Sheldon R. Gordon
Lab Location: 309 DHE, 311 DHE
Lab Phone: (248) 370-4218
Degree: Ph.D. University of Vermont, 1980
- BlO 104 Human Biology
- BlO 207 Human Physiology
- BIO 309 Biology of the Cell
- BIO 323 Developmental Biology
Research: Regulation of cell migration along natural extracellular matrices during wound repair; cytoskeletal function and cell-matrix interactions during mitosis and cell movement.
Sheldon Gordon is currently investigating mechanisms regulating corneal endothelial wound repair along its natural basement membrane (Descemet’s membrane), as well as the accompanying cytoskeletal changes and cell-matrix interactions that also occur during cell movement. The endothelium is a cell monolayer that is responsible for maintaining corneal hydration and thus tissue transparency. Recent work has focused on a soybean agglutinin (SBA) binding protein on the cell surface that appears in situations involving either stress or injury. Interfering with this protein prevents the reformation of cell-cell contact, disrupts the actin cytoskeleton and alters the expression of ZO-1, a cell junction protein during wound repair. In addition, although cell migration appears unaffected, cellular processes become blunted and fail to significantly extend from the cell body. Additional work on cell motility in his laboratory has also explored the roles of actin and tubulin during injury-induced cell movement and protease involvement in migration. His research has been funded by the National Eye Institute and the Michigan Eye Bank, and he has been an invited speaker at the 6th 7th, 8th and 14th meetings of the International Congress of Eye Research, and at the I st, 2nd and 3rd Congresses of Cellular and Molecular Biology. In addition, Dr. Gordon served on the editorial board of the journal Cellular and Molecular Biology and currently serves on the editorial boards of the Journal of Cytology and Molecular Biology and Journal of Cell Biology and Histology.
Gordon, S.R. (2014) Fibronectin antibody labels corneal stromal collagen fibrils in situ along their length and circumference and demonastrates distinct staining along the cell and stromal interfaces of Descemet's membrane. Curr Eye Res 39:312-316.
Gordon. S.R. (2011) The effects of soybean agglutinin binding on the corneal endothelium and the re-establishment of an intact monolayer following injury--a short review. J. Tiss. Viabil. 20:20-29.
Gordon. S.R. (2009) Cell migration along the basement membrane during wound repair. The cornea! endothelium as a model system. In Bioengineering Research of Chronic Wounds, SMTEB I. A. Gefen (ed.) Springer-Verlag. 43-84.
Gordon, S.R. and Wood. M. (2009) Soybean agglutinin binding to corneal endothelium cell surfaces disrupts in situ monolayer integrity and actin organization and interferes with wound repair. Cell Tiss. Res. 335: 551-563.
Gordon, S.R., Climie. M. and Hitt, A.L. (2005) 5-Fluorouracil interferes with actin organization, stress fiber formation and cell migration in corneal endothelial cells during wound repair along the natural basement membrane. Cell Motil. Cytoskel. 62: 244-258.
Gordon, S.R. (2002) Microfilament disruption in a noncycling organized tissue, the corneal endothelium, initiates mitosis. Exp. Cell Res. 272:127-134.
Gordon, S.R. and DeMoss, J. (1999) Exposure to lysosomotropic amines and protease inhibitors retard cornea! endothelial cell migration along the natural basement membrane during wound repair. Exp. Cell Res. 246: 233-242.
Gordon, S.R., Czwerwinski-Mowers, D., Marchand, J. and Shuffett, R. (1998) Endocytosis by the corneal endothelium. I. Regulation of binding and transport of hemeproteins and peroxidase-conjugated lectins across the tissue. Histochem. Cell Biol. 110: 251-262.
Gordon, S.R. and Buxar, R.M . (1997) Inhibition of cytoskeletal reorganization stimulates actin and tubular syntheses during injury-induced cell migration in the corneal endothelium. J. Cell Biochem. 67: 409-42 1.
Gordon, S.R. and Wood, M. (1997) Soybean (Glycine max) agglutinin binds to corneal endothelial cells during wound repair and alters their microfilament pattern. Cell Molec. Biol. 43: 329-336.