Hosmer Chair in Physiology
|Department of Physiology|
McIntyre Medical Sciences Building,
3655 Promenade Sir William Osler
Montréal, Québec H3G 1Y6
alvin [dot] shrier [at] mcgill [dot] ca
Laboratory Lab Site:
Research Area: Cardiovascular Physiology
Ion channels and membrane transporters are key determinants of the initiation and conduction of the cardiac impulse. Moreover, alterations in the function of these membrane proteins due to genetic mutation, disease or drugs can alter their function leading to abnormal cardiac rhythms. The work in my laboratory has been focused on attaining an understanding of ion channel function and localization on one hand and the initiation of complex cardiac rhythms on the other. We are using molecular methods, including yeast two-hybrid screens, and confocal microscopy with immunohistochemistry to identify protein interaction and localization. Using electrophysiological methods, including patch clamp techniques, we determine the functional expression and biophysical properties of channels in heterologous cells and isolated cardiac myocytes. In order to understand the genesis of cardiac rhythms we use optical dyes and a cooled CCD camera system or photodiodes to image the conduction of the cardiac impulse in cultured cardiac myocytes or cardiac tissue. The rhythms generated are analyzed and modeled using nonlinear mathematical techniques. The above approaches are used to study the changes that occur with development, cardiac arrhythmias and disease states, such as cardiac ischemia.
Education: B.Sc., Concordia, Ph.D., Dalhousie
Walker VE, Atanasiu R, Lam H, Shrier A.
Co-chaperone FKBP38 promotes HERG trafficking.
J Biol Chem. 2007 282(32):23509-16.
Han W, Nattel S, Noguchi T, Shrier A.
C-terminal domain of Kv4.2 and associated KChIP2 interactions regulate functional expression and gating of Kv4.2.
J Biol Chem. 2006 281(37):27134-44.
Bub G, Shrier A, Glass L.
Global organization of dynamics in oscillatory heterogeneous excitable media.
Phys Rev Lett. 2005 94(2): 028105.
Akhavan A, Atanasiu R, Noguchi T, Han W, Holder N and Shrier|, A
Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization
Journal of Cell Science 2005 118: 2803-2812
Sherman AJ, Shrier A, Cooper E.
Series resistance compensation for whole-cell patch-clamp studies using a membrane state estimator.
Biophys J. 1999 Nov;77(5):2590-601.
Petrecca K, Atanasiu R, Grinstein S, Orlowski J, Shrier A.
Subcellular localization of the Na+/H+ exchanger NHE1 in rat myocardium.
Am J Physiol. 1999 Feb;276(2 Pt 2):H709-17.
Petrecca K, Atanasiu R, Akhavan A, Shrier A.
N-linked glycosylation sites determine HERG channel surface membrane expression. J Physiol (Lond). 1999 Feb 15;515 ( Pt 1):41-8.
Bub G, Glass L, Publicover NG, Shrier A.
Bursting calcium rotors in cultured cardiac myocyte monolayers.
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):10283-7.
Paquette T, Clay JR, Ogbaghebriel A, Shrier A.
Effects of divalent cations on the E-4031-sensitive repolarization current, I(Kr), in rabbit ventricular myocytes.
Biophys J. 1998 Mar;74(3):1278-85.