Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein
Galectin-1 (Gal-1), a ubiquitous P-galactoside-binding protein expressed by various normal and pathological tissues, has been implicated in cancer and autoimmune/inflammatory diseases in consequence of its regulatory role in adhesion, cell viability, proliferation, and angiogenesis. The functions of...
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| Dokumentumtípus: | Cikk |
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Wiley-VCH Verlag GmbH & Co. KGaA
2010
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| Sorozat: | CHEMBIOCHEM
11 No. 2 |
| doi: | 10.1002/cbic.200900502 |
| mtmt: | 1321061 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/7552 |
| Tartalmi kivonat: | Galectin-1 (Gal-1), a ubiquitous P-galactoside-binding protein expressed by various normal and pathological tissues, has been implicated in cancer and autoimmune/inflammatory diseases in consequence of its regulatory role in adhesion, cell viability, proliferation, and angiogenesis. The functions of Gal-1 depend on its affinity for P-galactoside-containing glycoconjugates; accordingly, the inhibition of sugar binding blocks its functions, hence promising potential therapeutic tools. The Tyr-Xxx-Tyr peptide motifs have been reported to be glycomimetic sequences, mainly on the basis of their inhibitory effect on the Gal-1-asialofetuin (ASF) interaction. However, the results regarding the efficacy of the Tyr-Xxx-Tyr motif as a glycomimetic inhibitor are still controversial. The present STD and trNOE NMR experiments reveal that the Tyr-Xxx-Tyr peptides studied do not bind to Gal-1, whereas their binding to ASF is clearly detected. N-15,H-1 HSQC titrations with N-15-labeled Gal-1 confirm the absence of any peptide-Gal-1 interaction. These data indicate that the Tyr-Xxx-Tyr peptides tested in this work are not glycomimetics as they interact with ASF via an unrevealed molecular linkage. |
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| Terjedelem/Fizikai jellemzők: | 228-234 |
| ISSN: | 1439-4227 |