Bonnie Blazer-Yost

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https://hdl.handle.net/1805/14068

Dr. Bonnie Blazer-Yost’s primary interest is in epithelial cell biology as it relates to ion transport. Recently she has been investigating treatments for polycystic kidney disease. These studies resulted from a serendipitous finding regarding the potential use of Pioglitazone, a commonly used diabetes drug, in polycystic kidney disease patients. This research has progressed from tissue culture, through preclinical animal models and is currently funded as an initial clinical trial in polycystic kidney disease patients.

Dr. Blazer-Yost and her team are also researching potential treatments for hydrocephalus or “water on the brain.” Hydrocephalus may develop as a consequence of trauma, infection, tumors, intracranial hemorrhage or as a result of a congenital birth defect. Elderly patients may suffer from a poorly understood and underdiagnosed form called “normal pressure hydrocephalus,” characterized by urinary incontinence, gait instability, and dementia. Post-traumatic hydrocephalus occurs as the result of traumatic brain injury. Regardless of the form, brain surgery is currently the only effective long-term treatment. Dr. Blazer-Yost and her collaborators recently obtained a three-year Department of Defense grant to conduct translational studies in animal models with a goal of developing a drug treatment for hydrocephalus.

Dr. Blazer-Yost’s work to treat polycystic kidney disease and hydrocephalus is another example of how IUPUI faculty are TRANSLATING RESEARCH INTO PRACTICE.

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Browsing Bonnie Blazer-Yost by Subject "Animals"

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    Vasopressin Regulates the Phosphorylation State of AMP-activated Protein Kinase (AMPK) in MDCK-C7 Cells
    (2008) Nofziger, Charity; Kalsi, Kameljit; West, T. Aaron; Baines, Deborah; Blazer-Yost, Bonnie
    AMP-activated protein kinase (AMPK) is a regulatory kinase coupling cellular metabolism with ion transport. Madin-Darby Canine Kidney-Clone 7 (MDCK-C7) cells possess characteristics of the renal principal cell type, express the cystic fibrosis transmembrane regulator and the epithelial Na(+) channel, and display NPPB and amiloride-sensitive transepithelial transport when stimulated with [Arg(8)]-vasopressin. [Arg(8)]-vasopressin binding to its receptor on the basolateral membrane of MDCK-C7 results in cAMP production, activation of cAMP-dependent protein kinase A (PKA), and increases in Cl(-) and Na(+) transport. Ussing-style electrophysiology showed that the PKA inhibitor, H89, blocked Cl(-) and Na(+) transport. Unexpectedly, [Arg(8)]-vasopressin stimulation resulted in the dephosphorylation of pAMPK(thr172). H89 did not prevent this, suggesting that the dephosphorylation is independent of PKA. 24 hour, but not 15 minute, incubation with the AMPK activator, AICAR, also blocked [Arg(8)]-vasopressin-stimulated currents. Contrary to previous studies, immunoblotting revealed that AICAR did not increase abundance of the active, phosphorylated form of AMPK (pAMPK(thr172)); although, AICAR treatment significantly blocked [Arg(8)]-vasopressin -stimulated cAMP production. [Arg(8)]-vasopressin still caused pAMPK(thr172) dephosphorylation in the presence of AICAR, suggesting that this effect is also independent of cAMP. In summary, these data suggest [Arg(8)]-vasopressin regulates AMPK phosphorylation and that AICAR inhibits ion transport independently of AMPK in MDCK-C7 cells.