Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor

Loetscher, Hansruedi; Pan, Yu‐Ching E.; Lahm, Hans‐Werner; Gentz, Reiner; Brockhaus, Manfred; Tabuchi, Hisahiro; Lesslauer, Werner

doi:10.1016/0092-8674(90)90815-v

Cited by 859 publications

(334 citation statements)

References 39 publications

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“…48,49 Roles of TNFR family members in vivo TNF receptors TNFR1 is expressed on most cell types. 50,51 It has been regarded as the primary signalling receptor for TNF-α inflammatory responses, because TNFR1 knockout mice are resistant to endotoxic shock. 52,53 In addition, it has also been suggested that TNFR1 mediates signals required for proper formation of lymphoid structures such as primary B cell follicles and germinal centres, possibly through a defect in the development of follicular dendritic cells (FDC).…”

Section: Jnk Activationmentioning

confidence: 99%

Signalling by CD95 and TNF receptors: Not only life and death

Magnusson

Vaux

1999

Immunol Cell Biol

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The tumour necrosis factor receptor (TNFR)/nerve growth factor receptor (NGFR) family of molecules regulate a number of biological functions, such as growth, differentiation and apoptosis in multiple cell types. In the immune system, members of this receptor family are involved in the development of peripheral lymphoid organs, regulation of induced inflammatory responses and removal of cells at the end of an immune response.The TNFR family consists of more than 15 different molecules. Most are type I membrane proteins which resemble each other largely in their extracellular regions, which all contain 2-6 characteristic cysteine-rich domains. 1 The TNF family receptors are activated upon binding of their cognate ligands, most of which are trimers with a structure similar to TNF. Sometimes the ligands are cell bound type II membrane proteins, but several are cleaved off and appear as soluble trimers. Induction of trimers or higher order complexes of the TNF family of receptors allows their cytoplasmic domains to aggregate intracytoplasmic signalling molecules. Signalling pathways controlled by TNF receptorsThe cytoplasmic domains of the TNFR family, which are more diverse than the extracellular portions, do not have any intrinsic enzymatic activity, hence they signal by inducing aggregation of intracellular adaptor molecules (Fig. 1). Death domainsThe cytoplasmic domains of TNFR1 (p55), CD95 (Fas/ APO-1), NGFR (p75), death receptor (DR) 3, TRAIL-R1 and TRAIL-R2 all bear a motif termed a 'death domain' (DD), so-called because it is required for these receptors to transmit apoptotic signals. The DD is a protein-protein interaction motif consisting of six alpha helices that allow two proteins with DD to bind to each other. Structurally the DD is related to two other homotypic interaction domains, the death effector domain (DED), and the caspase recruitment domain (CARD). 2 Death domain adaptors: TRADD, FADD, RIP and RAIDDBinding of TNF to TNFR1 induces recruitment of the DDcontaining protein TRADD to the DD of TNFR1. 3 Overexpression of TRADD alone also induces the TNF-regulated responses apoptosis and activation of the transcription factors NF-κB and Jun kinase (JNK), presumably because TRADD provides docking sites for downstream signalling proteins to the receptor complex. 4 Two of the proteins that TRADD recruits to the signalling complex also bear death domains. One of these, RIP, has an N-terminal DD and a C-terminal kinase domain. Knockout studies have shown that RIP is required for induction of NFκB by TNF. 5 The other, Fas-associated protein with death domain (FADD), has a C-terminal DD, and an N-terminal DED. The FADD is required for cell death signalling by TNFR1 and also by CD95, to which it binds directly via its death domain. [6][7][8] The DED of FADD allows it to bind to DED in the pro-domain of caspase 8.Through these interactions, ligation of TNFR1 or CD95 can result in the formation of a death-inducing signalling complex, which leads to activation of caspase 8, a cell death effector protease. Once ac...

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Section: Jnk Activationmentioning

confidence: 99%

Signalling by CD95 and TNF receptors: Not only life and death

Magnusson

Vaux

1999

Immunol Cell Biol

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“…9 There are two distinct type cell-surface TNF receptors (TNFRs), designated p55 and p75. 10,11 Soluble, truncated versions of membrane TNFRs (sTNFR), consisting of only the extracellular, ligand-binding domain, are present in body fluids and are thought to be involved in regulating TNF activity. 12,13 Recombinant sTNFR:Fc fusion proteins, which are engineered sTNFRs linked to the Fc portion of immunoglobulin G1(IgG1), have been developed for therapeutic neutralization of TNF.…”

Section: Introductionmentioning

confidence: 99%

Electro-gene therapy of collagen-induced arthritis by using an expression plasmid for the soluble p75 tumor necrosis factor receptor-Fc fusion protein

Hahn

et al. 2003

Gene Ther

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“…Identities between E1 and these human proteins are 30% for ankyrin 1 [11], 22% for Fas/APO1 [14], 39% for Mortl/FADD [15,16], 24% for p55 TNF-R [17,18] and 29% for NGF-R [19]. The identity to Mortl/FADD [15,16] is also the highest among two members of the DD protein family [3], whereby the O. volvulus ankyrin sequence is more identical to the DD of the human Mortl/FADD than to the DD of human ankyrins.…”

Section: A049 P E E H R H S Q H E D H E a S G A E Q H S G Q D S G T Tmentioning

confidence: 99%

The putatively protective Onchocerca volvulus neuronal protein E1 is a member of the death domain protein family

1996

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Here we show that El, an ankyrin-related, potentially protective, neuronal protein of the human filarial nematode Onchocerca volvulus contains a death domain (DD), most similar to that of human MUrtl/FADD (39% identity). In addition, sequence comparison of E1 to its homologue from Litomosoides sigmodontis and to Caenorhabditis elegans ankyrin defines two further putative functional domains. One represents the end of the spectrin-binding domain of ankyrins, the other an unique domain, most highly conserved between these nematodes, containing a calpain sequence motif. Thus, E1 may be involved in apoptosis, raising the possibility that protection against this parasitic helminth may be induced by apoptotic processes.

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Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor

Cited by 859 publications

References 39 publications

Signalling by CD95 and TNF receptors: Not only life and death

Signalling by CD95 and TNF receptors: Not only life and death

Electro-gene therapy of collagen-induced arthritis by using an expression plasmid for the soluble p75 tumor necrosis factor receptor-Fc fusion protein

The putatively protective Onchocerca volvulus neuronal protein E1 is a member of the death domain protein family

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