Ram Sasisekharan, Ph.D.
Alfred H. Caspary Professor of Biological Engineering and
Health Sciences & Technology
Research group web site
Phone: (617) 258-9494
Fax: (617) 253-7498
Administrative Assistant: Ada Ziolkowski
Courses: 20.103, 20.105J, 20.203, 20.216
Honors & Awards
||National Institutes of General Medical Sciences MERIT Award
||American Institute for Medical and Biological Engineering (AIMBE) Fellow
||Princess Chulabhorn Gold Medal Award
||Princess Chulabhorn Institute Distinguished Lecturer Award
|| Indus Technovator Award
||CaPCure Foundation, CaPCure Award
||Beckman Foundation Young Investigator Award
||Burroughs Wellcome Fund Young Investigator Award in Pharamacological Sciences
||Edgerly Science Partnership Award
||CaPCure Foundation, CaPCure Award
||INLAKS FOUNDATION, London, England
Sasisekharan's laboratory's broad research objectives are aimed towards understanding the mechanisms governing the extracellular regulation of cell function, generating novel pharmacological approaches to modulate cell function for the treatment of diseases.
Glycosaminoglycans (GAGs), the polysaccharide component of the extracellular matrix (ECM), are the most acidic naturally occurring biopolymers. These GAGs not only hydrate the ECM, but also solubilize several transient molecules, such as growth factors, cytokines, enzymes etc. that diffuse from the outside of a tissue to the cell surface to modulate cellular function. GAGs are believed to regulate important physiological as well as pathological processes, which include morphogenesis, angiogenesis and tumor growth. At the present time, due to a lack of powerful methods and tools, there is little information as to how GAGs modulate or regulate a given biological process.
Using GAGs as a model system, our vision is to focus and develop on the one hand, a programmatic approach to investigate important questions addressing the biological roles and significance of these complex molecules. On the other hand, this strategy is built with the idea of plausible technological applications in mind, which include the development of much desired novel and powerful tools and agents for both diagnostic as well as therapeutic needs for unmet medical conditions.
Click here for a complete list of publications.
Raman R, Raguram S, Venkataraman G, Paulson J, Sasisekharan R (2005) Glycomics: Integrated Systems Approach to Structure-Function Relationships of Glycans, 2005 Nature Methods; 2(11):817-824
Sengupta S, Eavarone D, Capila I, Zhao G, Watson N, Kiziltepe T, Sasisekharan R. (2005) Temporal targeting of tumour cells and neovasculature with a nanoscale delivery system. Nature Jul 28;436(7050):568-72.
Shriver Z, Raguram S, Sasisekharan R (2004). Glycomics: a pathway to a class of new and improved therapeutics Nature Reviews Drug Discovery 3, 863-873. [pdf]
Sasisekharan R, and Myette J (2003) The Sweet Science of Glycobiology American Scientist. [pdf]
Sundaram M, Qi Y, Shriver Z, Liu D, Zhao G, Venkataraman G, Langer R, and Sasisekharan R (2003) Rational design of low molecular weight heparins with improved in vivo activity. Proc Natl Acad Sci U S A, 100, 651-6.
Liu, D., Shriver, Z., Venkataraman, G., & Sasisekharan R., (2002) Inhibition of Tumor Growth and Metastasis through Enzymatic Degradation of Heparan sulfate-like Glycosaminoglycans Proc. Natl. Acad Sci. USA 99, 568-73.
Editorial Commentary (2002): Six blind men and the elephant - The many faces of heparan sulfate. Proc. Natl. Acad. Sci. USA 99, 543-5.
Sasisekharan, R., Shriver, Z., & Narayanasami U., (2002) Roles of Heparan sulphate Glycosaminoglycans in Tumorigenesis. Nature Reviews Cancer; 2, 521-8
Shriver, Z., Raman, R., Venkataraman, G., Drummond, K., Turnbull, J., Toida., T., Linhardt, R., Biemann, K., & Sasisekharan, R (2000) Sequencing of 3-O Sulfate Containing Heparin Decasaccharides With a Partial Antithrombin III Binding Site, Proc. Natl. Acad. Sci. U.S.A. 97(19):10359-10364.
Shriver, Z., Sundaram, M., Venkataraman, G., Fareed, J., Linhardt, R., Biemann, K., & Sasisekharan, R (2000) Cleavage of the Antithrombin III Binding Site in Heparin by Heparinases: Implication in the Generation of Low Molecular Weight Heparin, Proc. Natl. Acad. Sci. U.S.A. 97(19):10365-10370.
Editorial commentary in PNAS: Heparin sequencing brings structure to the function of complex oligosaccharides. PNAS 2000 97: 10301-10303.
Keiser, N, Venkataraman, G., Shriver, Z., & Sasisekharan R., (2000) Direct isolation and sequencing of specific protein-binding glycosaminoglycans on a chip Nature Medicine 7:123-128.
Sasisekharan, R & Venkataraman, G., (2000) Heparin and Heparan Sulfate: Biosynthesis, Structure and Function Current Opinion in Chemical Biology, 4:6:626-631.
Venkataraman, G., Shriver, Z., Raman, R., & Sasisekharan, R. (1999) Sequencing Complex Polysaccharides. Science 286:537-542.
Binari, R.C., Staveley, B. E., Godavarti, R., Sasisekharan, R. & Manoukian, A.S. (1997) Genetic Evidence that Heparin-like Glycosaminoglycans are Required for wingless Signaling. Development 124, 2623-2632.
Ernst, S., Cooney, C. L., Langer, R. & Sasisekharan, R. (1995) Glycosaminoglycan Degrading Enzymes. Critical Reviews in Biochemistry & Molecular Biology 30, 387-444.