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Changes in Subcellular Distribution of Ependymins in Goldfish Brain Induced by Learning
Author(s) -
Schmidt Rupert
Publication year - 1987
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1987.tb05750.x
Subject(s) - extracellular , cytoplasm , differential centrifugation , radioimmunoassay , chemistry , centrifugation , antiserum , memory consolidation , glycoprotein , chromatography , biochemistry , biology , endocrinology , antibody , immunology , hippocampus
Goldfish were trained for 4 h to swim with an attached polystyrene foam float and tested for retention 3 days later. Intracerebroventricular injection of anti‐ependymin antisera was shown to prevent long‐term memory formation of this vestibulomotor learning task, as reported previously. In further experiments, fish were killed 4–14 h after the start of training. The brains were dissected, incubated in an isoosmolar solution for collection of proteins of the brain extracellular fluid (ECF), homogenized, and fractionated by differential centrifugation. The ECF, a supernatant fraction enriched in cytoplasmic constituents (S3), and various par‐ticulate subcellular fractions were analyzed for their epen‐dymin contents by radioimmunoassay. No statistically significant changes that might be induced by the learning were revealed in any of the participate fractions. Steady‐state concentrations of ependymins in the cytoplasm, however, increased temporarily by 39% in fish that had mastered the training task as compared with nonlearning animals (passive and active controls). In the ECF, the specific concentration of ependymins first decreased to 88% of control levels (4–5 h after the start of training), but later on, it increased to 138% (8–14 h). Apparently, ependymins present in the ECF are used during biochemical reactions of memory consolidation. The resulting decrease in extracellular epen‐dymin concentrations might trigger their resynthesis in the cytoplasm and lead to an increased release of these glyco‐proteins into the ECF.