Dr. Elam's research centers on the roles of glycoproteins in nerve-cell maintenance and response to injury. A particular focus is on molecules that are moved down the nerve-cell axon by the process of axonal transport and on a specific subclass of glycoproteins called proteoglycans. Axonal transport is known to be essential for maintaining the physiological viability of axons and synaptic terminals in mature neural tissue and for the formation of axons and synaptic terminals during development and nerve regeneration. Proteoglycans are of particular interest because they are found to play important functional roles in axonal-synaptic physiology and in the guidance of axons during developmental or regenerative growth.
Studies are conducted on fish because of the accessibility of certain elements of the nervous system and their remarkable capacity for nervous-system regeneration. Experiments are conducted in vivo to characterize axonally transported glycoproteins, whereas cell-culture studies are used to assess the various functions of the transported molecules.
The long-term objective of this research is to improve understanding of the functions of certain patterns of protein glycosylation in normal axonal and synaptic physiology and in the special molecular environments that favor axonal growth and synapse formation. It is particularly hoped that glycosylation patterns required for successful recovery from
nerve injury will be identifed.
- Pizzi M. A. and J.S. Elam 2004. Characterization of a chondroitin sulfate proteoglycan associated with regeneration in goldfish optic tract. Neurochemical Res. 29: 719-728
- Su, Y-K., and J.S. Elam. 2003. Proteoglycan regulation of goldfish retinal explant growth on optic tectal membranes. Dev Brain Res 142 : 169 - 175
- Su, Y-K., and J.S. Elam. 2002. Differential growth of goldfish retinal explants on regenerating and non-regenerating optic tract membranes. Dev Brain Res 139: 319-323.
- Challacombe, J. F., and J. S. Elam. 1997. Chondroitin 4-sulfate stimulates regeneration of retinal axons. Exper. Neurol. 143: 10-17.
- Elam, J. S. 1995. Further characterization of axonally transported proteoglycans. Neurochem. Res. 20: 187-193.
- Challacombe, J. F., and J. S. Elam. 1995. Structural analysis of glycosaminoglycans derived from axonally transported proteoglycans in regenerating goldfish optic nerve. Neurochem. Res. 20: 253-259.
- Challacombe, J. F., and J. S. Elam. 1995. Inhibition of proteoglycan synthesis influences regeneration of goldfish retinal axons on polylysine and laminin. Exp. Neurol. 134: 126-134.