Department Affiliation: Primary: Pharmacology and Molecular Sciences; Secondary: Neuroscience
Degree:Ph.D., Johns Hopkins University
Rank: Professor
Telephone Number: 410-955-8392
Fax Number: 410-955-4900
Email Address: schnaar@jhu.edu
Homepage URL: http://www.hopkinsmedicine.org/schnaar/
School of Medicine Address: 324 Wood Basic Science Building, 725 N. Wolfe Street, Baltimore, Maryland 21205
Molecular basis of cell-cell interactions in the nervous system; axon regeneration; Glycobiology
We explore the molecular mechanisms neural cells use to communicate with each other when they come into contact. This type of communication, Cell-Cell Recognition, is important to nervous system development, and the maintenance of proper intercellular contacts in the adult brain.
Cell-cell recognition occurs when complementary molecules on apposing cell surfaces meet. A receptor on one cell surface binds to its specific ligand on a nearby cell, initiating a cascade of events that regulates cell behaviors ranging from simple adhesion to cellular differentiation.
Complex carbohydrates, consisting of glycoproteins and glycolipids, decorate all cell surfaces, and represent the most prominent class of cell surface molecules. Members of this large and highly varied family act as ligands for complementary binding proteins, called lectins, on nearby cells. Lectin-glycan interactions mediate intercellular interactions in the brain and throughout the body. The study of cell surface glycans, lectins, and their roles in cell physiology are part of the rapidly emerging discipline called Glycobiology.
Current work in our laboratory focuses on Neuroglycobiology. Neural cells are rich in cell surface glycans called Gangliosides. We discovered that members of the ganglioside family are ligands for an important cell recognition protein called "Myelin-Associated Glycoprotein," or MAG. Our evidence demonstrates that MAG binds to gangliosides on nerve cells to initiate cell-cell recognition which is important for the long-term maintenance of Myelin, the essential insulation surrounding nerve cell axons. Myelin loss results in diseases such as multiple sclerosis. We also have shown that MAG-ganglioside interactions block Axon Regeneration after nervous system injury, such as paralytic spinal cord injury. A molecular understanding of these interactions may provide new ways to intervene in these disorders and enhance recovery.
Representative Publications:
- Mehta, N.R., Lopez, P.H.H., Vyas, A.A., and Schnaar R.L. Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells, J. Biol. Chem. 282:27875-27886, 2007. Pub Med Reference
- Whitmore C.D., Hindsgaul O., Palcic M.M., Schnaar R.L., and Dovichi N.J. Metabolic cytometry. Glycosphingolipid metabolism in single cells, Anal. Chem. 79:5139-5142, 2007. Pub Med Reference
- Yang, L.J.S, Lorenzini, I., Vajn, K., Mountney, A., Schramm, L.P., and Schnaar, R.L. Sialidase enhances spinal axon outgrowth in vivo, Proc. Natl. Acad. Sci. USA 103:11057-11062, 2006. Pub Med Reference
- Pan, B., Fromholt, S.E., Hess, E.J., Crawford, T.O., Griffin, J.W., Sheikh, K.A., and Schnaar, R.L. Myelin-associated glycoprotein and gangliosides mediate axon-myelin stability: Neuropathology and behavioral deficits in single- and double-null mice, Exp. Neurol. 195:208-217, 2005. Pub Med Reference
- Vyas, A.A., Blixt, O., Paulson, J.C., and Schnaar, R.L. Potent glycan inhibitors of myelin-associated glycoprotein enhance axon outgrowth in vitro, J. Biol. Chem. 280: 16305-16310, 2005. Pub Med Reference
- Bochner, B.S., Alvarez, R.A., Mehta, P., Bovin, N.V., Blixt, O., White, J.R., and Schnaar, R.L. Glycan array screening reveals a candidate ligand for Siglec-8, J. Biol. Chem. 280: 4307-4312, 2005. Pub Med Reference
Other graduate programs in which Dr. Schnaar participates:
BCMB Program
Anti-Cancer Drug Development Program
Neuroscience Graduate Program
Molecular basis of cell-cell interactions in the nervous system; axon regeneration; Glycobiology
We explore the molecular mechanisms neural cells use to communicate with each other when they come into contact. This type of communication, Cell-Cell Recognition, is important to nervous system development, and the maintenance of proper intercellular contacts in the adult brain.
Cell-cell recognition occurs when complementary molecules on apposing cell surfaces meet. A receptor on one cell surface binds to its specific ligand on a nearby cell, initiating a cascade of events that regulates cell behaviors ranging from simple adhesion to cellular differentiation.
Complex carbohydrates, consisting of glycoproteins and glycolipids, decorate all cell surfaces, and represent the most prominent class of cell surface molecules. Members of this large and highly varied family act as ligands for complementary binding proteins, called lectins, on nearby cells. Lectin-glycan interactions mediate intercellular interactions in the brain and throughout the body. The study of cell surface glycans, lectins, and their roles in cell physiology are part of the rapidly emerging discipline called Glycobiology.
Current work in our laboratory focuses on Neuroglycobiology. Neural cells are rich in cell surface glycans called Gangliosides. We discovered that members of the ganglioside family are ligands for an important cell recognition protein called "Myelin-Associated Glycoprotein," or MAG. Our evidence demonstrates that MAG binds to gangliosides on nerve cells to initiate cell-cell recognition which is important for the long-term maintenance of Myelin, the essential insulation surrounding nerve cell axons. Myelin loss results in diseases such as multiple sclerosis. We also have shown that MAG-ganglioside interactions block Axon Regeneration after nervous system injury, such as paralytic spinal cord injury. A molecular understanding of these interactions may provide new ways to intervene in these disorders and enhance recovery.
Representative Publications:
- Mehta, N.R., Lopez, P.H.H., Vyas, A.A., and Schnaar R.L. Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells, J. Biol. Chem. 282:27875-27886, 2007. Pub Med Reference
- Whitmore C.D., Hindsgaul O., Palcic M.M., Schnaar R.L., and Dovichi N.J. Metabolic cytometry. Glycosphingolipid metabolism in single cells, Anal. Chem. 79:5139-5142, 2007. Pub Med Reference
- Yang, L.J.S, Lorenzini, I., Vajn, K., Mountney, A., Schramm, L.P., and Schnaar, R.L. Sialidase enhances spinal axon outgrowth in vivo, Proc. Natl. Acad. Sci. USA 103:11057-11062, 2006. Pub Med Reference
- Pan, B., Fromholt, S.E., Hess, E.J., Crawford, T.O., Griffin, J.W., Sheikh, K.A., and Schnaar, R.L. Myelin-associated glycoprotein and gangliosides mediate axon-myelin stability: Neuropathology and behavioral deficits in single- and double-null mice, Exp. Neurol. 195:208-217, 2005. Pub Med Reference
- Vyas, A.A., Blixt, O., Paulson, J.C., and Schnaar, R.L. Potent glycan inhibitors of myelin-associated glycoprotein enhance axon outgrowth in vitro, J. Biol. Chem. 280: 16305-16310, 2005. Pub Med Reference
- Bochner, B.S., Alvarez, R.A., Mehta, P., Bovin, N.V., Blixt, O., White, J.R., and Schnaar, R.L. Glycan array screening reveals a candidate ligand for Siglec-8, J. Biol. Chem. 280: 4307-4312, 2005. Pub Med Reference
Other graduate programs in which Dr. Schnaar participates:
BCMB Program
Anti-Cancer Drug Development Program
Neuroscience Graduate Program
