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Robin L. Maser, Ph.D.

Robin Maser portrait
Professor, Clinical Laboratory Sciences
rmaser@kumc.edu

Professional Background

Robin Maser, Ph.D., directs graduate courses in molecular biotechnology, molecular techniques and its associated laboratory component.

In addition to teaching in the Department of Clinical Laboratory Sciences as professor, Maser also holds a joint appointment in the Department of Biochemistry and Molecular Biology in the KU School of Medicine. She also produces novel studies in the area of polycystic kidney disease (PKD) – her work intersecting with KU Medical Center's Jared Grantham Kidney Institute.

Academic Background
Maser earned a bachelor's degree in biology and chemistry from William Jewell College in Liberty, Missouri, in 1980. She obtained her doctoral and postdoctoral training in biochemistry and molecular biology from the University of Kansas.

Education and Training
  • BA, Biology and Chemistry, William Jewell Colllege, Liberty, Missouri
  • PhD, Biochemistry and Molecular Biology, University of Kansas, Kansas City, Kansas
  • Post Doctoral Fellowship, Mapping RNA:RNA Interactions, University of Kansas Medical Center, Kansas City, Kansas
  • Post Doctoral Fellowship, Gene Expression in Polycystic Kidney Disease, University of Kansas Medical Center, Kansas City, Kansas
Professional Affiliations
  • American Society of Nephrology, Member, 1995 - Present

Research

Overview

The principal investigator of the Maser Lab, her research is centered on understanding the pathobiology of polycystic kidney disease. In particular, Maser and her team are investigating the structure-function relationships of the protein polycystin-1, product of the PKD1 gene that is most commonly mutated in those with polycystic kidney disease.

They are also interested in the potential role that oxidant stress may play in the pathogenesis of this disease and the role of polycystin-1 in responding to mechanical stimili.

Publications
  • Maser, R., L, Calvet, J., P. 2020. Adhesion GPCRs as a paradigm for understanding polycystin-1 G protein regulation.. Cellular signalling, 72, 109637
  • Maser, R., L, Magenheimer, B., S, Calvet, J., P. 2019. Metanephric organ culture.. Methods in cell biology, 153, 169-183
  • Parnell, S., C, Magenheimer, B., S, Maser, Robin., L, Pavlov, T., S, Havens, M., A, Hastings, M., L, Jackson, S., F, Ward, C., J, Peterson, K., R, Staruschenko, A, Calvet, James., P. 2018. A Mutation Affecting Polycystin-1 Mediated Heterotrimeric G-Protein Signaling Causes PKD.. Human Molecular Genetics, 27 (19), 3313-3324
  • Nims, N., M, Vassmer, D, Maser, Robin., L. 2011. Effect of PKD1 gene missense mutations on polycystin-1 membrane topogenesis.. Biochemistry, 50 (3), 349-55
  • Maser, R., L, Magenheimer, B., S, Zien, C., A, Calvet, J., P. 2003. Transient transfection assays for analysis of signal transduction in renal cells.. Methods in molecular medicine, 86, 205-17
  • Nims, N, Vassmer, D, Maser, Robin., L. 2003. Transmembrane domain analysis of polycystin-1, the product of the polycystic kidney disease-1 (PKD1) gene: evidence for 11 membrane-spanning domains.. Biochemistry, 42 (44), 13035-48
  • Parnell, S., C, Magenheimer, B., S, Maser, Robin., L, Zien, C., A, Frischauf, A., M, Calvet, J., P. 2002. Polycystin-1 activation of c-Jun N-terminal kinase and AP-1 is mediated by heterotrimeric G proteins.. The Journal of Biological Chemistry, 277 (22), 19566-72
  • Maser, Robin., L, Vassmer, D, Magenheimer, B., S, Calvet, J., P. 2002. Oxidant stress and reduced antioxidant enzyme protection in polycystic kidney disease.. Journal of the American Society of Nephrology (JASN), 13 (4), 991-9
  • Parnell, S., C, Magenheimer, B., S, Maser, Robin., L, Rankin, C., A, Smine, A, Okamoto, T, Calvet, J., P. 1998. The polycystic kidney disease-1 protein, polycystin-1, binds and activates heterotrimeric G-proteins in vitro.. Biochemical and Biophysical Research Communications, 251 (2), 625-31
  • Maser, Robin., L, Magenheimer, B., S, Calvet, James., P. 1994. Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion.. The Journal of Biological Chemistry, 269 (43), 27066-73