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Further Evidence for Multiple Forms of an N-Methyl-d-Aspartate Recognition Domain in Rat Brain Using Membrane Binding Techniques
| Content Provider | Scilit |
|---|---|
| Author | Zuo, Pingping Ogita, Kiyokazu Suzuki, Takeo Han, Daiken Yoneda, Yukio |
| Copyright Year | 1993 |
| Description | Journal: Journal of Neurochemistry Pretreatment with sulfhydryl-reactive agents, such as N-ethylmaleimide and p-chloromercuriphenylsulfonic acid, invariably resulted in marked inhibition of the binding of DL-(E)-2-amino-4-[3H]propyl-5-phosphono-3-pentenoic acid ([3H]CGP 39653), a competitive antagonist at an N-methyl-D-aspartate (NMDA)-sensitive subclass of central excitatory amino acid receptors, in brain synaptic membranes extensively washed and treated with Triton X-100, but did not significantly affect the binding of L-[3H]-glutamic acid ([3H]Glu), an endogenous agonist. The pretreatment was effective in reducing the binding of [3H]-CGP 39653 at equilibrium, without altering the initial association rate, and decreased the affinity for the ligand. Pretreatment with sulfhydryl-reactive agents also enhanced the potencies of NMDA agonists to displace [3H]-CGP 39653 binding and attenuated those of NMDA antagonists, but had little effect on the potencies of the agonists and antagonists to displace [3H]Glu binding. The binding of both [3H]CGP 39653 and [3H]Glu was similarly sensitive to pretreatment with four different proteases in Triton-treated membranes, whereas pretreatment with phospholipase A2 or C markedly inhibited [3H]CGP 39653 binding without altering [3H]Glu binding. Moreover, both phospholipases not only induced enhancement of the abilities of NMDA agonists to displace the binding of [3H]CGP 39653 and [3H]Glu, but also caused diminution of those of NMDA antagonists. These results suggest that both sulfhydryl-reactive agents and phospholipases may predominantly interfere with radiolabeling of the NMDA recognition domain in a state favorable to an antagonist by [3H]CGP 39653, with concomitant facilitation of that in an antagonist-preferring form by [3H]Glu. The possible presence of multiple forms of the NMDA recognition domain is further supported by these data. |
| Related Links | http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.1993.tb09828.x/pdf |
| Ending Page | 1873 |
| Page Count | 9 |
| Starting Page | 1865 |
| e-ISSN | 14714159 |
| DOI | 10.1111/j.1471-4159.1993.tb09828.x |
| Journal | Journal of Neurochemistry |
| Issue Number | 5 |
| Volume Number | 61 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1993-11-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Neurochemistry Biochemistry and Molecular Biology N‐methyl‐d‐aspartate [3h]cgp 39653 Binding [3h]glutamate Bindin Ntagonist‐preferring for Gonist‐preferring for |
| Content Type | Text |
| Resource Type | Article |