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ABSTRACTS: 8
Identifying the receptor‐binding part of PIBF
Author(s) -
Halasz Melinda,
Polgar Beata,
Kozma Noemi,
Berta Gergely,
Toth Gabor,
SzekeresBartho Julia
Publication year - 2008
Publication title -
american journal of reproductive immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.071
H-Index - 97
eISSN - 1600-0897
pISSN - 1046-7408
DOI - 10.1111/j.1600-0897.2008.00626_8.x
Subject(s) - phosphorylation , exon , receptor , biology , signal transduction , blot , intracellular , microbiology and biotechnology , gene , computational biology , biochemistry
Problem: The PIBF1‐gene contains 18 exons and encodes a protein of 757 aminoacid residues with an 89‐kDa molecular mass. We aimed to identify the receptor‐binding region of the molecule, by its ability to activate signal transduction via JAK1/STAT6‐pathway in peripheral lymphocytes. Materials and Methods: Recombinant PIBF constructs and small synthetic PIBF analogues representing different regions of the molecule were designed. EMSA was performed to detect nuclear translocation of STAT6‐dimers while intracellular STAT6‐phosphorylation was tested by Western blotting. PIBF‐receptor binding ability of the selected analogue was confirmed by confocal microscopy. Results: Nuclear translocation of STAT6‐dimers was induced by PN1(exons 2‐3‐4), PN3(exons 8‐9), PN5(exons 3‐14‐15‐16) constructs. Peptide‐5 (in PN1) and 8 (in PN3‐4) were capable to activate STAT6‐phosphorylation. BodipyFL‐ labelled peptide‐8 bound to the PIBF‐receptor and was internalized in a time‐dependent manner. Conclusions: These data suggest that the receptor‐binding region of PIBF might be a conformational structure that includes remote sequences.