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Characterization of sodium‐independent β‐alanine binding to cerebral cortical membranes from 7‐day‐old and adult mice
Author(s) -
Saransaari Pirjo,
Oja Simo S.
Publication year - 1994
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(94)90033-7
Subject(s) - strychnine , alanine , glycine , glycine receptor , cerebral cortex , serine , binding site , chemistry , receptor , biochemistry , medicine , biology , endocrinology , amino acid , enzyme
The sodium‐independent binding of β‐alanine to cerebral cortical membranes from adult (3‐ and 12‐month‐old) and developing (7‐day‐old) mice was characterized for the first time. The binding was saturable in each age group, consisting of only one component. The affinity for β‐alanine was highest and the number of available binding sites greatest in young animals. The binding was not affected by strychnine, but inhibited by β‐alanine itself, glycine, l ‐alanine and l ‐serine, the IC 50 values being lower in immature mice. Glycine was shown to be a competitive inhibitor. The binding was also inhibited, albeit only in adults, by N ‐methyl‐ d ‐aspartate receptor antagonists acting at the glycine modulatory site and by some GABAergic substances. It is concluded that even though β‐alanine may possess binding sites of its own, particularly in the immature cerebral cortex, β‐alanine could at least partly bind to strychnine‐insensitive glycine sites in the N ‐methyl‐ d ‐aspartate receptor complex.