The cell surface localization and structural diversity of neuronal glycoproteins has resulted in the proposal that these molecules are important in cell recognition processes related to axon growth. Accordingly, alterations in cell surface glycoproteins, particularly those binding the mannose-specific lectin Concanavalin A, have been documented in developing neurons. However, a paucity of information has been provided concerning the molecular nature of these lectin receptors. This study investigated the properties, including lectin affinity, of axonally transported glycoproteins and their carbohydrate chains in regenerating garfish olfactory nerve. / Results of this study show that regeneration-related axon growth is accompanied by a two-fold increase in the proportion of low molecular weight (MW) carbohydrate chains associated with glycoproteins. When Con A affinity of the total glycopeptide fraction is assessed, the greatest proportional increase in Con A binding occurs in the low MW fraction. An analysis of the composition of these low MW Con A-binding molecules reveals a typical mannose-rich structure. This study also indicates that the proportion of radioactivity in low MW Con A-binding glycopeptides exhibits increases over intact nerve at all post-operative times analyzed, but to a significantly greater extent at earlier regeneration times. This result may indicate a participation by these molecules in axon-environmental interactions during axon growth. Consistent with this view, these mannose-rich glycopeptides are enriched 15-fold during axon growth in an axonal subcellular fraction that may resemble the cell surface coat or glycocalyx. / The analysis of intact glycoprotein molecules in garfish olfactory nerve reveals regeneration-dependent increases in the transport of glycoproteins with MWs of 180-200k, 105-115k and 80-90k daltons and a diminution in the transport of a 150-160k component. Con A fractionation of intact glycoproteins shows that in regenerating nerve an augmented proportion of glycoprotein radioactivity binds the lectin, with the largest growth-correlated increases occurring in molecules with MWs of 180-200k and 80-115k daltons. It can also be assumed that these Con A-binding glycoproteins probably contain a significant fraction of the mannose-rich carbohydrate chains described above. / Source: Dissertation Abstracts International, Volume: 43-07, Section: B, page: 2084. / Thesis (Ph.D.)--The Florida State University, 1982.
| Identifer | oai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_74892 |
| Contributors | COLE, GREGORY JAY., Florida State University |
| Source Sets | Florida State University |
| Detected Language | English |
| Type | Text |
| Format | 198 p. |
| Rights | On campus use only. |
| Relation | Dissertation Abstracts International |
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