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Mark Wallert

Mark Wallert Professor, Chair


Mark joined the Biology Department as Associate Professor Fall Semester 2015. Prior to coming to BSU, he was a Professor in the Biosciences Department at Minnesota State University for 25 years. Mark’s research focuses on the regulation of tumor development and metastasis in non-small cell lung cancer (NSCLC) and ovarian cancer. The Wallert Cancer Research Team currently has projects in four specific areas (see Research Interests below). Mark is the Northwest Regional Director for the American Society of Biochemistry and Molecular Biology Student Chapters Steering Committee where he has helped organize the Undergraduate Research in the Molecular Sciences annual meeting held in Moorhead, Minnesota for the past 11 years. In 2005, Mark was recognized as the Council for Advancement and Support of Education / Carnegie Foundation for the Advancement of Teaching Minnesota College Professor of the Year.


Postdoctoral Fellow, Pharmacology, Mayo Clinic

Ph.D. Physiology, Emory University

Bachelor of Arts, Biology and Chemistry, Southwest Minnesota State University


Fall Semester 2020

  • Biol 1400: Cellular Principles
  • Biol 3590/5590: Cell Biology and Laboratory
  • Biol 4470/5470: Introduction to Vaccinology
  • Biol 4894: Advanced Research Project I

Spring Semester 2021

  • BCMB 1000: Biochemistry, Cellular and Molecular Biology Careers
  • Biol 2360: Genetics
  • Biol 3260/5260: Human Physiology
  • Biol 4360/5360: Developmental and Tumor Biology
  • Biol 4895: Advanced Research Projects II

Research Interests

The Wallert Cancer Research Team investigates the function and regulation of a transmembrane, transport protein, the sodium-hydrogen exchanger isoform 1 (NHE1). Our research aims to define the normal regulation of NHE1 as well as dysregulation that occurs in disease states such as cancer and lung fibrosis. Our goal is to define a mechanism to use NHE1 as a therapeutic target for the treatment of these diseases.

Our investigations have four distinct avenues:

  1. The role of Calcineurin B Homologous Proteins Isoforms 1 and 2 (CHP1 and CHP2) in the development and progression of disease. The development of pathophysiologies including fibrosis and cancers involve the establishment of a tissue microenvironment characterized by hypoxia and low serum conditions. This project will investigate the role three proteins in the cellular response to these changes in tissue microenvironment; they are the: 1) sodium hydrogen exchanger isoform 1(NHE1), 2) calcineurin B homologous protein isoform 1 (CHP1), and 3) calcineurin B homologous protein isoform 2 (CHP2). The overarching goal of our proposal is to understand the regulation of cellular functions by CHP1, CHP2 and NHE1.
  2. The Role of NHE1 in the development and progression of Ovarian Cancer. Virtually all current ovarian cancer therapies have initial success but then recur as the cancer cells develop resistance to these therapies. We hypothesize that for these drug resistant cancers, the use of NHE1 inhibitors or inhibitors of the protein kinases that regulate NHE1 activity may provide a mechanism to overcome this resistance. This project focuses on characterizing the role of NHE1 in ovarian cancer and mechanisms we can use to target NHE1 transport activity as an adjuvant therapy for ovarian cancer treatment.
  1. The Regulation of Cell Function through the Phosphorylation and Palmitoylation of NHE1. S-palmitoylation of proteins is a post-translational modification in which C16 saturated palmitic acid is added via a thioester linkage to a cysteine residue. Protein phosphorylation is a post-translational modification in which a phosphate group is added to specific amino acids (Commonly Serine, Threonine, or Tyrosine) by a protein kinase. Our hypothesis is that NHE1 contains a distinct pattern of phosphorylation and palmitoylation in response to specific cellular stimuli. We propose that specific modification patterns will uniquely affect NHE1 function.
  1. The Role of NHE1 in the Development of Pulmonary Fibrosis. The Role of NHE1 in the Development and Progression of Pulmonary Fibrosis. Pulmonary fibrosis is a chronic, progressive lung disease characterized by extensive tissue remodeling leading to reduced respiratory function. The normal response to damage in the lung tissue is to increase recruitment and proliferation of fibroblasts, leading synthesis of extracellular matrix (ECM) proteins such as collagen. Upregulation of NHE1 is known to support increased cell proliferation and migration, suggesting that it may play a role in the behavior of fibroblast cells in pulmonary fibrosis. The overarching goal for this project is to determine whether the proliferation, myofibroblast differentiation, and collagen deposition of fibroblast cells are NHE1-dependent

Recent Work

Mark A. Wallert, Dan Hastle*, Clarice H. Wallert, Wayne Taylor Cottle*, and Joseph J. Provost. You can never have too many kinases: The sodium hydrogen exchanger isoform 1 regulation by phosphorylation. J. Cell Signal. 2016: 1:121

Wallert M.A, Hammes D.*, Nguyen T.*, Kiefer L.*, Berthelsen N.*, Kern A.*, Anderson-Tiege K.*, Shabb J.B., Muhonen W.W., Grove B.D., Provost J.J.
RhoA Kinase (Rock) and p90 Ribosomal S6 Kinase (p90Rsk) phosphorylation of the sodium hydrogen exchanger (NHE1) is required for lysophosphatidic acid-inducedtransport, cytoskeletal organization and migration. Cell Signaling 2015. 27(3):498-509.

Provost J.J. and Wallert M.A. Inside Out: Targeting NHE1 as an Intracellular and Extracellular Regulator of Cancer Progression. Chemical Biology and Drug Design 2013. 81(1): 85 – 101.

Provost J.J., Rastedt D*., Canine J*., Ngyuen T*., Haak A*., Kutz C. *, Berthelsen N. *, Slusser A*., Anderson K*., Dorsam G., Wallert, M. Urokinase plasminogen activator receptor induced non-small cell lung cancer invasion and metastasis requires NHE1 transporter expression and transport activity. Cellular Oncology 2012 35(2): 95-110

Wallert, M., McCoy, A*, Voog, J*, Rastedt, D*., Taves, J*,, Korpi-Steiner, N*., Canine, J. *, Ngyuen T*., Ngyuen C*., and Provost J.J.. alpha-1 adrenergic receptor-induced cytoskeletal organization and cell motility in CCL39 fibroblasts requires Phospholipase D1. J Cell Biochem. 2011 Oct;112(10):3025-34

Taves* J., Rastedt*, D., Canine* J., Mork D., Wallert, MA. and Provost, J.J. Sodium hydrogen exchanger and phospholipase D are required for alpha(1)-adrenergic receptor stimulation of metalloproteinase-9 and cellular invasion in CCL39 fibroblasts. Arch Biochem Biophys 2008: 477, 60-66.
Sang*, R.S., Johnson*, J.F., Taves*, J., Nyguen*, C., Wallert, M.A., and Provost, J.J.. alpha1-adrenergic receptor stimulation of cell motility requires phospholipase D mediated extracellular signal-regulated kinase activation. Chem Biol Drug Des 2007; 69: 240–250

Provost, J.J., Korp*i N.L. ,. Olmschenk* S.M , Funfar* M, McCoy* A., and Wallert M.A.. Protein Kinase C and Phospholipase Cß Mediate the alpha1-Adrenergic Activation of NHE1 in Chinese Hamster Lung Fibroblasts. Biochemistry and Cell Biology 2005 2. 123-132.

Wallert, M.A., H.L. Thronson*, N.L. Korpi*, S.M. Olmschenk*, A. McCoy*, M. Funfar*, and J.J. Provost. Two G-Protein Coupled Receptors Activate NHE1 in Chinese Hamster Lung Fibroblasts Through an ERK-dependent Pathway. Cellular Signaling 2004. 12: p. 231-242

* Undergraduate Student Authors