| Autor: |
Minami, Kazushi, Raymond, Cecile, Martin-Moutot, Nicole, Ohtake, Atsuko, Van Renterghem, Catherine, Takahashi, Masami, Seagar, Michael J., Mori, Yasuo, Sato, Kazuki |
| Zdroj: |
FEBS Letters; January 2001, Vol. 491 Issue: 1 p127-130, 4p |
| Abstrakt: |
As replacement of Thr 11of ω-conotoxin MVIIC with Ala significantly reduced the affinity for both N- and P/Q-type calcium channels, we examined the effect of substitution at this position with other residues. Binding assays using rat cerebellar P 2membranes showed that the affinity is in the order of Leu>Val, aminobutyric acid, Thr>Asn≫Ser, Ala, Asp, Phe, Tyr for N-type channels and Thr>Leu, Val, aminobutyric acid, Asn, Ser>Ala≫Asp, Phe, Tyr for P/Q-type channels, suggesting that aliphatic amino acids with longer side chains are favorable for block of N-type channels. The effects of substitution were examined electrophysiologically in BHK cells expressing N-type Ca 2+channels. Inhibition of Ba 2+current by the analogs did not completely correlate with binding affinity, although binding to BHK cells was comparable to rat cerebellar membranes. |
| Databáze: |
Supplemental Index |
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