TY  - JOUR
AU  - Wéber, Edit
AU  - Hetényi, Anasztázia
AU  - Váczi, Balázs
AU  - Szolnoki, Éva Tünde
AU  - Fajka-Boja, Roberta
AU  - Tubak, Vilmos
AU  - Monostori, Éva
AU  - Martinek, Tamás
TI  - Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein
JF  - CHEMBIOCHEM
J2  - CHEMBIOCHEM
VL  - 11
PY  - 2010
IS  - 2
SP  - 228
EP  - 234
PG  - 7
SN  - 1439-4227
DO  - 10.1002/cbic.200900502
UR  - https://m2.mtmt.hu/api/publication/1321061
ID  - 1321061
N1  - Chemicals/CAS: galectin 1, 258495-34-0; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; Asialoglycoproteins; Galectin 1; Glycoproteins; Peptides; Recombinant Proteins; Tyrosine, 55520-40-6; alpha-Fetoproteins; asialofetuin
Funding Agency and Grant Number: Hungarian Academy of Sciences; Hungarian Scientific Research Fund [K 69047, PD 75938]; NKTH-OTKA [CK 78188]; OTKA NF [69316]\n Funding text: A.H. and T.A.M. acknowledge the award of Janos Bolyai Research Fellowships by the Hungarian Academy of Sciences. This work was supported by grants from the Hungarian Scientific Research Fund (OTKA K 69047, PD 75938, NKTH-OTKA CK 78188, and OTKA NF 69316).\n
AB  - 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.
LA  - English
DB  - MTMT
ER  -