Chapter 8 Manipulation of PKC Isozymes by RNA Interference and Inducible Expression of PKC Constructs

Alakananda Basu, Shalini D. Persaud, Usha Sivaprasad

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

1 Scopus citations

Abstract

Protein kinase C (PKC), a family of serine/threonine kinases, plays an important role in apoptosis. Several members of the PKC family act as substrates for caspases. In addition, PKCs can also regulate caspase activation and cell death by apoptosis. The cleavage of PKCs separates the regulatory domain from the catalytic domain. The full-length, the catalytic domain, and the regulatory domain of PKC family members may have distinct function in apoptosis. Delineating the role of protein kinase C (PKC) isozymes in apoptosis has been challenging because of the lack of selective inhibitors of PKC isozymes and difficulty in generating stable cell lines expressing pro-apoptotic PKC isozymes. In this chapter, we describe the use of RNA interference (siRNA) technology and tetracycline-inducible expression of PKC isozymes to study their function in apoptosis.

Original languageEnglish
Title of host publicationProgrammed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B
EditorsRoya Khosravi-Far, Zahra Zakeri, Richard Lockshin, Mauro Piacentini
Pages141-157
Number of pages17
DOIs
StatePublished - 2008

Publication series

NameMethods in Enzymology
Volume446
ISSN (Print)0076-6879

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