Accession Number ADA570588
Title Identification of New Substrates for Breast Tumor Specific LMW Cyclin E/CDK2 Kinase.
Publication Date Sep 2012
Media Count 18p
Personal Author S. Akli
Abstract Cyclin E overexpression occurs in 25% of breast cancer tumors and is linked to poor prognosis. In tumor cells full length cyclin E (FL-E) is processed by an elastase-like protease into low-molecular weight isoforms (LMW-E) that are biochemically hyperactive. We recently demonstrated in a transgenic mouse model that CDK2 is required for LMW-E-induced breast cancer. The hypothesis is that the biological and biochemical differences between FL-E and LMW-E may be due to the phosphorylation of a distinct set of substrates when complexed with CDK2. The Protoarray analysis led us to discover Hbo1 and CINP as novel substrates of the LMW-E/CDK2 complex that may mediate critical downstream signaling to contribute to the oncogenic potential of LMW-E in breast cancer. We will pursue the identification of new substrates by phosphorylating a cell lysate in vitro with cyclin EL/CDK2 (F80G) and cyclin ELMW/ CDK2 (F80G) and PE-ATP-(gamma)-S. The identification of new physiological LMW-E/CDK2 substrates will lead to the development of novel targets for therapeutics and the identification of the biological function for the treatment of the aggressive LMW-E expressing triple negative breast cancer.
Keywords Biochemistry
Breast cancer
Cells(Biology)
Neoplasms
Phosphorylation
Substrates
Transcription(Genetics)


 
Source Agency Non Paid ADAS
NTIS Subject Category 57E - Clinical Medicine
57F - Cytology, Genetics, & Molecular Biology
Corporate Author M.D. Anderson Cancer Center, Houston, TX.
Document Type Technical report
Title Note Final rept. 1 Sep 2010-31 Aug 2012.
NTIS Issue Number 1315
Contract Number W81XWH-10-1-0815

Science and Technology Highlights

See a sampling of the latest scientific, technical and engineering information from NTIS in the NTIS Technical Reports Newsletter

Acrobat Reader Mobile    Acrobat Reader