Binding, Internalization, and Intracellular Processing of Proteins Interacting with Recycling Receptors

Bajzer, Željko; Myers, Alyssa; Vuk-Pavlović, S.

doi:10.1016/s0021-9258(18)80042-4

Cited by 41 publications

(5 citation statements)

References 24 publications

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“…It is not clear which regions on the T N F molecule and their corresponding cell surface receptor(s) inter act. However, binding of T N F with its specific cell surface receptor is the necessary first step in inducing subsequent effects (Bajzer et al 1989;W atanabe et al 1989). T he ultrastructure of T N F has been elucidated down to 2.6 Af (Eck & Sprang 1989).…”

Section: Discussionmentioning

confidence: 99%

“…T N F causes haem orrhagic necrosis of certain transplantable tum ours in mice (Carswell et al 1975) and is also involved in a spectrum of im portant immunological and inflam m atory reactions (Goeddel et al 1986;Beutler & Cerami 1988). Although the m olecular mechanisms whereby T N F induces these diverse responses is still unknown, it is necessary that T N F first bind to specific cell m em brane receptors (Bajzer et al 1989;W atanabe et al 1989).…”

Section: Introductionmentioning

confidence: 99%

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A 20 amino acid synthetic peptide of a region from the 55 kDa human TNF receptor inhibits cytolytic and binding activities of recombinant human tumour necrosis factorin vitro

Hwang

Gatanaga

Innins

et al. 1991

Proc. R. Soc. Lond. B

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Tumour Necrosis Factor (TNF) and Lymphotoxin (LT) can exert a wide range of effects on cells and tissues and they are important effector molecules in cell mediated immunity. All these effects are induced subsequent to the binding of these cytokines to specific membrane receptors. Recently, two of these membrane receptors of 55 and 75 kDa, have been identified which share some amino acid (AA) homology in their N-terminal extracellular domains but differ in their intracellular domains. We synthesized two synthetic 20 AA peptides from hydrophilic regions of the N-terminal extracellular domains of the 55 kDa receptor; peptide A shares homology with both 55 and 75 kDa receptors, peptide B is unique. We found peptide B inhibits both the binding and cytolytic activity of recombinant human TNF when tested on murine L929 cells in vitro. Polyclonal antiserum generated against peptide B will block binding of 125I-labelled TNF to these cells in vitro. However, peptide A and antiserum prepared against peptide A are without effect in these same assay systems. These data suggest that the 20 AA sequences from AA 175 to 194 in the N-terminal extracellular domain of the 55 kDa TNF receptor are expressed on the cell surface and are involved in the binding of TNF.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A 20 amino acid synthetic peptide of a region from the 55 kDa human TNF receptor inhibits cytolytic and binding activities of recombinant human tumour necrosis factorin vitro

Hwang

Gatanaga

Innins

et al. 1991

Proc. R. Soc. Lond. B

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“…Linear detection of ligand over a broad range of concentrations could be facilitated by the following properties reported for other receptors (Fig. 1, B to D, and SOM text): (i) mobilization, defined as ligand-induced additional transport of newly synthesized receptor from intracellular pools to the plasma membrane ( 8); (ii) recycling, consisting of ligand-induced receptor endocytosis and subsequent transport back to the plasma membrane (9); and (iii) turnover, comprising ligand-independent transport of newly synthesized receptor to the plasma membrane and removal from the plasma membrane by ligand- independent receptor endocytosis and subsequent degradation (10). A further potential strategy to cope with particularly high ligand concentrations is expression of large amounts of receptor on the plasma membrane (11).…”

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confidence: 99%

“…Out-group aggression may be driven by the desire to increase the in-group's relative status and power in the intergroup competition (henceforth "out-group hate"). Alternatively, it may be driven by the vigilant desire to defend and protect the ingroup against real or perceived out-group threat (8,9).…”

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confidence: 99%

Covering a Broad Dynamic Range: Information Processing at the Erythropoietin Receptor

Becker

Schilling

Bachmann

et al. 2010

Science

153

185

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Cell surface receptors convert extracellular cues into receptor activation, thereby triggering intracellular signaling networks and controlling cellular decisions. A major unresolved issue is the identification of receptor properties that critically determine processing of ligand-encoded information. We show by mathematical modeling of quantitative data and experimental validation that rapid ligand depletion and replenishment of the cell surface receptor are characteristic features of the erythropoietin (Epo) receptor (EpoR). The amount of Epo-EpoR complexes and EpoR activation integrated over time corresponds linearly to ligand input; this process is carried out over a broad range of ligand concentrations. This relation depends solely on EpoR turnover independent of ligand binding, which suggests an essential role of large intracellular receptor pools. These receptor properties enable the system to cope with basal and acute demand in the hematopoietic system.

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“…Internalized receptors may degrade or recycle to the cell membrane, where they can rebind to sTNF [34]. Ligand-free TNFRs also turn over (internalize) [82,83]. In the extracellular space, intact sTNF may dissociate from the sTNF/TNFR2 complex shed.…”

Section: Single-cell Tnf/tnfr Kinetics and Cellular Organization Within A Simulated Bead Granulomamentioning

confidence: 99%

Mathematical Models of Anti‐TNF Therapies and their Correlation with Tuberculosis

Marino

Fallahi-Sichani

Linderman

et al. 2012

Antibody‐Mediated Drug Delivery Systems

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Binding, Internalization, and Intracellular Processing of Proteins Interacting with Recycling Receptors

Cited by 41 publications

References 24 publications

A 20 amino acid synthetic peptide of a region from the 55 kDa human TNF receptor inhibits cytolytic and binding activities of recombinant human tumour necrosis factorin vitro

A 20 amino acid synthetic peptide of a region from the 55 kDa human TNF receptor inhibits cytolytic and binding activities of recombinant human tumour necrosis factorin vitro

Covering a Broad Dynamic Range: Information Processing at the Erythropoietin Receptor

Mathematical Models of Anti‐TNF Therapies and their Correlation with Tuberculosis

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