Scientific Advisory Board
The Algomedix Scientific Advisory Board is composed of global leaders in TRP biology, pharmacology and medicinal chemistry.
William A. Catterall, Ph.D.
Chair and Professor, Department of Pharmacology, University of Washington
Dr. Catterall and his colleagues at the University of Washington discovered the voltage-gated sodium and calcium channel proteins, which are responsible for generation of electrical signals in the brain, heart, skeletal muscles, and other excitable cells. Their subsequent work has contributed much to understanding the structure, function, regulation, and molecular pharmacology of these key cell-signaling molecules. Dr. Catterall’s recent work has turned toward understanding diseases caused by impaired function and regulation of voltage-gated ion channels, including epilepsy and periodic paralysis.
Dr. Catterrall has received numerous accolades for his research achievements including the 2010 Canada Gairdner Award for “Discovery of the voltage-gated sodium channel and calcium channel proteins and the elucidation of their function and regulation.” Additional recognitions include the Bristol-Myers Squibb Award for Distinguished Achievement in Neuroscience Research in 2003, the McKnight Foundation Senior Neuroscience Investigator Award in 1998, the Mathilde Solowey Award in Neuroscience from the National Institutes of Health and the H.B. Van Dyke Award in Pharmacology from Columbia University in 1995 and the Basic Science Prize of the American Heart Association in 1992. Dr. Catterall’s early research was recognized with the Jacob Javits Neuroscience Investigator Awards in 1984 and 1991 and the Passano Foundation Young Scientist Award in 1981.
Dr. Catterall was elected to the National Academy of Sciences in 1989, where he served as Chair of the Section of Physiology & Pharmacology from 1998 to 2001. He was elected to the Institute of Medicine and the American Academy of Arts & Sciences in 2000, and he was elected as a Foreign Member of the Royal Society of London in 2008. He served as editor-in-chief of Molecular Pharmacology from 1985 to 1990, was a founding member of the editorial board of Neuron in 1988, and has been an editorial board member of numerous other professional journals. Dr. Catterall and his colleagues have published more than 400 research papers and 30 reviews and reference works on voltage-gated ion channels.
Dr. Catterall received his BA degree in Chemistry from Brown University in 1968, his PhD in Physiological Chemistry from Johns Hopkins School of Medicine in 1972, and his postdoctoral training in neurobiology and molecular pharmacology as a Muscular Dystrophy Association Research Fellow with Dr. Marshall Nirenberg at the National Institutes of Health from 1972 to 1974. Following three more years as a staff scientist at the National Institutes of Health, he joined the faculty of the University of Washington School of Medicine in 1977 as an associate professor in the Department of Pharmacology, became professor in 1981, and Chair of the Department of Pharmacology in 1984.
Dr. Stuart Dryer, Ph.D.
University of Houston
Dr. Stuart Dryer’s laboratory studies physiological and pathophysiological processes that occur in the kidney. The current research focuses on the role of ion channels and receptors in the regulation of cells that form the glomerular filtration barrier, and the proximal tubule. The lab has recently focused on a Ca2+-permeable cation channel known as TRPC6. Mutations that cause gain of function in these channels lead to devastating genetic forms of kidney disease. Dryer’s lab is interested in understanding the normal function and regulation of TRPC6 channels, including the factors that activate their gating and abundance at the cell surface. They are also interested in the role of TRPC6 in driving non-genetic forms of glomerular disease.
In a second research program, he has been studying renal NMDA receptors and their role in normal and abnormal physiology. NMDA receptors are best known for their role in synaptic transmission. However, they are also present in many peripheral tissues including the kidney, where their function remains a mystery. The Dryer Lab has recently shown that sustained activation of NMDA receptors in podocytes induces oxidative stress, changes in expression of regulatory proteins, and apoptotic cell death. They have also observed marked up-regulation of NMDA receptors throughout the kidney in mouse models of type 1 diabetes, and have shown that sustained treatment of NMDA antagonists reduces nephropathy in mouse models of type 1 diabetes. They are currently working to understand how NMDA receptors are regulated in normal and diseased kidneys, including understanding the molecules that normally cause them to become active.
Dr. Yasuo Mori
Kyoto University, Japan
Dr. Yasuo Mori is a full professor at Kyoto University, Laboratory of Molecular Biology, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering.
Cells composing living bodies are equipped with many machineries to maintain independence from the external environment. In addition, cells are also prepared to respond to stimulation from extracellular milieu. Needless to say, intracellular and extracellular media are solution containing inorganic ions. Intracellular concentrations of Na+, K+, Ca2+ and Cl- are not equal to those on the extracellular side, and fluctuate in response to various stimuli from the external milieu.
This ambivalence in regard to the relationship with the extracellular environment is a distinctive feature of living cells. Ion channels (pore on plasma membrane carrying ions), transporters and pumps (transporting various substances including inorganic ions) play important roles to control dependence or independence of living cells on extracellular environment. In this division, we focus on ion channels.
Among various inorganic ions, Ca2+ is particularly important triggering diverse biological functions such as muscle contraction and neurotransmitter release.Ca2+ is known to regulate cellular HOMEostasis such as cell proliferation, survival and death as well. Intracellular Ca2+ concentration is quite low before stimulation (nM levels), but once cells are stimulated, it increases to mM levels. How does Ca2+ influx occur in the Ca2+ cellular responses to increase intracellular Ca2+ concentration? Now it is believed that influx occurs via Ca2+ channel across plasma membrane from extracellular media where extracellular Ca2+ concentration is 1-2 mM. Ca2+ channels are diverse, including voltage-dependent Ca2+ channels gated by electrical potential difference across the plasma membrane, and receptor-mediated Ca2+ channels activated by inositol metabolites and other cellular messengers.
Dr. Palmer Taylor
UCSD School of Medicine
Dr. Taylor’s studies have employed spectroscopic physical methods, X ray crystallography, sequence and three dimensional structural determinations to investigate the principles of molecular recognition. He has worked with nicotinic acetylcholine receptors and acetylcholinesterase since the mid-1970’s with current interests directed to structure and dynamics as they relate to ligand design. For acetylcholinesterase (AChE), reactivating antidotes to organophosphate nerve agent and insecticide exposure are designed to confer oral bioavailability and CNS reactivation capabilities. These studies evolved from collaboration with Barry Sharpless of TSRI using AChE as the first target template for freeze-frame, click chemistry to synthesize in situ selective cholinesterase inhibitors and reactivator antidotes. Collaborative studies with nicotinic receptors also employ click-chemistry in structure- guided drug design. In this case, a soluble surrogate for the extracellular domain of the nicotinic receptor is used as the template for the in situ synthesis of novel nicotinic receptor ligands directed to the α7 subtype. More recently, Taylor has conducted studies into the structure and function of a post-synaptic adhesion protein homologous to AChE, neuroligin, and its pre- synaptic partner, neurexin. Studies employ both crystallographic and solution-based techniques and are directed to macromolecular recognition of ectodomain adhesion molecules.
Dr. Michael Zhu
UT Health Science Center
Dr. Michael X. Zhu is a professor at The University of Texas Health Science Center at Houston, McGovern Medical School, Department of Integrative Biology and Pharmacology. His focus is on understanding how Calcium ions (Ca2+) play a critical role in cell functions ranging from secretion, contraction, to gene expression and programmed cell death. Our research focuses on understanding mechanisms regulating stimulus-evoked intracellular Ca2+ increases and their physiological implications. One area of our research includes functional characterizations of Transient Receptor Potential (TRP) channels. This novel family of ion channels includes ~28 members with diverse functions in mammalian species and they generally serve as sensors for environmental changes inside and outside cells. We focus on studying the roles of TRP channels in Ca2+ signaling and their regulation by Ca2+. We also study the mechanism of regulation and physiological functions of a number of TRP channels including TRPCs, TRPV1, TRPV3, TRPA1, and TRPM8. Some of these channels are involved in pain sensing, especially inflammatory pain. In addition, we aim to identify chemical ligands of therapeutic values for some TRP channels. In a separate study, we investigate molecular mechanism of Ca2+ release from acidic organelles (endosomes and lysosomes). We recently identified two-pore channels (TPC1, TPC2, and TPC3) as receptors for the potent Ca2+ mobilizing messenger, nicotinic acid adenine dinucleotide phosphate (NAADP), expressed in membranes of endolysosomes. We aim to illustrate the roles of two-pore channels and NAADP signaling in overall Ca2+ handling and of endolysosomal Ca2+ regulation in animal cells.