DR. MICHAEL P. WALSH

  Ph.D Professor, Department of Biochemistry and Molecular Biology

Affilitaions: Member - Smooth Muscle Research Group.  

 Research Interests:

The molecular basis of myogenic tone in the vasculature (in collaboration with Dr. Bill Cole) - The mechanism of regulation of urethral smooth muscle contraction by Rho-associated kinase. 
 Research in the Walsh laboratory is focused on signal transduction pathways involved in the regulation of smooth muscle contraction and relaxation. Areas of interest include: - Calcium sensitization of smooth muscle contraction - Calcium-independent phosphorylation of myosin - The mechanism of activation of myosin light chain kinase by calcium and calmodulin - The roles of protein kinase C and Rho-associated kinase in phosphorylation and inhibition of myosin light chain phosphatase and the phosphatase inhibitor CPI-17 - Structural and functional characterization of S100A11 (a calmodulin-related calcium-binding protein) and its interaction with the calcium- and phospholipid-binding protein annexin A6 - Regulation of delayed rectifier potassium current in vascular smooth muscle (in collaboration with Dr. Bill Cole) - Development of highly sensitive proteomic methods for the analysis of myosin phosphorylation in the renal microvasculature (in collaboration with Dr. Rodger Loutzenhiser) - The involvement of Rho-associated kinase in the regulation of delayed rectifier potassium channels in vascular smooth muscle (in collaboration with Dr. Don Welsh)

Personnel:

View Pub Med for Recent publications & abstracts

Recent Publications:

• Mita, M., Kuramoto, T., Ito, K., Toguchi-Senrui, N., Hishinuma, S. ,Walsh, M. P. and Shoji, M. (2010) Clin. Exp. Pharmacol. Physiol. 37: 350-357. Impairment of a1-adrenoceptor-mediated contractile activity in caudal arterial smooth muscle from Type 2 diabetic Goto-Kakizaki rats.
• Mita, M., Ito, K., Taira, K., Nakagawa, J., Walsh, M. P. and Shoji, M. (2010) Clin. Exp. Pharmacol. Physiol. DOI: 10.1111/j.1440-1681.2010.05373.x. Attenuation of store-operated Ca2+ entry and enhanced expression of TRPC channels in caudal arterial smooth muscleof type 2 diabetic Goto-Kakizaki rats.
• El-Yazbi, A. F., Johnson, R. P., Walsh, E. J., Takeya, K., Walsh, M. P.and Cole, W. C. (2010) J. Physiol. 588: 1747-1762. Pressure-dependent contribution of Rho kinase-mediated calcium sensitization in serotonin-evoked vasoconstriction of rat cerebral arteries.
• Bultot, L., Horman, S., Neumann, D., Walsh, M. P., Hue, L. and Rider, M. H. (2009) FEBS Lett. 583: 25-28. Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes.
• Luykenaar, K. D., Abd El-Rahman, R., Walsh, M. P. and Welsh, D. G. (2009) Am. J. Physiol. 296: H917-H926. Rho-kinase-mediated suppression of K_DR current in cerebral arteries requires an intact actin cytoskeleton.
• Johnson, R. P., El-Yazbi, A. F., Takeya, K., Walsh, E. J., Walsh, M. P. and Cole, W. C. (2009) Ca²⁺ sensitization via phosphorylation of myosin phosphatase targeting subunit at threonine-855 by Rho kinase contributes to the arterial myogenic response. J. Physiol. 587: 2537-2553.
• Johnson, R. P., El-Yazbi, A. F., Hughes, M. F., Schriemer, D. C., Walsh, E. J., Walsh, M. P. and Cole, W. C. (2009) J. Biol. Chem. 284: 16562-16574. Identification and functional characterization of protein kinase A-catalyzed phosphorylation of potassium channel Kv1.2 at serine 449.  
• Hong, F., Haldeman, B. D., John, O. A., Brewer, P. D., Wu, Y-Y., Ni, S.,Wilson, D. P., Walsh, M. P., Baker, J. E. and Cremo, C. R. (2009) J. Mol. Biol. 390: 879-892. Characterization of tightly associated smooth muscle myosin-myosin light-chain kinase-calmodulin complexes.
• Ihara, E., Moffat, L., Borman, M. A., Amon, J. E., Walsh, M. P. and MacDonald, J. A. (2009) Am. J. Physiol. 297: G361-G370. Ca2+-independent contraction of longitudinal ileal smooth muscle is potentiated by a zipper-interacting protein kinase pseudosubstrate peptide.
Takeya, K., Loutzenhiser, K., Shiraishi, M., Loutzenhiser, R. D. and Walsh, M. P. (2008) Am. J. Physiol. 294: F1487-F1492. A highly sensitive technique to measure myosin regulatory light chain phosphorylation: The first quantification in renal arterioles.
Horman, S., Morel, N., Vertommen, D., Hussain, N., Neumann, D., Beauloye, C., El Najjar, N., Forcet, C., Viollet, B., Walsh, M. P., Hue, L. and Rider, M. H. (2008) J. Biol. Chem. 283: 18505-18512. AMP-activated protein kinase phosphorylates and desensitizes smooth muscle myosin light chain kinase. 
• Gui, Y., Zheng, J., Zheng, X.-L. and Walsh, M. P. (2008) Am. J. Physiol. 295: H1935-H1942. Inhibition of rat aortic smooth muscle contraction by 2-methoxyestradiol
• Gui, Y., He, G., Walsh, M. P., Jankowski, V., Jankowski, J. and Zheng, X.-L. (2008) Am. J. Physiol. 294: L733-L738. Up4A stimulates endothelium-independent contraction of isolated rat pulmonary artery.
• Gui, Y., Yin, H., He, J.-Y., Yang, S., Walsh, M. P. and Zheng, X.-L. (2007) Am. J. Physiol. 292: H1313-H1320. Endoreduplication of human smooth muscle cells induced by 2-methoxyestradiol: a role for cyclin-dependent kinase 2.
• Chang, N., Sutherland, C., Hesse, E., Winkfein, R., Wiehler, W. B., Pho, M., Veillette, C., Li, S., Wilson, D. P., Kiss, E. and Walsh, M. P. (2007) Am. J. Physiol. 292: C1417-C1430. Identification of a novel interaction between the Ca²⁺-binding protein S100A11 and the Ca²⁺- and phospholipid-binding protein annexin A6.
• Ihara, E., Edwards, E., Borman, M., Wilson, D. P., Walsh, M. P. and MacDonald, J. A. (2007) Am. J. Physiol. 292: C1951-C1959. Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide. 
• Corteling, R. L., Brett, S. E., Yin, H., Zheng, X.-L., Walsh, M. P. and Welsh, D. G. (2007) Am. J. Physiol. 293: H440-H447. The functional consequence of RhoA knockdown by RNA interference in rat cerebral arteries.
• Gui, Y., He, G. H., Walsh, M. P. and Zheng, X.-L. (2007) Am. J. Physiol. 293: L702-L711. Predisposition to tetraploidy in pulmonary vascular smooth muscle cells derived from the Eker rats.
• Ihara, E., Moffat, L., Ostrander, J., Walsh, M. P. and MacDonald, J. A. (2007) Am. J. Physiol. 293: G699-G710. Characterization of protein kinase pathways responsible for Ca²⁺ sensitization in rat ileal longitudinal smooth muscle.
• Xiao, B., Tian, X., Xie, W., Jones, P. P., Cai, S., Wang, X., Jiang, D., Zhang, L., Chen, K., Walsh, M. P., Cheng, H. and Chen, S. R. W. (2007) J. Biol. Chem. 282: 30256-30264. Functional consequence of PKA-dependent phosphorylation of the cardiac ryanodine receptor: sensitization of store-overload-induced Ca²⁺ release (SOICR).
• Walsh, M. P., Susnjar, M., Deng, J., Sutherland, C., Kiss, E. and Wilson, D. P. (2007) in Methods in Molecular Biology - Protein Phosphatase Protocols (Moorhead, G., ed.), Vol. 365, pp 209-224, Humana Press, Totowa, USA. Phosphorylation of the protein phosphatase type 1 inhibitor protein, CPI-17, by protein kinase C.
• Gifford, J. L., Walsh, M. P. and Vogel, H. J. (2007) Biochem. J. 405: 199-221. Structures and metal ion-binding properties of the Ca²⁺-binding helix-loop-helix EF-hand motifs.
• Contact Information
  The University of Calgary,
  Room 72B Heritage Medical Research Building,
  3330 Hospital Drive NW,
  Calgary, Alberta
  Canada T2N 4N1
  Phone (403) 220-3021
  Fax: (403) 270-2211
  E-mail: walsh [at] ucalgary [dot] ca.