With respect to human squamous cell carcinoma of the head and neck (SCCHN), the OGF-OGFr axis has been shown to be present (4,7,(16)(17)(18)(19) and functional (4,7,16,20,21). Clinical studies assessing the level of OGFr in surgical specimens of SCCHN (19) indicated that OGFr binding sites and protein levels were 9-fold and 5-fold, respectively, less in tissues of patients with SCCHN than in normal epithelium from patients undergoing uvulapalatoplasty or tonsillectomy.…”
Section: Introductionmentioning
confidence: 99%
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“…With respect to human squamous cell carcinoma of the head and neck (SCCHN), the OGF-OGFr axis has been shown to be present (4,7,(16)(17)(18)(19) and functional (4,7,16,20,21). Clinical studies assessing the level of OGFr in surgical specimens of SCCHN (19) indicated that OGFr binding sites and protein levels were 9-fold and 5-fold, respectively, less in tissues of patients with SCCHN than in normal epithelium from patients undergoing uvulapalatoplasty or tonsillectomy.…”
Section: Introductionmentioning
confidence: 99%
“…The mechanism of action appears to be that OGF upregulates the cyclindependent kinase inhibitor pathway in order to delay the G 0 /G 1 phase of the cell cycle (14). OGF and OGFr have been demonstrated by immunohistochemistry, radioimmunoassay, and/or receptor binding to be present in a variety of human and animal tumors and cancer cell lines (1)(2)(3)(4)(5)8,(15)(16)(17)(18)(19).…”
Section: Introductionmentioning
confidence: 99%
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“…OGF interacts with the OGF receptor (OGFr) to delay the G 1 /S interface of the cell cycle by modulating cyclin-dependent kinase inhibitory pathways (4 -6). Attenuation of the OGF-OGFr axis in cancer cells through: 1) disruption of OGF-OGFr interfacing by continuous exposure to opioid antagonists [e.g., naltrexone (NTX)] (2, 15, 34), 2) neutralization of OGF by antibodies to the peptide (15), or 3) a decrease in OGFr by antisense cDNA or siRNA for OGFr (26,37), stimulates cell proliferation. An increase in OGF-OGFr activity in cancer cells by 1) addition of exogenous OGF (2,15,34); 2) treatment with imidazoquinoline compounds, such as imiquimod and resiquimod (26); or 3) transfection of sense cDNA for OGFr (18,35), depresses cell proliferation.…”
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confidence: 99%