Sara Szuchet, PhD


Education & Training
  • Doctor of Philosophy, Cambridge University, UK
  • Tucker-Price Research Scholar, Girton College, Cambridge, UK
  • Oliver Gatty Research Student, University of Cambridge, UK
  • Post-doctoral Fellow, Department of Chemistry, Princeton University
  • National Multiple Sclerosis Fellow, Department of Neurology, University of Chicago
  • American Cancer Society Scholar, Cancer Research Foundation, La Jolla, CA
  • Dana Haughton Senior Fellow, Cancer Research Foundation, La Jolla, CA
  • National Research Service Visiting Scientist, Developmental Genetics, NINDS, NIH
Research Interests
  • Etiology and Pathogenesis of Multiple Sclerosi
  • The long-term goals are directed at deciphering the signaling pathways and at identifying the key molecules that are instrumental in segregating oligodendrocytes (OLGs) into their different phenotypes. We aim at elucidating the events that direct some OLGs toward axons in order to enwrap them with myelin, and others to associate with neuronal somata to become satellites.
  • Current research centers on delineating the biological function of proteins identified in our laboratory and believed to play critical roles in OLGs and other glial cells, but not in astrocytes. They are listed below.
  • OTMP is an OLG transmembrane protein that in white mater is present in OLG precursors prior to their commitment to the myelinating phenotype and in gray matter is found in OLGs abutting neuronal somata.
  • NOVOcan is a member of the BTB family – the BTB is a highly conserved domain that partakes in protein-protein interaction. NOVOcan is present in OLGs during early stages of differentiation; it is also found in embryonic and neonate radial glial cells but not their progeny, neurons and astrocytes. Novocan is expressed by ependymal cells and tanycytes throughout their life.
  • GRASP behaves as an adhesion molecule for OLGs. We speculate that GRASP functions as a surrogate for an axonal protein. We are attempting to identify its putative receptor on the surface of OLGs.
Selected Publications
  1. Szele F, and Szuchet S (2004). Cells lining the ventricular system: evolving concepts underlying developmental events in the embryo and adult. Adv. Mol. Cell Biol. 31: 127 – 147.
  2. Szuchet S and Seeger MA (2004). Oligodendrocyte phenotypical and morphological heterogeneity: a reexamination of old concepts in view of new findings. Adv. Mol. Cell Biol. 31: 53 – 74.
  3. Szuchet S, Seeger MA, Plachetzki D, Domowicz MS, Szele FG, (2004). NOVOcan: A molecular link among selected glial cells. Biophys Chem 108: 245 – 258.
  4. Szuchet S, Plachetzki DC and Karialukas R (2002). Oligodendrocytes express an α/β interferon-susceptible Mx gene: molecular characterization of the encoded protein. Glia. 37:183-189.
  5. Szuchet S, Plachetzki DC and Eaton KS (2001). Oligodendrocyte transmembrane protein: A novel member of the glutamate-binding protein subfamily. Biochem. Biophys. Res. Commun. 283:900-907.
  6. Szuchet S, Watanabe K and Yamaguchi Y (2000). Regeneration/differentiation of oligodendrocytes entails the assembly of a cell-associated matrix. Intl. J. Dev. Neurosci. 18:705-720.
  7. Szuchet S (1995). The morphology of cultured oligodendrocytes and its functional implication. In: Neuroglial Cells (H Kettenmann and B Ransom, eds. ). Oxford University Press, New York, pp. 23-43.
  8. LoPresti, P, Szuchet S, Papasozomenos SC, Zinkowski RP and Binder LI (1995). New functional implications for microtubule-associated protein TAU: localization in oligodendrocytes. PNAS 92,10369 -10373.
  9. Schirmer E, Farooqui J, and Szuchet S (1994). GRASP: A novel heparin-binding serum glycoprotein that mediates oligodendrocyte-substratum adhesion. J. Neurosci. Res. 39, 457-473.
  10. Ludwin SK and Szuchet S (1993). Myelination by mature ovine oligodendrocytes in vivo and in vitro: evidence that different steps in the myelination process are independently controlled. Glia 8, 219-31.
  11. Arvanitis D, Polak PE, and Szuchet S (1992). Myelin palingenesis: I. Electron miscroscopical localization of myelin/oligodendrocyte proteins in multilamellar structures by the immunogold method. Dev. Neurosci. 14, 313-327.
  12. Arvanitis D, Dumas M, and Szuchet S (1992). Myelin palingenesis: II. Immunocytochemical localization of myelin/oligodendrocyte lipids in multilamellar structures. Dev. Neurosci. 14, 328-335.
  13. Yim SH, Szuchet S and Polak PE (1986). Cultured oligodendrocytes: a role for cell-substratum interaction in phenotypic expression. J. Biol. Chem. 261, 11808-11815.
  14. Vartanian T, Szuchet S, Dawson G and Campagoni AT (1986). Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein. Science 234, 1395-1397.