|
Contact
information:
Telephone: (514) 398-7290
e-mail address:
michel.tremblay@mcgill.ca
website:
http://www.mcgill.ca/biochemistry/department/faculty/tremblay/
http://www.medicine.mcgill.ca/cancer/tremblay.htm
http://www.medicine.mcgill.ca/oncology/displayoncology.asp?Oncology_ID=32
Projects for Thesis
Supervision:
1. The PTP 1b enzyme is a
tyrosine phosphatase that controls several signaling events in diabetes
and obesity. In order to understand which tissue/organ is responsible
for the protection caused by the PTP1b inhibition, several transgenic
animals expressing a dominant negative mutant of PTP1b in different
tissues will be generated and characterized.
2. PTP-PEST is a tyrosine
phospatase that controls the polymerization of actin. Several signaling
molecules interact with the PTP to control cell movement. Using a
proteomic approach we will purify large amounts of the PTP protein
complex to isolate and identify these associated proteins.
3. We have recently generated
inhibitors of PTP with the intent to treat diabetes mouse models. These
inhibitors must be studied by informatics docking and by NMR studies.
The end point of this study is the development of lead compounds for
preclinical trials and for their use in mouse rodent models.
Recent
Publications:
Dube N, A Cheng and
ML Tremblay.
The role of protein tyrosine phosphatase 1B in ras signaling. Proc.
Natl. Acad. Sci. (USA) 101: 1834-1839, 2004.
Persson C, C Savenhed, A
Bourdeau, ML Tremblay, B. Markova,
FD Bohmer, FG Haj, BG Neel, A Elson, C-H Heldin, L Ronnstrand, A Ostman
and C Hellberg.
Site-selective regulation of platelet-derived growth factor b-receptor
tyrosine phosphorylation. Mol. Cell. Biol. 24: 2190-2201, 2004.
Thompson KM, N. Uetani, C.
Mannitt, M. Elchebly, ML Tremblay
and TE Kennedy.
Receptor protein tyrosine phosphatase sigma inhibits axonal regeneration
and the rate of axon extension. Mol. Cell. Neuroscience 4:
681-692, 2003.
|
