Cancer cell proliferation in H4IIE rat hepatoma cells expressing a PKC-delta knockdown

CHED 788

Jason T Henderson1, Mary Ruhoff2, Dr. Andrew Piefer1, and Dr. Michael Greene2. (1) Department of Chemistry, Hartwick College, Oneonta, NY 13820, (2) The Research Institute, Mary Imogene Bassett Hospital, Cooperstown, NY 13326
A kinase is a type of enzyme that transfers phosphate groups from high-energy donor molecules, such as ATP, to specific substrates. Protein Kinase C is part of the serine/threonine protein kinase family, and is vital to signaling pathways that support cell growth. There are 11 isoenzymes of PKC that are divided into three major groups: conventional, novel, and atypical. PKC isoenzymes are categorized into groups based on the molecules that activate the kinase. In this experiment, the isoenzyme PKC-delta was examined in the cancerous rat hepatoma cell line H4IIE. PKC-delta is part of the novel group of PKCs; it is activated by diacylglycerol. Using short hairpin RNA (shRNA) silencing techniques to knockdown the expression of PKC-delta, the growth rate was compared to H4IIE cells expressing a control shRNA. Cell proliferation was quantified and the data was graphed to show the differences in growth rate.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008