| Autor: |
Jägerbrink T; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden., Lindahl E, Shafqat J, Jörnvall H |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2009 Sep 11; Vol. 387 (1), pp. 31-5. Date of Electronic Publication: 2009 Jun 18. |
| DOI: |
10.1016/j.bbrc.2009.06.074 |
| Abstrakt: |
Based on nickel-catalyzed cross-labeling where binding partners become biotinylated, we have studied molecular interactions with an N-terminally fused GGH-tag proinsulin C-peptide. Since C-peptide has been reported to influence phosphatase activity in intact cells, we employed this method to study possible binding of the peptide to protein tyrosine phosphatase 1B (PTP-1B). C-peptide was found to interact with PTP-1B (and for control, also with antibodies to C-peptide), as did also the N- and C-terminal fragments of C-peptide which have sequence similarities with PTP-1B binding proteins. The labeling data combined with enzyme activity analysis indicate a functional interaction between acidic regions of C-peptide and specific sites of PTP-1B. Results highlight the importance of possible phosphatase/C-peptide roles in diabetes, and the usefulness of the cross-labeling reaction also for acidic peptides like C-peptide. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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