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Titolo:
Temperature-sensitive differential affinity of TRAIL for its receptors - DR5 is the highest affinity receptor
Autore:
Truneh, A; Sharma, S; Silverman, C; Khandekar, S; Reddy, MP; Deen, KC; Mclaughlin, MM; Srinivasula, SM; Livi, GP; Marshall, LA; Alnemri, ES; Williams, WV; Doyle, ML;
Indirizzi:
SmithKline Beecham Pharmaceut, Dept Immunol, King Of Prussia, PA 19406 USASmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA SmithKline Beecham Pharmaceut, Dept Prot Biochem, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA SmithKline Beecham Pharmaceut, Dept Comparat Genet, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA SmithKline Beecham Pharmaceut, Dept Biol Struct, King Of Prussia, PA 19406USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 a, PA 19406USA SmithKline Beecham Pharmaceut, Clin Pharmacol Unit, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut King Of Prussia PA USA 19406 , PA 19406 USA Thomas Jefferson Univ, Kimmel Canc Inst, Philadelphia, PA 19107 USA ThomasJefferson Univ Philadelphia PA USA 19107 hiladelphia, PA 19107 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 30, volume: 275, anno: 2000,
pagine: 23319 - 23325
SICI:
0021-9258(20000728)275:30<23319:TDAOTF>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOTOXIC LIGAND TRAIL; NF-KAPPA-B; DEATH DOMAIN; CRYSTAL-STRUCTURE; INDUCED APOPTOSIS; PICHIA-PASTORIS; BINDING; MEMBER; FAMILY; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Truneh, A SmithKline Beecham Pharmaceut, Dept Immunol, 709 Swedeland Rd, King Of Prussia, PA 19406 USA SmithKline Beecham Pharmaceut 709 Swedeland RdKing Of Prussia PA USA 19406
Citazione:
A. Truneh et al., "Temperature-sensitive differential affinity of TRAIL for its receptors - DR5 is the highest affinity receptor", J BIOL CHEM, 275(30), 2000, pp. 23319-23325

Abstract

TRAIL is a member of the tumor necrosis factor (TNF) family of cytokines which induces apoptotic cell death in a variety of tumor cell lines. It mediates its apoptotic effects through one of two receptors, DR4 and DR5, whichare members of of the TNF receptor family, and whose cytoplasmic regions contain death domains. In addition, TRAIL also binds to 3 "decoy" receptors,DcR2, a receptor with a truncated death domain, DcR1, a glycosylphosphatidylinositol-anchored receptor, and OPG a secreted protein which is also known to bind to another member of the TNF family, RANKL. However, although apoptosis depends on the expression of one or both of the death domain containing receptors DR4 and/or DR5, resistance to TRAIL-induced apoptosis does not correlate with the expression of the "decoy" receptors. Previously, TRAILhas been described to bind to all its receptors with equivalent high affinities. In the present work, we show, by isothermal titration calorimetry and competitive enzyme-linked immunosorbent assay, that the rank order of affinities of TRAIL for the recombinant soluble forms of its receptors is strongly temperature dependent. Although DR4, DR5, DcR1, and OPG, show similar affinities for TRAIL at 4 degrees C, their rank-ordered affinities are substantially different at 37 degrees C, with DR5 having the highest affinity (K-D less than or equal to 2 nM) and OPG having the weakest (K-D = 400 nM). Preferentially enhanced binding of TRAIL to DR5 was also observed at the cell surface. These results reveal that the rank ordering of affinities for protein-protein interactions in general can be a strong function of temperature, and indicate that sizeable, but hitherto unobserved, TRAIL affinity differences exist at physiological temperature, and should be taken into account in order to understand the complex physiological and/or pathological roles of TRAIL.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/08/20 alle ore 07:04:50