Mark E. Anderson, MD, PhD
Disclosures: Nothing to disclose
0925-0001/0002, PHS 398, PHS 2590 (Rev. 08/12), Biographical Sketch Format Page

OMB No. 0925-0001 and 0925-0002 (Rev. 03/2020 Approved Through 03/28/2023)


Provide the following information for the Senior/key personnel and other significant contributors.

Follow this format for each person.  DO NOT EXCEED FIVE PAGES.\


NAME: Mark E. Anderson

eRA COMMONS USER NAME (credential, e.g., agency login):  ANDERSM2


EDUCATION/TRAINING (Begin with baccalaureate or other initial professional education, such as nursing, include postdoctoral training and residency training if applicable. Add/delete rows as necessary.)




(if applicable)



Macalester College, St. Paul, MN




University of Minnesota, Minneapolis, MN




University of Minnesota, Minneapolis, MN




Stanford University, Stanford, CA



Internal Medicine

Stanford University, Stanford, CA




Stanford University, Stanford, CA





A. Personal Statement  Our research focuses on fundamental mechanisms of cellular signaling that contribute to cardiovascular diseases, heart failure, arrhythmias and sudden cardiac death.  Work from our laboratory contributed to current concepts about the role of the multifunctional Ca2+/calmodulin dependent protein kinase II (CaMKII) as a nodal signal for cardiovascular physiology and disease. Our work has extended to the role of CaMKII in asthma and inflammatory signaling.  I  am currently or have served as mentor to more than 30 trainees. Many of my mentees are actively pursuing academic careers in research.

B. Positions and Honors


1996              Assistant Professor, Cardiology Division, Vanderbilt University, Nashville, TN

1997              Assistant Professor, Department of Pharmacology, Vanderbilt University, Nashville, TN

1997-05              Director, Electrophysiology Fellowship Program, Vanderbilt University, Nashville, TN

1999-05              Director, Cardiovascular Fellowship Training Program, Vanderbilt University, Nashville, TN

2001              Associate Professor (tenure), Depts of Medicine/Pharmacology, Vanderbilt University, Nashville TN

2002-05              Director, Clinical Arrhythmia Service, Vanderbilt University, Nashville TN

2005              Professor, Departments of Medicine and Pharmacology, Vanderbilt University, Nashville, TN

2005-09              Professor & Director, Cardiovascular Medicine, Carver College of Medicine, University of Iowa

2005-12              Associate Director, Iowa Cardiovascular Research Center, University of Iowa, Iowa, City, IA

2009-14              Chair, Department of Internal Medicine, Carver College of Medicine, University of Iowa

2012-14              Director, Cardiovascular Research Center, Carver College of Medicine, University of Iowa

2014-              Director, Department of Medicine and Physician in Chief Johns Hopkins University Hospital


Editorial Boards and Professional Memberships

1998-09              Editorial Board, J Cardiovascular Electrophysiology

2001              Fellow, American College of Cardiology

2002              Member, American Society for Clinical Investigation

2004-16              Editorial Board, Heart Rhythm

2005              Founding Fellow, Heart Rhythm Society

2006              Member, Association of American Physicians

2006-              Editorial Board, Circulation

2007-              Editorial Board, J Molecular and Cellular Cardiology

2007-              Member, Association of University Cardiologists

2009-12              Scientific Committee of the Sarnoff Cardiovascular Research Foundation

2009              Member, Association of Professors of Medicine
2010              Member, Heart Rhythm Society Research Task Force

2010-17              Editorial Board member, Circulation Research

2012-              Editorial Board member, Journal of Clinical Investigation

2017-22              Associate Editor, Journal of Clinical Investigation

2020-22              2020-2022              Member, AAIM Governance Committee (as an AAIM Board representative).


Honors and Lectureships

1988              A.O.A., National Medical Honorary Society, University of Minnesota

2000              Established Investigator, American Heart Association

2002              Betty and Jack Bailey Chair in Medicine, Vanderbilt University, Nashville, TN

2002              Elected, American Society for Clinical Investigation

2003              Elliott Newman Prize for Outstanding Research Contribution, Dept of Medicine, Vanderbilt University
2004              Borun Visiting Professor, Division of Cardiology, UCLA School of Medicine

2004-08              Study section member, NHLBI, Electrical Signaling, Ion Transport and Arrhythmias

2005              Potter-Lambert Chair in Cardiology, Department of Medicine, University of Iowa, Iowa City, IA

2006              Lecturer, Ohio Discovery Series, OSU, Columbus, OH

2006              Elected, Association of American Physicians

2007              Dan May Lecturer, Vanderbilt University, Nashville, TN

2009              Elected Councilor, International Society of Heart Research (2009-2015)

2009-              François M. Abboud Chair in Internal Medicine

2010-              Elected Fellow, International Society for Heart Research
2010-12              Member, Council of Central Society for Clinical Research

2010              Senior Fellow, American Asthma Association

2010              Fellow, American College of Physicians

2010              Fellow, European Society of Cardiology

2011              Brutsaert Lecture, European Society of Cardiology

2011              Association of Black Cardiologists 2011 Diversity in Cardiology Award

2012-14              Elected Vice Chair/Chair Gordon Research Conference, Cardiac Regulatory Mechanisms

2013              Harrison Society Visiting Professor, Vanderbilt University

2013              Eldon Smith Lectureship, University of Calgary

2014              William Osler Professor of Medicine

2014              Team Leader, Scientific Sessions Program Committee, Heart Rhythm Society

2015               Research Achievement Award, International Society of Heart Research

2015              Scientific Advisory Board Member, Fondation Leducq

2016              Elected Member, Interurban Clinical Club

2017              Distinguished Scientist Award, Heart Rhythm Society, May 2017, Chicago

2018              Elected Member, National Academy of Medicine

2019-20              Vice President, Scientific Advisory Committee, Fondation Leducq

2019-20              President, Association of Professors in Medicine (APM), Alliance for Academic Internal Medicine

2019              Distinguished Scientist Award, American Heart Association

2020-21              President, Scientific Advisory Committee, Fondation Leducq

C.  Contribution to Science

1.               CaMKII is proarrhythmic and CaMKII inhibition is antiarrhythmic

Cardiac arrhythmias are a major cause of suffering and death but current drug therapies are inadequate.  Classical antiarrhythmic drugs are ion channel antagonists but these have the untoward propensity to induce arrhythmias (pro-arrhythmia), particularly in patients with structural heart disease who are most at risk for sudden death.  My group was the first to identify CaMKII, a serine-threonine kinase, as a pro-arrhythmic signal and therapeutic target (US Patent #6,518,245 and US Patent #7,251,525).  During my post-doctoral fellowship training, we found that CaMKII augmented voltage-gated Ca2+ current (Anderson Circ Res 1994) and that this property contributed to arrhythmia-triggering early (Anderson JPET 1998; Wu Am J Physiol 1999) and delayed (Wu Circ Res 1999) after-depolarizations.  Through our work and the work of many other groups, CaMKII now is recognized to affect multiple ionic currents, Ca2+ homeostatic proteins and is a widely validated pro-arrhythmic signal and therapeutic target.  Our work led to patents and motivated active industry efforts to develop CaMKII inhibitor drugs, in part, to treat cardiac arrhythmias.

a)      Anderson ME, Braun AP, Schulman H, Premack BA.  Multifunctional Ca2+/calmodulin– dependent protein kinase mediates Ca2+-induced enhancement of the L-type Ca2+ current in rabbit ventricular myocytes. Circ Res 1994 Nov; 75(5):854-61.  [PMID:7923631]

b)      Anderson ME*, Braun AP, Wu Y, Lu T, Wu Y, Schulman H, Sung RJ.  KN-93, an inhibitor of multifunctional Ca2+/calmodulin dependent protein kinase, decreases early after-depolarizations in rabbit heart.  J Pharmacol Exper Ther 1998 Dec; 287(3):996-1006. [PMID:9864285]

c)      Wu Y, Roden DM, Anderson, ME.  Calmodulin Kinase inhibition prevents development of the arrhythmogenic transient inward current.  Circ Res 1999 Apr 30; 84(8):906-12. [PMID:10222337]

d)      Wu Y, MacMillan LB, McNeill RB, Colbran RJ, Anderson ME.  CaM kinase augments cardiac of L-type Ca2+ current: A cellular mechanism for long QT arrhythmias.  Am J Physiol 1999 Jun; 276(6 Pt 2):H2168-78.  [PMID:10362701]


2.               CaMKII promotes cardiomyopathy and CaMKII inhibition protects against heart failure

Heart failure is a growing public health problem costing billions of dollars in the United States each year.  Improved therapies with the ability to prevent and slow progression of heart failure in high risk individuals are needed to control this epidemic.  In the late 1990s CaMKII emerged as a signal that was consistently upregulated in failing myocardium from patients and from animal models of heart failure, but the potential for CaMKII to be an effective therapeutic target in heart failure was uncertain.  Our group was the first to publish evidence (Zhang Nat Med 2005) and win a patent (US Patent #7,320,959) that myocardial CaMKII inhibition was protective against clinically relevant models of heart failure in mice.  CaMKII is now widely celebrated as a nodal signal for orchestrating diverse, maladaptive mechanisms in the syndrome of heart failure.  I was the North American leader of a Fondation Leducq Alliance for CaMKII Signaling in Heart Failure and Arrhythmias. There are now several active commercial programs for developing CaMKII inhibitory drugs for heart failure and arrhythmias.  

a)      Zhang R, Khoo MS, Wu Y, Yang Y, Grueter CE, Ni G, Price EE Jr, Thiel W, Guatimosim S, Song LS, Madu EC, Shah AN, Vishnivetskaya TA, Atkinson JB, Gurevich VV, Salama G, Lederer WJ, Colbran RJ, Anderson ME.  Calmodulin kinase II inhibition protects against structural heart disease.  Nat Med 2005 Apr; 11(4):409-17.  [PMID:15793582]  Commentary in Nat Med, 2005 Apr; 11(4): 379-80 [PMID:15812516]

b)      Khoo MS, Li J, Singh MV, Yang Y, Kannankeril P, Wu Y, Grueter CE, Guan X, Oddis CV, Zhang R, Mendes L, Ni G, Madu EC, Yang J, Bass M, Gomez RJ, Wadzinski BE, Olson EN, Colbran RJ, Anderson ME.  Death, cardiac dysfunction and arrhythmias are increased by calmodulin kinase II in calcineurin-induced cardiomyopathy.  Circulation 2006 Sep 26; 114(13):1352-9. [PMID:16982937]

c)       Singh MV, Kapoun A, Higgins L, Kutschke WJ, Thurman JM, Singh M, Yang J, Guan X, Lowe JS, Weiss RM, Zimmerman K, Yull FE, Blackwell TS, Mohler PJ, Anderson ME.  Ca2+/calmodulin-dependent kinase II triggers cell membrane injury by inducing complement factor B gene expression in the mouse heart.  J Clin Invest 2009 Apr; 119(4):986-96.  PMCID: PMC2662543.  Commentary in Nat Med 2009; 15:375.

d)      Joiner ML, Koval OM, Li J, He BJ, Allamargot C, Gao Z, Luczak ED, Hall DD, Fink BD, Chen B, Yang J, Moore SA, Scholz TD, Strack S, Mohler PJ, Sivitz WI, Song LS, and Anderson ME.  CaMKII determines mitochondrial stress responses in heart.  Nature 2012 Nov 8; 491(7423):269-73. PMCID: PMC3471377. Commentary in Circ Res 2013 Apr 26; 112(9):1208-11 [PMID: 23620234]. 


3.               Novel mechanisms of cardiac pacemaker physiology and disease

Understanding mechanisms of cardiac pace-making is a longstanding goal of physiological research and sinoatrial node (SAN) dysfunction is an important cause of sudden death.  Although effective, current electronic pacemakers require surgical implantation, are costly and associated with complications and require periodic replacement.  New therapeutic approaches for preventing SAN disease could benefit many patients.  Our group identified CaMKII as a critical signal for supporting physiological fight or flight heart rate acceleration by enhancing sarcoplasmic reticulum Ca2+ uptake and release, and discovered that excessive CaMKII activation by angiotensin II or hyperglycemia led to SAN cell death and pacemaker dysfunction.  Furthermore, CaMKII inhibition by transgenic expression of CaMKII inhibitory peptides or SAN-targeted CaMKII inhibitory gene therapy prevented SAN cell death and pacemaker dysfunction in response to pathological stress.  Recently, we discovered a metabolic pathway for pacemaker acceleration by Ca2+ entry through the mitochondrial Ca2+ uniporter (MCU).  Our findings suggest that SAN MCU inhibition could selectively control rapid heart rates without slowing resting heart rates.

a)      Wu Y, Gao Z, Chen B, Koval OM, Singh MV, Guan X, Hund TJ, Kutschke WJ, Sarma S, Grumbach IM, Wehrens XH, Mohler PJ, Song LS, Anderson M.E.  Calmodulin kinase II is required for fight or flight sinoatrial node physiology.  Proc Natl Acad Sci 2009 Apr 7; 106(14):5972-7. PMCID: PMC2667018.  Chosen as a “From the Cover” article in PNAS Commentary in Sci Signaling 2009; 2:ec130.

b)      Swaminathan PD, Purohit A, Soni S, Voigt N, Singh MV, Glukhov AV, Gao Z, He BJ, Luczak ED, Joiner ML, Kutschke W, Yang J, Donahue JK, Weiss RM, Grumbach IM, Ogawa M, Chen PS, Efimov IR, Dobrev D, Mohler PJ, Hund TJ, Anderson ME .  Oxidized CaMKII causes cardiac sinus node dysfunction in mice.  J Clin Invest 2011 Aug; 121(8):3277-88.  PMCID: PMC3223923.  Commentary in J Clin Invest 2011 Aug; 121(8):2975-7. PMCID: PMC3148748. 

c)      Wu Y, Rasmussen TP, Koval OM, Joiner MA, Hall DD, Chen B, Luczak ED, Wang Q, Rokita AG, Wehrens XHT, Song L, Anderson ME.   The mitochondrial uniporter controls fight or flight heart rate increases. Nature Communications 2015 Jan 20; 6:6081. PMCID: PMC4398998.

d)      Wu Y, Valdivia H, Wehrens X, Anderson ME.   A single PKA or CaMKII site does not control the cardiac pacemaker Ca2+ clock.  Circulation Arrhythmia and Electrophysiology 2016 Feb; 9(2).  PMID 26857906 PMCID: PMC4755317.


4.               CaMKII is activated by oxidant stress

Elevated reactive oxygen species (ROS) are a feature of many or most chronic diseases of adults, but comparatively little is known about concise molecular pathways with the potential to transduce ROS into common disease phenotypes.  Based on earlier studies suggesting CaMKII could be activated by ROS, we identified a pair of conserved methionines (281/282 in CaMKII) in the regulatory domain and developed evidence that oxidation of these methionines ‘locked’ CaMKII (ox-CaMKII) into a persistently active conformation.  Furthermore, we discovered that ox-CaMKII could be reduced by methionine sulfoxide reductase A (MsrA).  MsrA was of interest because Msra-/- mice had reduced lifespan, while worms and flies overexpressing MsrA exhibited enhanced longevity.  Our study identified CaMKII as one of the first bona fide MsrA target proteins, resulted in a patent application (US Patent #20100226929) and antiserum for detecting ox-CaMKII.  Recently we engineered CaMKII knockin mice where methionines 281/282 were replaced with valines (M281/282V), a mutation that selectively impaired CaMKII activation by ROS while leaving activation by Ca2+ and calmodulin unchanged from wild type CaMKII.  These M281/282V mice are resistant to pathological effects of ROS in models of diabetes (Luo JCI 2013) and atrial fibrillation (Purohit Circulation 2013).  The role of CaMKII as a redox sensor has rapidly gained traction and been embraced widely by researchers in diverse areas (e.g. cancer, botany, neuroscience), suggesting ox-CaMKII is a fundamental mechanism for ROS signaling in health and disease.

a)   Erickson JR, Joiner ML, Guan X, Kutschke WJ, Yang J, Oddis CV, Bartlett RK, Lowe JS, O’Donnell SE, Aykin-Burns N, Zimmerman MC, Zimmerman K, Ham AJ, Weiss RM, Spitz DR, Shea MA, Colbran RJ, Mohler PJ, Anderson MEA dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 2008 May 2; 133(3):462-74. PMCID: PMC2435269.  Published with accompanying editorial in Cell 2008 May 2; 133(3):397-9.  PMCID: PMC2655315. Commentaries in Nat Med, 2008 May 2; 14(5):612 and Science Signaling, 2008, 1:ec161.

b)   Konstantinidis K, Bezzerides VJ, Lai L, Isbell HM, Wei AC, Wu Y, Viswanathan MC, Blum ID, Granger JM, Zhang D, Heims-Waldron D, Luczak ED, Murphy KR, Lu F, Gratz DH, Manta B, Wang Q, Wang Q, Kolodkin AL, Gladyshev VN, Hund TJ, Pu WT, Cammarato A, Bianchet MA, Shea MA, Levine RL, Anderson ME.  MICAL1 constrains cardiac stress responses and protects against disease by oxidizing CaMKII.  J Clin Invest 2020 (in press)


5.               Oxidized CaMKII (ox-CaMKII) contributes to cardiovascular, metabolic and pulmonary disease

Although excessive ROS is thought to contribute to many diseases, clinical trials of untargeted antioxidants have been disappointing.  We hypothesized that excessive ROS could contribute to disease by increasing ox-CaMKII and CaMKII inhibition could be a novel and effective ‘antioxidant’ strategy for treating common, chronic diseases.  In a series of studies we determined that ox-CaMKII was increased in patients with myocardial disease and important for cardiomyopathic effects of myocardial infarction, angiotensin II (Erickson Cell 2008; Swaminathan JCI 2011), aldosterone (He Nat Med 2011) and hyperglycemia (Luo JCI 2013).  Our group won a foundation award (Sandler/American Asthma Association) to extend our studies into asthma.  This allowed us to test our ideas beyond the cardiovascular system and to discover ox-CaMKII expression was increased in airway epithelium from asthmatic patients and in mouse models of allergic asthma.  We showed that ox-CaMKII promoted diverse pathological airway phenotypes important for asthma, including airway reactivity, mucus production and epithelial proliferation (Sanders Sci Transl Med 2013).  These studies provide hope that CaMKII inhibitory drugs under development for cardiovascular disease indications will prove useful in other conditions where excessive ROS is important for disease progression.

a)      He BJ, Joiner ML, Singh MV, Luczak ED, Swaminathan PD, Koval OM, Kutschke W, Allamargot C, Yang J, Guan X, Zimmerman K, Grumbach IM, Weiss RM, Spitz DR, Sigmund CD, Blankesteijn WM, Heymans S, Mohler PJ,               Anderson ME.  Oxidation of CaMKII determines cardiotoxic effects of aldosterone. Nat Med 2011 Nov 13; 17(12): 1610-9. PMCID: PMC3332099. 

b)      Luo M, Guan X, Luczak ED, Di L, Kutschke W, Gao Z, Yang J, Glynn P , Sossalla S, Swaminathan PD, Weiss RM, Yang B, Rokita AG,5, Maier LS, Efimov I, Hund TJ, Anderson ME.  Diabetes increases mortality after myocardial infarction by oxidizing CaMKII.  J Clin Invest 2013 Mar 1; 123(3):1262-74. PMCID: PMC3673230. Erratum: J Clin Invest 2013 May 1; 123(5): 2333.

c)              Sanders PN, Koval OM, Jaffer OA, Prasad AM, Businga TR, Scott JA, Hayden PJ,  Luczak ED, Dickey DD,  Allamargot C, Olivier AK, Meyerholz DK, Robison AJ,  Winder DG, Blackwell TS, Dworski R, Sammut D, Wagner BA, Buettner GR, Pope MR, Miller FJ, Dibbern ME, Haitchi HM, Mohler PJ, Howarth PH, Zabner J, Kline JN, Grumbach IM, Anderson ME. CaMKII is Essential for the Proasthmatic Effects of Oxidation.  Sci Trans Med 2013 Jul 24; 5(195):195 ra97. PMID: 23884469. PMCID: PMC4331168 Commentary in JAMA. 310(9):894.

d)              Qu J, Danh CD, Zhou Y, Luczak E, Mitzner W, Anderson ME, Gao P.  Oxidized CaMKII promotesasthma through the activation of mast cells.  J Clin Invest Insight. 2017 Jan 12;2(1):e90139.  PMCID: PMC5214090.


Complete List of Published Work in MyBibliography:

D.  Additional Information: Research Support and/or Scholastic Performance

Ongoing Research Support

NIH/NHLBI R35 HL140034-02 (Anderson – PI)                                                                                                                                            01/01/18-12/31/24

CaMKII signaling in physiology, heart failure              and arrhythmias


Completed Research Support


AHA AWRP Collaborative Sciences Award 17CSA33610107                                                                      07/01/17-06/30/20             

(Anderson and Hart – Co-PIs)

Defining a new metabolic pathway in myocardial disease


NIH/NHLBI (HL) 1R01 HL070250 (Anderson - PI)                                                                                                                               10/01/05-07/31/18

“Mitochondrial Calmodulin Kinase II in Physiology and Disease”

This is a proposal to study the consequences of sub-cellularly-targeted calmodulin kinase inhibition on molecular, cellular and in vivo mechanisms of disease-resistance.

NIH/NHLBI R01 HL096652 (Anderson - PI)                                                                                                                                                               07/15/09-07/31/17

“CaMKII in Sinus Node Physiology and Disease”                                                                                                                               NCE 07/31/18

This project tests the hypothesis that CaMKII activity is necessary for physiological increases in heart rate but when excessively activated, contributes to sinoatrial nodal failure.


JHU SOM Discovery Fund Program (Anderson and Hart co-PIs)                                                                      07/01/16-06/30/17             

Synergy Award

CaMKII-OGT Axis in metabolic heart disease


NIH/NHLB R01 HL113001 (Anderson - PI)                                                                                                                                                           04/01/12-02/28/17

“Oxidized CaMKII in atrial fibrillation”


NIH R01 HL-079031 (Anderson - PI) (NCE)                                                                                                                                                          12/15/10-11/30/16

“Methionine sulfoxide reductase A and oxidized CaMKII in structural heart disease”


Fondation Leducq Transatlantic Network                            (Anderson PI)                                                                                    10/01/08-12/31/13             

Alliance for CaMKII Signaling