Cloning and Expression Analysis of Protein Kinase C Alpha Isolated from MCF7 Cell Line

Protein kinase C (PKC) is a group of phospholipid-dependent serine/threonine kinases, which is often additional divided into three PKC isozymes subfamilies conventional, novel, and atypical. PKC isozymes are recognized to participate in cell proliferation, living expenses, invasion, migration, apoptosis, angiogenesis, as well as drug resistance. PKC isozymes are essential signal transducers associated with natural physiology and disease and have been dramatically implicated in cancers development. Enhanced PKC activity in malignant breast tissue and real correlations between PKC activity and expression of a much more excessive phenotype in breast cancer cell lines propose an activity on this signal transduction pathway in the pathogenesis and/or development of breast cancer. Resulting from their fundamental functions in cell signaling, PKC isozymes include the possibilities to be potential therapeutic objectives for several diseases. The current investigation aimed to monitor the impact of fever-range hyperthermia on human breast cancer cell line MCF7 considering cell viability and proliferation. MCF7 breast adenocarcinoma cell line were evaluated after subjected to 37C and 40C, cell viability, cell proliferation, and apoptosis was determined. MCF7 showed reduction in the proliferation activity combined with increasing in PKC expression after exposing to fever range hyperthermia. Point mutation were determined using the PKC gene sequence analysis and revealed a missense mutation in the kinase domain converted a conserved hydrophobic amino acid isoleucine into polar threonine that proved its effect on function alternation from suppression to promotion for the proliferation of the MCF7 breast adenocarcinoma cell line.