EVENT PARTNERS AND SPEAKERS
Federal Ministry of Education and Research AGeNT-D
Nokia Technology Academy Foundation
The Millennium Technology Prize Chinano
Carl Zeiss Shell International Exploration and Production
Daimler BASF - The Chemical Company
Bayer Material Science Lux Research
Saudi Aramco Bax & Willems Consulting Venturing
Thermo Fisher Scientific Nanotechnologie
Hessen-Nanotech NMN
ENNaB INM
CC NanoChem Upob
INCH CeNTech GmbH
NanOP NanoBioNet
NanoMat
GOLD MEDIA PARTNER
MATCHMAKING PARTNER
Technology Review Enterprise Europe Network
GLOBAL PARTNER
OFFICIAL AIRLINE
nano tech 2010 Lufthansa – German Airlines
CO-ORGANISER
LEAD ORGANISER
TU Berlin Spinverse Consulting


Cancer crusade-use of nano-targetted delivery of CaMK II in specific lung epithelial cells of the lung

Sri Harsha Meghadri (1), Rohit Radhakrishnan (1)

1 Rajalakshmi Engineering College, India 

Abstract
Nanotechnology holds the key for crusade against lung cancer, which is a prominent disease amongst varied age groups. This article gives a brief hypothesis on cancer cure using fullerene C60 or Colloidal Gold nano-particles for targeting CamKII towards cancer cells. p53 (also known as protein 53 or tumor protein 53), is a transcription factor encoded by the TP53 gene. p53 is important in multicellular organisms, where it regulates the cell cycle and thus functions as a tumor suppressor that is involved in preventing cancer. When the p53 is bound to certain proteins for e.g.MMD2 protein gets nonfunctional which leads to cancer and tumor.Pirh2, a gene regulated by p53 that encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase activity. Pirh2 physically interacts with p53 and promotes ubiquitination of p53 independently of Mdm2. Expression of Pirh2
decreases the level of p53 protein and abrogation of endogenous Pirh2 expression increases the level of p53. Phosphorylated Pirh2 is far more unstable than its unphosphorylated form. Calmodulin-dependent kinase II (CaMK II) phosphorylates Pirh2 on residues Thr-154 and Ser-155. Phosphorylation of Pirh2 appears to be regulated through cell cycle-dependent mechanism. CaMK II-mediated Pirh2 phosphorylation abrogates its E3 ligase activity toward p53.This Pirh2 expression was higher in 27 of 32 (84 percent) of human lung cancers. Thus, by using specifically targeted nano-particles containing CaM KII encapsulated to the lung epidermal cells the ligase activity of Pirh2 can be effectively tackled thereby improving the levels of p53 protein.