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Alan S. Mak

 
  Regulation of Smooth Muscle

 
  Contact Information:  
  Professor of Biochemistry
Ph.D., University of Manitoba;
Postdoctoral Fellowship, University of Alberta;
Visiting Scientist, University of Calgary

Tel: (613) 533-2989
Fax: (613) 533-2497
email: maka@post.queensu.ca


 
  Background: Smooth muscle cells are unique that they can be stimulated to de-differentiate and lose their contractile apparatus and become proliferative and migratory. This process is a major contribution to the formation of atherosclerotic plaques which is a major cause of cardiovascular disease.

Research interests: The roles of members of the RhoGTPases (Rho, Rac and Cdc42) and their downstream effector kinases in smooth muscle cell contraction and motility.

  • Structure and function of cytoskeletal proteins (e.g. caldesmon, desmin, cortactin) in the regulation of the cytoskeletal architecture of smooth muscle and non-muscle cells.

Methodology:

  • Biochemical, cell biology and molecular biology techniques are employed in these studies.

  • Protein-protein interaction, protein purification, phosphorylation and chemical modification of proteins, immunochemical assays.

  • Immunofluorescence microscopy, cell motility imaging.

  • Protein expression in bacteria, yeast and insect cells, site-directed and deletion mutations, yeast-two hybrid analyses of protein-protein interactions.



 
  Publications:  
  Foster, D.B., L. Shen, J. Kelly, P. Thibault, J. Van Eyk and A.S. Mak. Phosphorylation of caldesmon by p21-activated kinase: implication for the Ca2+-sensitivity of smooth muscle contraction. J. Biol. Chem. 275:1959.-1965 (2000).

Pelaez, N.J., S.L. Osterhaus, A.S. Mak, Y. Zhao, H.W. Davis and C.S. Packer. MAPK and PKC activity are not required for H2O2-induced arterial muscle contraction. Am. J. Physiol. In Press. (2000

Van Eyk, J.E., D.K. Arrell, D.B. Foster, J.D. Strauss, T.Y. Heinonen, E. Furmaniak-Kazmierczak, G.P. Cote, and A.S. Mak. Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle. J.Biol.Chem. 273:23433-23439 (1998).

Graether, S.P., Heinonen, T.Y.K., Raharjo, W.H., Jin, J.-P. and Mak, A.S. Tryptophan residues in caldesmon are major determinants for calmodulin binding. Biochemistry 36 364-369 (1997).

Zhou, N., Yuan, T., Mak, A.S. and Vogel, H.J. NMR studies of caldesmon-calmodulin interactions. Biochemistry 36:2817-2825. (1997).