Protein kinase C in melanoma
- 1 June 2005
- journal article
- review article
- Published by Springer Nature in Cancer and Metastasis Reviews
- Vol. 24 (2) , 287-300
- https://doi.org/10.1007/s10555-005-1578-8
Abstract
Protein kinase C (PKC) is activated by diacylglycerol generated by receptor-mediated hydrolysis of membrane phospholipids to mediate signals for cell growth and plays as a target of tumor-promoting phorbol esters in malignant transformation. PKC is a family of enzymes and their expression profiles have been examined in the normal melanocytes and melanoma cells, and studies have been carried out on the functions of PKC isoforms in proliferation, transformation, and metastasis of melanoma cells. Here, we summarize current knowledge of the expression and possible roles of the PKC family in melanoma in comparison with those of normal melanocytes.Keywords
This publication has 73 references indexed in Scilit:
- PKCδ inhibits PKCα-mediated activation of phospholipase D1 in a manner independent of its protein kinase activityFEBS Letters, 2003
- Dual regulation of phospholipase D1 by protein kinase C α in vivoBiochemical and Biophysical Research Communications, 2002
- Mutations of the BRAF gene in human cancerNature, 2002
- Protein kinase Cδ controls self-antigen-induced B-cell toleranceNature, 2002
- The Hallmarks of CancerCell, 2000
- Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation.The Journal of cell biology, 1996
- Differential Down-Regulation of Protein Kinase C Subspecies in Normal Human Melanocytes: Possible Involvement of the ζ Subspecies in Growth RegulationJournal of Investigative Dermatology, 1995
- Modulation of Human Melanoma Cell Metastasis and Adhesion May Involve Integrin Phosphorylation Mediated Through Protein Kinase CBiochemical and Biophysical Research Communications, 1994
- Alterations in Gene Expression and Signal Transductions in Human Melanocytes and Melanoma CellsCritical Reviews™ in Oncogenesis, 1994
- Failure of wild-type or a mutant form of protein kinase C-α to transform fibroblastsNature, 1991