Academic Journal

Identification of an antiangiogenic FGF2-binding site in the N terminus of the soluble pattern recognition receptor PTX3.

التفاصيل البيبلوغرافية
العنوان: Identification of an antiangiogenic FGF2-binding site in the N terminus of the soluble pattern recognition receptor PTX3.
المؤلفون: CAMOZZI M, RUSNATI M, BUGATTI A, BOTTAZZI B, MANTOVANI A, BASTONE A, INFORZATO, A, VINCENTI S, BRACCI, LUISA, MASTROIANNI D, PRESTA M.
المساهمون: Camozzi, M, Rusnati, M, Bugatti, A, Bottazzi, B, Mantovani, A, Bastone, A, Inforzato, A, Vincenti, S, Bracci, Luisa, Mastroianni, D, Presta, M.
سنة النشر: 2006
المجموعة: Università degli Studi di Siena: USiena air
الوصف: Long-pentraxin 3 (PTX3) is a soluble pattern recognition receptor with non-redundant functions in inflammation and innate immunity. PTX3 comprises a pentraxin-like C-terminal domain involved in complement activation via C1q interaction and an N-terminal extension with unknown functions. PTX3 binds fibroblast growth factor-2 (FGF2), inhibiting its pro-angiogenic and pro-restenotic activity. Here, retroviral transduced endothelial cells (ECs) overexpressing the N-terminal fragment PTX3-(1-178) showed reduced mitogenic activity in response to FGF2. Accordingly, purified recombinant PTX3-(1-178) binds FGF2, prevents PTX3/FGF2 interaction, and inhibits FGF2 mitogenic activity in ECs. Also, the monoclonal antibody mAb-MNB4, which recognizes the PTX3-(87-99) epitope, prevents FGF2/PTX3 interaction and abolishes the FGF2 antagonist activity of PTX3. Consistently, the synthetic peptides PTX3-(82-110) and PTX3-(97-110) bind FGF2 and inhibit the interaction of FGF2 with PTX3 immobilized to a BIAcore sensor chip, FGF2-dependent EC proliferation, and angiogenesis in vivo. Thus, the data identify a FGF2-binding domain in the N-terminal extension of PTX3 spanning the PTX3-(97-110) region, pointing to a novel function for the N-terminal extension of PTX3 and underlining the complexity of the PTX3 molecule for modular humoral pattern recognition
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/16769728; info:eu-repo/semantics/altIdentifier/wos/WOS:000239542600021; volume:281; issue:32; firstpage:22605; lastpage:22613; numberofpages:9; journal:THE JOURNAL OF BIOLOGICAL CHEMISTRY; http://hdl.handle.net/11365/36608; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-33747336999
DOI: 10.1074/jbc.M601023200
الاتاحة: http://hdl.handle.net/11365/36608
https://doi.org/10.1074/jbc.M601023200
رقم الانضمام: edsbas.6882BCB8
قاعدة البيانات: BASE