We are analyzing https://link.springer.com/article/10.1007/s00109-006-0073-1.

Title:
A CD40–CD95L fusion protein interferes with CD40L-induced prosurvival signaling and allows membrane CD40L-restricted activation of CD95 | Journal of Molecular Medicine
Description:
We analyzed a novel bifunctional fusion protein, CD40ed–CD95Led, consisting amino-terminally of the extracellular domain of CD40 and carboxy-terminally of the extracellular domain of CD95L. On cells lacking CD40L, this fusion protein is poorly active with respect to CD95 activation [median effective dose (ED50)>1 μg/ml], but it stimulates CD95 signaling with high efficiency upon binding to membrane-expressed CD40L (ED50<1 ng/ml). Thus, cell surface immobilization mediated by the CD40 part of the molecule unmasks the high-latent, CD95-stimulating capacity of the otherwise poorly active CD95L fusion protein. Moreover, interaction of the CD40 part of CD40ed–CD95Led with CD40L prevents the activation of cellular CD40. The CD40ed–CD95Led fusion protein therefore simultaneously blocks antiapoptotic CD40 activation and induces CD95-mediated apoptosis. Indeed, T47D cells displaying an antiapoptotic autocrine CD40–CD40L signaling loop were significantly more sensitive toward CD40ed–CD95Led than toward soluble CD95L artificially activated by crosslinking. Fusion proteins of RANK and CD95L (RANKed–CD95Led) and CD40 and tumor necrosis factor-related apoptosis inducing ligand (TRAIL) (CD40ed–TRAILed), with domain architectures similar to CD40ed–Cd95Led, displayed RANKL-dependent CD95 and CD40L-dependent TRAILR2 activation, respectively, indicating the principle feasibility of this fusion protein design.
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article, pubmed, cas, google, scholar, fusion, activation, cell, apoptosis, protein, signaling, wajant, tumor, ligand, trail, pfizenmaier, cdl, necrosis, factor, gerspach, med, immunol, privacy, cookies, content, journal, cdcdl, cdedcdled, soluble, factorrelated, access, death, tnf, growth, rev, information, publish, search, membrane, assohouluty, siegmund, harald, domain, cancer, autoimmune, biology, mol, apoptosisinducing, nat, biol,

Topics {✒️}

tnf-related apoptosis-inducing ligand month download article/chapter cell-surface antigen-restricted activation induces cd95-mediated apoptosis signal fadd-dependent apoptosis tumor necrosis factor cd95/cd95l signaling pathway autocrine anti-apoptotic role receptor-mediated apoptosis induction trail-induced apoptosis—results displayed rankl-dependent cd95 membrane cd40l-restricted activation cd40l-induced prosurvival signaling tnf/tnfr family members cd40ed–cd95led fusion protein recombinant apo2l/trail versions cd40l-dependent trailr2 activation bertrand huard cutaneous t-cell lymphoma accelerated autoimmune diseases defective thymocyte apoptosis bifunctional fusion protein strail fusion protein article assohou-luty membrane-bound fas fusion protein design programmed cell death stimulates cd95 signaling full article pdf membrane-expressed cd40l privacy choices/manage cookies author information authors membrane-anchored tnf cd95-stimulating capacity related subjects enhanced apoptosis induction target cell-restricted autonomous cell growth tnf receptor superfamilies fusion protein dose–response studies experimental autoimmune encephalomyelitis apoptosis signaling cd40/cd154 interactions cd40 signalosome anchored harald wajant apoptosis induced linked therapeutic targets cells lacking cd40l cd40 ligand

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         headline:A CD40–CD95L fusion protein interferes with CD40L-induced prosurvival signaling and allows membrane CD40L-restricted activation of CD95
         description:We analyzed a novel bifunctional fusion protein, CD40ed–CD95Led, consisting amino-terminally of the extracellular domain of CD40 and carboxy-terminally of the extracellular domain of CD95L. On cells lacking CD40L, this fusion protein is poorly active with respect to CD95 activation [median effective dose (ED50)>1 μg/ml], but it stimulates CD95 signaling with high efficiency upon binding to membrane-expressed CD40L (ED50<1 ng/ml). Thus, cell surface immobilization mediated by the CD40 part of the molecule unmasks the high-latent, CD95-stimulating capacity of the otherwise poorly active CD95L fusion protein. Moreover, interaction of the CD40 part of CD40ed–CD95Led with CD40L prevents the activation of cellular CD40. The CD40ed–CD95Led fusion protein therefore simultaneously blocks antiapoptotic CD40 activation and induces CD95-mediated apoptosis. Indeed, T47D cells displaying an antiapoptotic autocrine CD40–CD40L signaling loop were significantly more sensitive toward CD40ed–CD95Led than toward soluble CD95L artificially activated by crosslinking. Fusion proteins of RANK and CD95L (RANKed–CD95Led) and CD40 and tumor necrosis factor-related apoptosis inducing ligand (TRAIL) (CD40ed–TRAILed), with domain architectures similar to CD40ed–Cd95Led, displayed RANKL-dependent CD95 and CD40L-dependent TRAILR2 activation, respectively, indicating the principle feasibility of this fusion protein design.
         datePublished:2006-08-04T00:00:00Z
         dateModified:2006-08-04T00:00:00Z
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      headline:A CD40–CD95L fusion protein interferes with CD40L-induced prosurvival signaling and allows membrane CD40L-restricted activation of CD95
      description:We analyzed a novel bifunctional fusion protein, CD40ed–CD95Led, consisting amino-terminally of the extracellular domain of CD40 and carboxy-terminally of the extracellular domain of CD95L. On cells lacking CD40L, this fusion protein is poorly active with respect to CD95 activation [median effective dose (ED50)>1 μg/ml], but it stimulates CD95 signaling with high efficiency upon binding to membrane-expressed CD40L (ED50<1 ng/ml). Thus, cell surface immobilization mediated by the CD40 part of the molecule unmasks the high-latent, CD95-stimulating capacity of the otherwise poorly active CD95L fusion protein. Moreover, interaction of the CD40 part of CD40ed–CD95Led with CD40L prevents the activation of cellular CD40. The CD40ed–CD95Led fusion protein therefore simultaneously blocks antiapoptotic CD40 activation and induces CD95-mediated apoptosis. Indeed, T47D cells displaying an antiapoptotic autocrine CD40–CD40L signaling loop were significantly more sensitive toward CD40ed–CD95Led than toward soluble CD95L artificially activated by crosslinking. Fusion proteins of RANK and CD95L (RANKed–CD95Led) and CD40 and tumor necrosis factor-related apoptosis inducing ligand (TRAIL) (CD40ed–TRAILed), with domain architectures similar to CD40ed–Cd95Led, displayed RANKL-dependent CD95 and CD40L-dependent TRAILR2 activation, respectively, indicating the principle feasibility of this fusion protein design.
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      dateModified:2006-08-04T00:00:00Z
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         CD40
         CD95
         Fusion protein
         TRAIL
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         Human Genetics
         Internal Medicine
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            name:Gisa Tiegs
            affiliation:
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            address:
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      name:Gisa Tiegs
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            name:University of Erlangen-Nuremberg
            address:
               name:Institute of Experimental and Clinical Pharmacology and Toxicology, University of Erlangen-Nuremberg, Erlangen, Germany
               type:PostalAddress
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      name:Department of Molecular Internal Medicine, Medical Clinic and Polyclinic II, University of Wuerzburg, Wuerzburg, Germany
      name:Department of Molecular Internal Medicine, Medical Clinic and Polyclinic II, University of Wuerzburg, Wuerzburg, Germany
      name:Dermatology Department, Geneva University Medical Center, Geneva 4, Switzerland
      name:Institute of Experimental and Clinical Pharmacology and Toxicology, University of Erlangen-Nuremberg, Erlangen, Germany
      name:Institute of Cell Biology and Immunology, University of Stuttgart, Stuttgart, Germany
      name:Department of Molecular Internal Medicine, Medical Clinic and Polyclinic II, University of Wuerzburg, Wuerzburg, Germany
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