Ronald M Lynch, PhD

Professor, Physiology

Associate Professor, Pharmacology

Professor, BIO5 Institute

Director, Aribi Institute

Professor, Biomedical Engineering

Professor, Physiological Sciences - GIDP

Associate Director, Shared Resources

rlynch@u.arizona.edu

Links

Department Profile

NCBI Bibliography

Dr. Lynch received a Ph.D. in Physiology and Biophysics from the University of Cincinnati (1984) followed by postdoctoral training at the NIH in Cardiac Energetics. In 1987 Dr. Lynch moved to the Biomedical Imaging Group at the University of Massachusetts Medical Center then joined the University of Arizona in 1990 where he is Professor of Physiology with a joint appointments in Pharmacology and Biomedical Engineering, and is the Director of the Arizona Research Institute for Biomedical Imaging. Dr. Lynch is a member of the American Diabetes Association Grant Review Committee and is a Councilor for the American Physiological Society with service on other national grant and journal review committees.

Cancer Focus

Research in the Lynch lab is focused on the coupling of metabolism and second messenger signaling in nutrient sensing and cancer cells. Analyses of subcellular protein distributions, second messenger signaling, and ligand binding is performed using state of the art microscopy and analysis approaches. For the past 30 years, we have developed unique microscopic imaging and spectroscopy tools to study cell and tissue function, as well as screening assays for cell signaling and ligand binding.

Research Program Role

Clinical and Translational Oncology Program

Display Name

Ronald M Lynch, PhD

Publications

Trigonal scaffolds for multivalent targeting of melanocortin receptors.

Elshan NGRD, Jayasundera T, Anglin BL, Weber CS, Lynch RM, Mash EA. 2015. Trigonal scaffolds for multivalent targeting of melanocortin receptors. Org Biomol Chem. 13:1778–91. doi:10.1039/c4ob02094d.

Preventing the autophagic survival response by inhibition of calpain enhances the cytotoxic activity of bortezomib in vitro and in vivo.

Escalante AM, McGrath RT, Karolak MR, Dorr RT, Lynch RM, Landowski TH. 2013. Preventing the autophagic survival response by inhibition of calpain enhances the cytotoxic activity of bortezomib in vitro and in vivo. Cancer Chemother Pharmacol. 71:1567–76. doi:10.1007/s00280-013-2156-3.

Heterobivalent ligands target cell-surface receptor combinations in vivo.

Xu L, Josan JS, Vagner J, Caplan MR, Hruby VJ, Mash EA, Lynch RM, Morse DL, Gillies RJ. 2012. Heterobivalent ligands target cell-surface receptor combinations in vivo. Proc Natl Acad Sci U S A. 109:21295–300. doi:10.1073/pnas.1211762109.

Design, synthesis, and biological studies of efficient multivalent melanotropin ligands: tools toward melanoma diagnosis and treatment.

Brabez N, Lynch RM, Xu L, Gillies RJ, Chassaing G, Lavielle S, Hruby VJ. 2011. Design, synthesis, and biological studies of efficient multivalent melanotropin ligands: tools toward melanoma diagnosis and treatment. J Med Chem. 54:7375–84. doi:10.1021/jm2009937.

Mitochondrial-mediated disregulation of Ca2+ is a critical determinant of Velcade (PS-341/bortezomib) cytotoxicity in myeloma cell lines.

Landowski TH, Megli CJ, Nullmeyer KD, Lynch RM, Dorr RT. 2005. Mitochondrial-mediated disregulation of Ca2+ is a critical determinant of Velcade (PS-341/bortezomib) cytotoxicity in myeloma cell lines. Cancer Res. 65:3828–36. doi:10.1158/0008-5472.CAN-04-3684.

Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells.

Martinez-Zaguilan R, Lynch RM, Martinez GM, Gillies RJ. 1993. Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells. Am J Physiol. 265:C1015–29. doi:10.1152/ajpcell.1993.265.4.C1015.