Monomeric and polymeric forms of ependymin: a brain extracellular glycoprotein implicated in memory consolidation processes.
Ependymin, a brain extracellular glycoprotein that appears to be implicated in neural circuit modifications associated with the process of memory consolidation, can rapidly polymerize into fibrous aggregates when the Ca2+ concentration in solution is reduced by the addition of EGTA or by dialysis. Such aggregates, once formed, could not be redissolved in boiling 1% SDS in 6 M urea, acetic acid, saturated aqueous potassium thiocyanate, and trifluoroacetic acid. They were, however, soluble in formic acid. Investigations of the immunological properties of ependymin indicated that various monomers, oligomers and polymers of the molecule with differing carbohydrate contents can be obtained. The polymerization properties of the ependymins may play an important role in their functions in memory consolidation mechanisms.
Shashoua
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Ralph Lowell Laboratories, McLean Hospital, Harvard Medical School, Belmont, MA 02178.
D000818:Animals; D001923:Brain Chemistry; D005110:Extracellular Space / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification*; D006054:Goldfish; D008568:Memory / Q000502:physiology; D008968:Molecular Conformation; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*
D006023:Glycoproteins; D009419:Nerve Tissue Proteins; C031632:ependymins