Free radicals are formed when the body uses oxygen to make energy, to process foreign particles, like drugs, even when we encounter sunlight or radiation. Sometimes, when free radicals react with the body’s tissues, damage can occur, leading to heart disease, cancer and many conditions associated with aging.
In my lab, we study the damage that happens when free radicals interact with cells and try to observe how cells protect themselves or change themselves in the process. We have learned that sometimes the body’s reaction to the free radicals, rather than the free radicals themselves, can cause the most damage.
Some cells have the ability to adjust to free radical damage and function normally, or even benefit from the interaction. Other cells see little or no damage from free radicals, while some simply shut down or die.
In heart disease, certain white blood cells often react to free radicals by transforming themselves into “foam” cells. Those cells can lead to atherosclerosis, an inflammatory disease that clogs blood vessels and causes heart disease.
Our goal is to understand these changes so we can use them to our benefit. By identifying the triggers that can either increase good cell responses or decrease bad ones, we may learn ways to prevent many kinds of human disease.
There are two primary activities in my laboratory: characterizing changes in protein expression in hearts and mitochondria from mice that are consuming a high-fat diet and characterizing the sites and chemical structure of oxidant-damaged proteins. A unique aspect of my experiments is the use of mass spectrometry to sequence and characterize proteins. These types of experiments are broadly referred to a proteomics.
In the first area of investigation, we use a proteomic approach – gel electrophoresis and quantitative mass spectrometry – to identify proteins that are differentially expressed in the heart and mitochondria. The general hypothesis being tested in this work is that the high fat diet produces a chronic oxidative stress that alters heart and mitochondrial function through changes in protein expression. Our goal is to discover previously unidentified or unstudied proteins that help drive the progression of the diet-induced heart failure.
In the second area of investigation, we use tandem mass spectrometry to characterize the site and structure of oxidative modifications to proteins. One theory of how oxidative stress affects cells is that key proteins become modified in a manner that alters their function. Our goal is to trace the specific structures that are characterized to new information about the oxidation reactions leading to those modifications and the link between those modifications and cell/tissue damage.
B.S. Chemistry, James Madison University, Harrisonburg, VA, 1982
Ph.D. Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, 1986
Postdoc, Clinical Chemistry, University of Virginia, Charlottesville, VA, 1986-1988
American Society for Mass Spectrometry
American Society for Biochemistry and Molecular Biology
Society for Free Radical Biology and Medicine
Joined OMRF Scientific Staff in 2008.
Cardoso AC, Lam NT, Savla JJ, Nakada Y, Pereira AHM, Elnwasany A, Menendez-Montes I, Ensley EL, Petric UB, Sharma G, Sherry AD, Malloy CR, Khemtong C, Kinter MT, Tan WLW, Anene-Nzelu CG, Foo RS, Nguyen NUN, Li S, Ahmed MS, Elhelaly WM, Abdisalaam S, Asaithamby A, Xing C, Kanchwala M, Vale G, Eckert KM, Mitsche MA, McDonald JG, Hill JA, Huang L, Shaul PW, Szweda LI, Sadek HA. Mitochondrial Substrate Utilization Regulates Cardiomyocyte Cell Cycle Progression. Nat Metab 2:167-178, 2020 February, PMID: 32617517, PMCID: PMC7331943
Sataranatarajan K, Pharaoh G, Brown JL, Ranjit R, Piekarz KM, Street K, Wren JD, Georgescu C, Kinter C, Kinter M, Freeman WM, Richardson A, Van Remmen H. Molecular changes in transcription and metabolic pathways underlying muscle atrophy in the CuZnSOD null mouse model of sarcopenia. Geroscience, 2020 May, PMID: 32394347
Pharaoh G, Owen D, Yeganeh A, Premkumar P, Farley J, Bhaskaran S, Ashpole N, Kinter M, Van Remmen H, Logan S. Disparate Central and Peripheral Effects of Circulating IGF-1 Deficiency on Tissue Mitochondrial Function. Mol Neurobiol, 2019 November, PMID: 31732912, PMCID: PMC7060968
Fu Y, Kinter M, Hudson J, Humphries KM, Lane RS, White JR, Hakim M, Pan Y, Verdin E, Griffin TM. Aging Promotes SIRT3-dependent Cartilage SOD2 Acetylation and Osteoarthritis. Arthritis Rheumatol. 2016 Aug;68(8):1887-98. PMID: 26866626 PMCID: PMC5331855
Walsh ME, Bhattacharya A, Sataranatarajan K, Qaisar R, Sloane L, Rahman MM, Kinter M, Van Remmen H. The histone deacetylase inhibitor butyrate improves metabolism and reduces muscle atrophy during aging. Aging Cell 2015 Dec; 14(6): 957–970. PMID: 26290460 PMCID: PMC4693467
Fernandes J, Weddle A, Kinter CS, Humphries KM, Mather T, Szweda LI, Kinter M. Lysine acetylation activates mitochondrial aconitase in the heart. Biochemistry 2015 Jun 30;54(25):4008-18. PMID: 26061789 PMCID: PMC4513942
Kinter CS, Lundie JM, Patel H, Rindler PM, Szweda LI, Kinter M. A Quantitative proteomic profile of the Nrf2-mediated antioxidant response of macrophages to oxidized LDL determined by multiplexed selected reaction monitoring. PLoS One 7:e50016, 2012. PMID: 23166812 PMCID: PMC3500347
Conway JP, Kinter M. Proteomic and transcriptomic analyses of macrophages with an increased resistance to oxidized low density lipoprotein (oxLDL)-induced cytotoxicity generated by chronic exposure to oxLDL. Mol Cell Proteomics 4:1522-1540, 2005. PMID: 16006650
Aging & Metabolism Research Program, MS 21
Oklahoma Medical Research Foundation
825 N.E. 13th Street
Oklahoma City, OK 73104
Phone: (405) 271-7572
Fax: (405) 271-1437
News from the Kinter lab
A new wave of researchers has joined the Oklahoma Medical Research Foundation’s scientific staff as part of the foundation’s expansion. OMRF has added seven new scientists to its staff. In addition, two research assistants have been promoted to faculty-level positions. The new researchers have come to OMRF from a variety of institutions across the U.S. […]