Office: 1011 Ag & Life Sciences Bldg
Telephone: (541) 737-8867
Fax: (541) 737-4371
Email Address: joe.beckman@oregonstate.edu
Mailing/Express Delivery Address:
Joseph Beckman, Ph.D.
Environmental Health Sciences Center
Oregon State University
1011 Ag & Life Sciences Bldg
Corvallis, OR 97331-7302
| 1975 | B.A., Molecular Biology (Cum Laude), University of Colorado, Boulder, CO |
| 1977 | M.A., Population Biology, University of Colorado, Boulder, CO |
| 1984 | Ph.D., Plant Physiology and Biochemistry, Duke University, Durham, NC |
| 1978 | Administrative Officer, 665th Medical Detachment (Dental), US Eighth Army, Seoul, Korea |
| 1979 | Company Commander, Co. D, 1st Battalion, Academy of Health Sciences, Fort Sam Houston, Texas |
| 1979-1991 | Captain, Medical Service Corps, US Army Reserve |
| 1984 | Research Associate, Department of Pulmonary Medicine, Duke University, Durham, NC |
| 1985 | Research Instructor, Department of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL |
| 1988 | Assistant Professor, Department of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL |
| 1992 | Associate Professor, Department of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL |
| 1994 | Professor, Departments of Anesthesiology, Biochemistry and Molecular Genetics, and Neurobiology, University of Alabama at Birmingham, Birmingham, AL |
| 1995 | Guest Professor, ETH Swiss Federal Institute of Technology, Zürich |
| 2000 | Guest Professor, Universität Konstanz, Germany |
| 2001-present | Principal Investigator, Ava Helen Pauling Chair, Linus Pauling
Institute Professor, Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon (OR) |
| 2002-present | Director, Environmental Health Sciences Center |
| 2003-08 | NIH P01 AT002034 "CER on CAM Antioxidant Therapies (CERCAT)", Project Leader "CAM Antioxidants and ALS" |
| 2005-06 | ALS Association "Measuring Copper, Zinc, and Cysteine Oxidation of SOD1 in ALS Mice and Rats" |
| 2007-10 | ALS Association "Relating Superoxide with Zinc Deficiency of SOD1 in ALS Rats and Mice" |
| 2008-13 | NIH P01 AT002034 "CER on CAM Antioxidant Therapies (CERCAT)", Project Leader "CAM Antioxidants in Amyotrophic Lateral Sclerosis" |
| 2008-13 | NIH R01 NS058628 "Superoxide Dismutase, Peroxynitrite and ALS" |
The first major project in the laboratory is aimed at understanding how oxidative stress, superoxide dismutase and zinc are involved in Lou Gehrig's disease, also known as amyotrophic lateral sclerosis (ALS). ALS is a dreadful disease killing about 5,000 Americans each year. The disease is caused by the unexplained death of motor neurons in the spinal cord. These neurons control the movement of all voluntary muscles. As more and more motor neurons die, the victim's muscles progressively atrophy and they become paralyzed. Mutations to an antioxidant enzyme called superoxide dismutase are the only known cause of ALS. Our research indicates that the loss of zinc from superoxide dismutase is what causes motor neurons to die in ALS. This gives us a chemical target to develop new treatments in the laboratory. One compound we have identified by cell culture tests is also the most protective compound yet identified in animal models of ALS. We are using powerful new tools involving rapid molecular evolution to derive novel proteins that will inactivate zinc-deficient superoxide dismutase. We have developed new methods that robots can use to rapidly screen hundreds of thousands of existing drugs and other compounds, including dietary constituents, for therapeutic benefits. We are characterizing how zinc is handled in motor neurons and why superoxide dismutase can become zinc deficient in ALS. Our goal is to understand how superoxide dismutase causes ALS and to find new ways to stop the disease.
The second major project in the laboratory focuses on the roles of nitric oxide, peroxynitrite and nitrotyrosine in human disease. The major function of superoxide dismutase is to scavenge the oxygen radical superoxide. We discovered that a major target for superoxide is nitric oxide. Until fifteen years ago, nitric oxide was only considered as a toxic air pollutant, damaging the lung and promoting cancer by damaging DNA. However, nitric oxide is also produced by cells lining the arterial walls to relax the underlying smooth muscle and increase blood flow. For example, nitric oxide is the active metabolite produced from nitroglycerin that stops angina in heart disease patients. Viagra works by prolonging the effects of nitric oxide in blood vessels in the penis to maintain erections. Nitric oxide also has a "dark side" and, following reaction with superoxide to produce the powerful oxidant peroxynitrite, can promote oxidative damage to blood vessels, skin, heart, lung, kidney and brain. We are characterizing the role of peroxynitrite in injuring cells and how cells respond to this damage. One sign of damage left by peroxynitrite is nitration of amino acids in proteins. We have identified a variety of such proteins modified in tissues. We hypothesize that nitration is particularly important as a defense against viral infections, damaging proteins and RNA necessary for viral replication, but at the same time can be damaging to host tissues and cells, thereby contributing to acute injury and chronic disease.
Free Radical Biology & Medicine
Archives Biochemistry and Biophysics
Chemical Research in Toxicology
Regular Reviewer, NIH NSPA (1996-2000)
Regular Reviewer, NIH NLS-3 (1993-1996)
Ad Hoc Reviewer, NIH SBIR
The Oxygen Society
American Society of Biochemistry and Molecular Biology
Society for Cerebral Blood Flow and Metabolism
Scientific Advisor to International Nitric Oxide Society
Scientific Advisor to the Muscular Dystrophy Association ALS Group
Barbeito AG, Martinez-Palma L, Vargas MR, Pehar M, Mañay N, Beckman JS, Barbeito L, Cassina P. Lead exposure stimulates VEGF expression in the spinal cord and extends survival in a mouse model of ALS. Neurobiol Dis 37:574-580, 2010.
Gandelman M, Peluffo H, Beckman JS, Cassina P, Barbeito L. Extracellular ATP and the P2X(7) receptor in astrocyte-mediated motor neuron death: implications for amyotrophic lateral sclerosis. J Neuroinflammation 7:33, 2010.
Sahawneh MA, Ricart KC, Roberts BR, Bomben VC, Basso M, Ye Y, Sahawneh J, Franco MC, Beckman JS, Estevez AG. Cu,Zn superoxide dismutase (SOD) increases toxicity of mutant and Zn-deficient superoxide dismutase by enhancing protein stability. J Biol Chem 285:33885-33897, 2010.
Rhoads TW, Lopez NI, Zollinger DR, Morré JT, Arbogast BL, Maier CS, DeNoyer L, Beckman JS. Measuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry. Anal Biochem 415:52-58, 2011.
Voinov VG, Deinzer ML, Beckman JS, Barofsky DF. Electron capture, collision-induced, and electron capture-collision induced dissociation in Q-TOF. J Am Soc Mass Spectrom 22:607-611, 2011.
Wei H, Frei B, Beckman JS, Zhang WJ. Copper chelation by tetrathiomolybdate inhibits lipopolysaccharide-induced inflammatory responses in vivo. Am J Physiol Heart Circ Physiol 301:H712-720, 2011.
Trumbull KA, McAllister D, Gandelman MM, Fung WY, Lew T, Brennan L, Lopez N, Morré J, Kalyanaraman B, Beckman JS. Diapocynin and apocynin administration fails to significantly extend survival in G93A SOD1 ALS mice. Neurobiol Dis 45:137-144, 2012.
