methyl-2-5-dihydroxycinnamate has been researched along with Neoplasms* in 2 studies
2 other study(ies) available for methyl-2-5-dihydroxycinnamate and Neoplasms
| Article | Year |
|---|---|
Tyrosine kinase inhibitor, methyl 2,5-dihydromethylcinnimate, induces PML nuclear body formation and apoptosis in tumor cells.
Promyelocytic leukemia (PML) nuclear bodies (PML-NBs) are the nuclear structure consisting of various proteins such as PML, SUMO-1, and p53. PML-NBs are implicated in the regulation of tumor suppression, antiviral responses, and apoptosis. In this study, we searched for bioactive metabolites that would promote the formation of PML-NBs in tumor cells. As a result, methyl 2,5-dihydromethylcinnimate (2,5-MeC), a tyrosine kinase inhibitor, enhanced expression and/or stability of PML proteins and induced PML-NB formation in p53 null H1299 cells established from non-small cell lung cancer (NSCLC) and wild-type p53-expressing U2OS cells derived from osteosarcoma. Furthermore, it enhanced apoptosis by exogenously expressed wild type p53 and the expression of p53-responsive genes, such as PUMA and p21, in H1299 cells. 2,5-MeC also activated endogenous p53 and induced apoptosis in U2OS cells. The results suggest that 2,5-MeC is likely to be a promising candidate drug for the clinical treatment of terminal cancer-expressing wild-type p53. Topics: Antineoplastic Agents; Apoptosis; Cell Line, Tumor; Cinnamates; Humans; Neoplasm Proteins; Neoplasms; Nuclear Proteins; Promyelocytic Leukemia Protein; Protein Kinase Inhibitors; Protein-Tyrosine Kinases; SUMO-1 Protein; Transcription Factors; Tumor Suppressor Protein p53; Tumor Suppressor Proteins | 2007 |
Inhibition of protein tyrosine kinases or protein kinase C prevents nonspecific killer T lymphocyte-mediated tumoricidal activity.
The signal transduction events which govern major histocompatibility complex-unrestricted tumour cell destruction by nonspecific killer T lymphocytes induced with anti-CD3 antibody have not yet been determined. In this study we used pharmacologic inhibitors to investigate the role of protein tyrosine kinases (PTK) and protein kinase C (PKC) in this process. The PTK-inhibitors herbimycin A, genistein, and methyl 2,5-dihydroxycinnamate blocked anti-CD3-activated killer T (AK-T) lymphocyte-mediated killing of tumour target cells. The PKC-inhibitors staurosporine, calphostin C, and myristoylated PKC pseudosubstrate peptide, as well as PKC desensitization by phorbol 12-myristate 13-acetate pretreatment, also suppressed the cytolytic effector function of AK-T lymphocytes. Lack of tumoricidal activity was not due to reduced AK-T lymphocyte binding to tumour target cells but was associated with the abrogation of granule exocytosis, indicating that PTK and PKC are involved in the postbinding process which results in delivery of the 'lethal hit' by AK-T lymphocytes. Topics: Animals; Antibody-Dependent Cell Cytotoxicity; Benzoquinones; Cinnamates; Female; Genistein; Granzymes; Immunosuppressive Agents; Isoflavones; Killer Cells, Natural; Lactams, Macrocyclic; Mice; Mice, Inbred C57BL; Muromonab-CD3; Neoplasms; Protein Kinase C; Protein-Tyrosine Kinases; Quinones; Rifabutin; Serine Endopeptidases; Signal Transduction | 1997 |