Joe M. McCord

Last updated
Joe Milton McCord
BornMarch 3, 1945 (1945-03-03) (age 79)
Citizenship United States
Alma mater Rhodes College, Duke University
Known forDiscovery of superoxide dismutase
Scientific career
Fields Biochemistry
Institutions University of Colorado
Doctoral advisor Irwin Fridovich

Joe Milton McCord (born March 3, 1945) is an American biochemist. While serving as a graduate student, he and his supervisor Irwin Fridovich were the first to describe the enzymatic activity of superoxide dismutase. [1] [2] McCord joined the board of directors of the LifeVantage Corporation (makers of the dietary supplement Protandim) in 2006, serving as the company's chief science officer from 2011 to 2012, and retired from the company in June 2013. [3]

Contents

Academic background

McCord received a B.S. degree in chemistry from Rhodes College (graduated 1966) and a Ph.D. in biochemistry from Duke University (graduated 1970), where he also conducted postdoctoral research.[ citation needed ]

McCord is a past recipient of the Discovery Award from the Society for Free Radical Biology and Medicine (shared with Irwin Fridovich), [4] the Elliott Cresson Medal, and a Lifetime Achievement Award from the Oxygen Society.[ citation needed ]

LifeVantage/Protandim

McCord served on the board of directors (Director of Science) of the LifeVantage Corporation beginning in 2006 and was listed by the SEC as an insider shareholder. [5] LifeVantage is a Utah-based multilevel marketing company that distributes an antioxidant dietary supplement known as Protandim. McCord co-authored 7 studies on the product [6] [7] [8] [9] [10] [11] [12] and participated in distributor training. [5] McCord served as chief scientific officer for LifeVantage from June 2011 until September 2012, and then became a member of the company's science advisory board. LifeVantage announced McCord's retirement in June 2013. [3] [13] Under the terms of the separation agreement, McCord was to receive a payment of $1.7 million from the company. [13]

Pathways Bio

McCord co-founded Pathways Bioscience to improve health span and overcome health and wellness problems associated with aging by supporting the body's own defense mechanisms that allow it to protect and heal itself. Pathways Bioscience is focused on the discovery and development of new agents that regulate gene expression and exert beneficial effects by influencing cell defense pathways. [14]

Related Research Articles

Antioxidants are compounds that inhibit oxidation, a chemical reaction that can produce free radicals. Autoxidation leads to degradation of organic compounds, including living matter. Antioxidants are frequently added to industrial products, such as polymers, fuels, and lubricants, to extend their usable lifetimes. Foods are also treated with antioxidants to forestall spoilage, in particular the rancidification of oils and fats. In cells, antioxidants such as glutathione, mycothiol, or bacillithiol, and enzyme systems like superoxide dismutase, can prevent damage from oxidative stress.

<span class="mw-page-title-main">Superoxide dismutase</span> Class of enzymes

Superoxide dismutase (SOD, EC 1.15.1.1) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O
2
) anion radical into normal molecular oxygen (O2) and hydrogen peroxide (H
2
O
2
). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use intracellular manganese to prevent damage from reactive O
2
.

<span class="mw-page-title-main">Catalase</span> Enzyme decomposing hydrogen peroxide

Catalase is a common enzyme found in nearly all living organisms exposed to oxygen which catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.

In chemistry, a superoxide is a compound that contains the superoxide ion, which has the chemical formula O−2. The systematic name of the anion is dioxide(1−). The reactive oxygen ion superoxide is particularly important as the product of the one-electron reduction of dioxygen O2, which occurs widely in nature. Molecular oxygen (dioxygen) is a diradical containing two unpaired electrons, and superoxide results from the addition of an electron which fills one of the two degenerate molecular orbitals, leaving a charged ionic species with a single unpaired electron and a net negative charge of −1. Both dioxygen and the superoxide anion are free radicals that exhibit paramagnetism. Superoxide was historically also known as "hyperoxide".

<span class="mw-page-title-main">Glutathione peroxidase</span> Enzyme family protecting the organism from oxidative damages

Glutathione peroxidase (GPx) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water.

<span class="mw-page-title-main">Melatonin</span> Hormone released by the pineal gland

Melatonin, an indoleamine, is a natural compound produced by various organisms, including bacteria and eukaryotes. Its discovery in 1958 by Aaron B. Lerner and colleagues stemmed from the isolation of a substance from the pineal gland of cows that could induce skin lightening in common frogs. This compound was later identified as a hormone secreted in the brain during the night, playing a crucial role in regulating the sleep-wake cycle, also known as the circadian rhythm, in vertebrates.

The free radical theory of aging states that organisms age because cells accumulate free radical damage over time. A free radical is any atom or molecule that has a single unpaired electron in an outer shell. While a few free radicals such as melanin are not chemically reactive, most biologically relevant free radicals are highly reactive. For most biological structures, free radical damage is closely associated with oxidative damage. Antioxidants are reducing agents, and limit oxidative damage to biological structures by passivating them from free radicals.

<span class="mw-page-title-main">Reactive oxygen species</span> Highly reactive molecules formed from diatomic oxygen (O₂)

In chemistry and biology, reactive oxygen species (ROS) are highly reactive chemicals formed from diatomic oxygen (O2), water, and hydrogen peroxide. Some prominent ROS are hydroperoxide (O2H), superoxide (O2-), hydroxyl radical (OH.), and singlet oxygen. ROS are pervasive because they are readily produced from O2, which is abundant. ROS are important in many ways, both beneficial and otherwise. ROS function as signals, that turn on and off biological functions. They are intermediates in the redox behavior of O2, which is central to fuel cells. ROS are central to the photodegradation of organic pollutants in the atmosphere. Most often however, ROS are discussed in a biological context, ranging from their effects on aging and their role in causing dangerous genetic mutations.

Lipid peroxidation, or lipid oxidation, is a complex chemical process that leads to oxidative degradation of lipids, resulting in the formation of peroxide and hydroperoxide derivatives. It occurs when free radicals, specifically reactive oxygen species (ROS), interact with lipids within cell membranes, typically polyunsaturated fatty acids (PUFAs) as they have carbon–carbon double bonds. This reaction leads to the formation of lipid radicals, collectively referred to as lipid peroxides or lipid oxidation products (LOPs), which in turn react with other oxidizing agents, leading to a chain reaction that results in oxidative stress and cell damage.

<span class="mw-page-title-main">Oxidative stress</span> Free radical toxicity

Oxidative stress reflects an imbalance between the systemic manifestation of reactive oxygen species and a biological system's ability to readily detoxify the reactive intermediates or to repair the resulting damage. Disturbances in the normal redox state of cells can cause toxic effects through the production of peroxides and free radicals that damage all components of the cell, including proteins, lipids, and DNA. Oxidative stress from oxidative metabolism causes base damage, as well as strand breaks in DNA. Base damage is mostly indirect and caused by the reactive oxygen species generated, e.g., O
2
, OH and H2O2. Further, some reactive oxidative species act as cellular messengers in redox signaling. Thus, oxidative stress can cause disruptions in normal mechanisms of cellular signaling.

<span class="mw-page-title-main">Myricetin</span> Chemical compound

Myricetin is a member of the flavonoid class of polyphenolic compounds, with antioxidant properties. Common dietary sources include vegetables, fruits, nuts, berries, tea, and red wine.

Protandim is a herbal dietary supplement marketed with unsupported claims that it can treat a number of medical conditions. The product is a patented mix of five herbal ingredients and sold by LifeVantage Corporation, a Utah-based multi-level marketing company. The manufacturers of Protandim make no claims that it can prevent or cure any medical conditions. In 2017, LifeVantage was issued a warning letter by the U.S. Food and Drug Administration (FDA) regarding illegal advertising claims on the company's websites suggesting that Protandim can help to cure various ailments, including cancer and diabetes.

<span class="mw-page-title-main">SOD1</span> Protein-coding gene in the species Homo sapiens

Superoxide dismutase [Cu-Zn] also known as superoxide dismutase 1 or hSod1 is an enzyme that in humans is encoded by the SOD1 gene, located on chromosome 21. SOD1 is one of three human superoxide dismutases. It is implicated in apoptosis, familial amyotrophic lateral sclerosis and Parkinson's disease.

<span class="mw-page-title-main">SOD2</span> Enzyme

Superoxide dismutase 2, mitochondrial (SOD2), also known as manganese-dependent superoxide dismutase (MnSOD), is an enzyme which in humans is encoded by the SOD2 gene on chromosome 6. A related pseudogene has been identified on chromosome 1. Alternative splicing of this gene results in multiple transcript variants. This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer.

<span class="mw-page-title-main">Irwin Fridovich</span> American biochemist (1929-2019)

Irwin Fridovich was an American biochemist who, together with his graduate student Joe M. McCord, discovered the enzymatic activity of copper-zinc superoxide dismutase (SOD),—to protect organisms from the toxic effects of superoxide free radicals formed as a byproduct of normal oxygen metabolism. Subsequently, Fridovich's research group also discovered the manganese-containing and the iron-containing SODs from Escherichia coli and the mitochondrial MnSOD (SOD2), now known to be an essential protein in mammals. He spent the rest of his career studying the biochemical mechanisms of SOD and of biological superoxide toxicity, using bacteria as model systems. Fridovich was also Professor Emeritus of Biochemistry at Duke University.

<span class="mw-page-title-main">NOX5</span> Protein-coding gene in the species Homo sapiens

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.

Hara Prasad Misra is an American biochemist and professor emeritus of biomedical sciences and pathology in the Virginia-Maryland Regional College of Veterinary Medicine at Virginia Tech. Misra is currently serving as vice president for research and graduate studies at the Virginia College of Osteopathic Medicine in Blacksburg, Virginia. Misra is a well-known teacher of undergraduate, graduate and DVM professional students for a period spanning over 30 years.

All living cells produce reactive oxygen species (ROS) as a byproduct of metabolism. ROS are reduced oxygen intermediates that include the superoxide radical (O2) and the hydroxyl radical (OH•), as well as the non-radical species hydrogen peroxide (H2O2). These ROS are important in the normal functioning of cells, playing a role in signal transduction and the expression of transcription factors. However, when present in excess, ROS can cause damage to proteins, lipids and DNA by reacting with these biomolecules to modify or destroy their intended function. As an example, the occurrence of ROS have been linked to the aging process in humans, as well as several other diseases including Alzheimer's, rheumatoid arthritis, Parkinson's, and some cancers. Their potential for damage also makes reactive oxygen species useful in direct protection from invading pathogens, as a defense response to physical injury, and as a mechanism for stopping the spread of bacteria and viruses by inducing programmed cell death.

<span class="mw-page-title-main">Superoxide dismutase mimetics</span> Synthetic compounds

Superoxide dismutase (SOD) mimetics are synthetic compounds that mimic the native superoxide dismutase enzyme. SOD mimetics effectively convert the superoxide anion, a reactive oxygen species, into hydrogen peroxide, which is further converted into water by catalase. Reactive oxygen species are natural byproducts of cellular respiration and cause oxidative stress and cell damage, which has been linked to causing cancers, neurodegeneration, age-related declines in health, and inflammatory diseases. SOD mimetics are a prime interest in therapeutic treatment of oxidative stress because of their smaller size, longer half-life, and similarity in function to the native enzyme.

<span class="mw-page-title-main">Mitochondrial theory of ageing</span> Theory of ageing

The mitochondrial theory of ageing has two varieties: free radical and non-free radical. The first is one of the variants of the free radical theory of ageing. It was formulated by J. Miquel and colleagues in 1980 and was developed in the works of Linnane and coworkers (1989). The second was proposed by A. N. Lobachev in 1978.

References

  1. McCord JM, Fridovich I (November 1969). "Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)". J. Biol. Chem. 244 (22): 6049–55. doi: 10.1016/S0021-9258(18)63504-5 . PMID   5389100.
  2. Keele BB, McCord JM, Fridovich I (November 1970). "Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme". J. Biol. Chem. 245 (22): 6176–81. doi: 10.1016/S0021-9258(18)62675-4 . PMID   4921969.
  3. 1 2 Corporation, Lifevantage (25 June 2013). "Dr. Joe McCord, LifeVantage Corporation's First Chief Science Officer, Retires From Company". GlobeNewswire News Room (Press release). Retrieved 19 April 2021.
  4. "SFRBM - Society for Free Radical Biology and Medicine".
  5. 1 2 http://secwatch.com/mccord-joe-m%5B%5D
  6. Nelson SK, Bose SK, Grunwald GK, Myhill P, McCord JM (January 2006). "The induction of human superoxide dismutase and catalase in vivo: a fundamentally new approach to antioxidant therapy". Free Radic. Biol. Med. 40 (2): 341–7. doi:10.1016/j.freeradbiomed.2005.08.043. PMID   16413416.
  7. Velmurugan K, Alam J, McCord JM, Pugazhenthi S (February 2009). "Synergistic induction of heme oxygenase-1 by the components of the antioxidant supplement Protandim". Free Radic. Biol. Med. 46 (3): 430–40. doi:10.1016/j.freeradbiomed.2008.10.050. PMID   19056485.
  8. Liu J, Gu X, Robbins D, et al. (2009). "Protandim, a fundamentally new antioxidant approach in chemoprevention using mouse two-stage skin carcinogenesis as a model". PLOS ONE. 4 (4): e5284. Bibcode:2009PLoSO...4.5284L. doi: 10.1371/journal.pone.0005284 . PMC   2668769 . PMID   19384424.
  9. Robbins D, Gu X, Shi R, et al. (2010). "The chemopreventive effects of Protandim: modulation of p53 mitochondrial translocation and apoptosis during skin carcinogenesis". PLOS ONE. 5 (7): e11902. Bibcode:2010PLoSO...511902R. doi: 10.1371/journal.pone.0011902 . PMC   2912769 . PMID   20689586.
  10. Bogaard HJ, Natarajan R, Henderson SC, et al. (November 2009). "Chronic pulmonary artery pressure elevation is insufficient to explain right heart failure". Circulation. 120 (20): 1951–60. doi: 10.1161/CIRCULATIONAHA.109.883843 . PMID   19884466.
  11. Qureshi MM, McClure WC, Arevalo NL, et al. (June 2010). "The Dietary Supplement Protandim Decreases Plasma Osteopontin and Improves Markers of Oxidative Stress in Muscular Dystrophy Mdx Mice". J Diet Suppl. 7 (2): 159–178. doi:10.3109/19390211.2010.482041. PMC   2926985 . PMID   20740052.
  12. Joddar B, Reen RK, Firstenberg MS, et al. (March 2011). "Protandim attenuates intimal hyperplasia in human saphenous veins cultured ex vivo via a catalase-dependent pathway". Free Radic. Biol. Med. 50 (6): 700–9. doi:10.1016/j.freeradbiomed.2010.12.008. PMID   21167278.
  13. 1 2 "Form 8-K for LifeVantage Corp". Yahoo.com. June 25, 2013. Retrieved November 10, 2013.
  14. https://www.pathwaysbio.com/ [ bare URL ]