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Robert M. Blanton, Jr., MD
Cardiologist; Investigator and Co-Director, Mouse Physiology Core Laboratory, Molecular Cardiology Research Institute; Assistant Professor, Tufts University School of Medicine
Department + Services
Medicine, CardioVascular Center, Cardiology
General cardiology, preventive cardiology
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|Programs + Specialties
|Training + Education
Washington University School of Medicine; Barnes-Jewish Hospital; Washington University School of Medicine; Tufts Medical Center
||Internal Medicine, Cardiovascular Disease
Tufts Medical Center
South Building, 3rd Floor
800 Washington St.
Boston, MA 02111
Fax #: 617-636-1444
Phone #: 617-636-2273
Sasaki H, Nagayama T, Blanton RM, Seo K, Zhang M, Zhu G, Lee DI, Bedja D, Hsu S, Tsukamoto O, Takashima S, Kitakaze M, Mendelsohn ME, Karas RH, Kass DA, Takimoto E. PDE5 inhibitor efficacy is estrogen dependent in female heart disease. J Clin Invest. 2014 Jun 2;124(6):2464-71.
Kong Q, Blanton RM. Protein Kinase G I and Heart Failure: Shifting Focus From Vascular Unloading to Direct Myocardial Antiremodeling Effects. Circ Heart Fail. 2013; 6:1268-83.
Wang G, Surks HK, Tang KM, Zhu Y, Mendelsohn ME, Blanton RM. Steroid-sensitive Gene-1 is a Novel cGMP-dependent Protein Kinase I Substrate in Vascular Smooth Muscle Cells. J Biol Chem. 2013; 288: 24972-24983
Blanton RM, Takimoto E, Aronovitz M, Thoonen R, Kass D, Karas R, Mendelsohn ME. Mutation of the PKG I alpha leucine zipper domain produces hypertension and progressive LVH: a novel mouse model of age-dependent hypertensive heart disease. J Gerontol A Biol Sci Med Sci. 2013; 68:1351-1355.
Blanton RM, Takimoto E, Lane A, Piotrowski R, Aronovitz M, Karas RH, Kass DA, Mendelsohn M. Protein kinase Gl alpha inhibits pressure overload-induced cardiac remodeling and is required for the cardioprotective effect of sildenafil in vivo. J Am Hrt Assoc 2012 Oct;1(5):e003731
Kato M, Blanton R, Wang GR, Judson TJ, Abe Y, Myoishi M, Karas R, Mendelsohn ME. Direct Binding and Regulation of RhoA by Cyclic GMP-dependent Protein Kinase Ia. J Biol Chem. 2012; 287:41342-41351. (co-first author).
Originally from Texas, Rob attended college and medical school at Washington University in St. Louis. He joined the MCRI and the Cardiology Division in 2005 as a clinical/research fellow, following his residency training in internal medicine at Barnes-Jewish Hospital. He completed his cardiovascular fellowship in 2009 and is now an Assistant Professor of Medicine. Rob's research examines the molecular mechanisms regulating the development and inhibition of cardiac hypertrophy. In addition, he serves as the Scientific Director of the MCRI Mouse Physiology Core.
The disease of congestive heart failure has reached epidemic proportions in the U.S. and throughout the world. While heart failure is a clinical syndrome, it generally arises from cardiac remodeling: a chronic process of pathologic hypertrophy, dilation, and dysfunction of the myocardium. The overarching goal of the Blanton laboratory is to uncover novel signaling mechanisms in the myocardium which attenuate cardiac remodeling, and thus might serve as new therapeutic targets in the treatment and prevention of heart failure. To this end, our studies encompass basic molecular screens, state of the art in vivo models of cardiac remodeling, and studies in human patients.
1. Exploring novel anti-remodeling molecules regulated by the signaling molecule PKGI: Multiple pre-clinical studies have identified augmentation of cGMP, and its downstream effector protein kinase G (PKG) as inhibiting pathologic cardiac remodeling. However, human studies of PKG-activating drugs (sildenafil, cinaciguat, and nesiritide) have been less successful in improving outcomes in humans with heart failure. Specifically, hypotension arising from PKG-induced vasodilation has proven a critical limitation of many of these agents. We have therefore explored downstream PKG antiremodeling substrates in the myocardium, which remain poorly understood. This strategy might identify candidate myocardial-specific therapeutic targets to inhibit remodeling yet avoid hypotension arising from systemic PKGI activation. Our lab has identified several novel PKGI substrates which we are now investigating both in in vitro studies and in animal models of heart failure.
2. PKG leucine zipper substrates as regulators of cardiovascular physiology: We have performed a number of molecular screens for proteins which interact with the unique PKGI leucine zipper binding domain. These screens have revealed a number of novel PKGI substrates. We are currently exploring the role of these substrates in cardiovascular processes such as: pathologic cardiac hypertrophy; blood pressure control; and left ventricular function.
3. Translational studies of novel anti-remodeling pathways: We are extending our studies to begin to understand the function of newly-identified anti-remodeling proteins in the human failing heart, in order to test the hypothesis that these molecules could serve as therapeutic targets for the treatment and prevention of heart failure.
4. In vivo cardiovascular phenotyping studies: Our lab has significant experience with specialized assays of cardiovascular physiology in mice, such as invasive cardiac hemodynamic studies, echocardiography, and isolation of cardiac myocytes. In this capacity we have a number of ongoing collaborations ranging from cardiovascular analysis of genetically altered mice to testing of novel compounds for therapeutic efficacy.