ritonavir and Melanoma

ritonavir has been researched along with Melanoma* in 2 studies

Other Studies

2 other study(ies) available for ritonavir and Melanoma

ArticleYear
Senescence as a main mechanism of Ritonavir and Ritonavir-NO action against melanoma.
    Molecular carcinogenesis, 2019, Volume: 58, Issue:8

    The main focus of this study is exploring the effect and mechanism of two HIV-protease inhibitors: Ritonavir and Ritonavir-nitric oxide (Ritonavir-NO) on in vitro growth of melanoma cell lines. NO modification significantly improved the antitumor potential of Ritonavir, as the IC

    Topics: Actins; beta-Galactosidase; Cell Line, Tumor; Cell Proliferation; Cellular Senescence; HIV Protease Inhibitors; Humans; Lipofuscin; Melanoma; Reactive Oxygen Species; Ribosomal Protein S6 Kinases; Ritonavir; Tubulin; Tumor Suppressor Protein p53; Vinculin

2019
Naturally processed and concealed HLA-A2.1-restricted epitopes from tumor-associated antigen tyrosinase-related protein-2.
    International journal of cancer, 2000, Jul-15, Volume: 87, Issue:2

    In this study, a computer-assisted reverse immunology approach was utilized in order to identify potentially antigenic peptides derived from the differentiation antigen TRP-2, a melanosomal protein frequently expressed in melanoma. Among the seven peptides complying with HLA-A2.1-binding motifs, two induced specific CD8(+) cytotoxic T lymphocytes. HLA-A2.1(+) melanoma cells expressing TRP-2 were lysed by clones specific for TRP-2(360-368) (TLDSQVMSL) peptide, thus identifying it as a naturally processed epitope. Other T-cell clones directed against TRP-2(476-484) (VMGTLVALV) were unable to lyse HLA-matched TRP-2(+) cell lines. The role of intracellular proteolytic processing in the generation of this epitope was investigated by transfecting mini-genes encoding the TRP-2(476-484) peptide alone or carrying N- or C-terminal extensions. Specific T-cell clones recognized target cells expressing the cytotoxic T-lymphocyte (CTL)-defined epitope or its C-terminally extended precursor, but failed to recognize cells expressing the N-terminally extended TRP-2(476-484) peptide, suggesting the presence of a negative processing signal (NPS). Regarding C-terminus-flanking regions, mutational analysis indicates that the GLY485 residue plays a key role in the processing of the TRP-2(476-484) epitope. Interestingly, proteasome inhibitors preventing the generation of the MART-1/Melan-A(27-35) immunodominant melanoma tumor-associated antigen (TAA) promoted detectable presentation of TRP-2(476-484) epitope in HLA-A2.1(+) and TRP-2(+) tumor lines, as witnessed by cytokine release by specific T-cell clones.

    Topics: Acetylcysteine; Antigens, Neoplasm; CD8-Positive T-Lymphocytes; Cell Line, Transformed; Coculture Techniques; Cysteine Proteinase Inhibitors; DNA Mutational Analysis; Enzyme-Linked Immunosorbent Assay; Epitopes; HIV Protease Inhibitors; HLA-A2 Antigen; Humans; Intramolecular Oxidoreductases; Leukocytes, Mononuclear; Melanoma; Peptides; Reverse Transcriptase Polymerase Chain Reaction; Ritonavir; T-Lymphocytes, Cytotoxic; Tumor Cells, Cultured

2000