The Role of APO‐1‐Mediated Apoptosis in the Immune System

Krammer, Peter H.; Dhein, Jens; Walczak, Henning; Behrmann, Iris; Mariani, Sara M; Matiba, Bernd; Fath, Michael; Daniel, Peter T.; Knipping, Eckart; Westendorp, Michael O.; Stricker, Kirstin; Bäumler, Caroline; Hellbardt, Stefan; Germer, Matthias; Peter, Marcus E.; Debativ, Klaus‐Michael ‐M

doi:10.1111/j.1600-065x.1994.tb00889.x

Cited by 220 publications

(105 citation statements)

References 49 publications

(21 reference statements)

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“…[3][4][5][6] The CD95, a 48 kDa type I transmembrane receptor (CD95) is a member of the tumor necrosis factor/nerve growth factor (TNF/NGF) receptor superfamily of cell surface molecules which includes various molecules involved in immune regulation, such as TNF receptors I and II, CD27, CD30 and CD40. [7][8][9][10][11][12] CD95 crosslinking by agonistic antibodies or the natural ligand activates a signal cascade via FADD/MORT-1 and FLICE/MACH (caspase-8) that directly leads to activation of ICE/Ced-3 proteases (caspases) which function as downstream effectors of cell death.…”

Section: The Cd95 Pathwaymentioning

confidence: 99%

Cytotoxic drugs and the CD95 pathway

1999

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Section: The Cd95 Pathwaymentioning

confidence: 99%

Cytotoxic drugs and the CD95 pathway

1999

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“…lpr and gld mice further show B-cell hyperreactivity associated with the production of autoan-induced hepatitis, graft-versus-host disease and autoimmune diseases, such as diabetes and encephalomyelitis [71Ϫ75]. Allison tibodies, suggesting that CD95 also controls the expansion of the B-cell compartment (reviewed in [37,53]). et al [76] reported that transgenic expression of CD95L in pancreatic islets failed to protect these from allogeneic transplant Just as a defect of the CD95 system is intimately linked to autoimmune diseases caused by the impaired removal of autore-rejection when placed under the kidney capsule.…”

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Apoptosis signaling by death receptors

Schulze‐Osthoff

Ferrari

Łos

et al. 1998

European Journal of Biochemistry

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Death receptors have been recently identified as a subgroup of the TNF-receptor superfamily with a predominant function in induction of apoptosis. The receptors are characterized by an intracellular region, called the death domain, which is required for the transmission of the cytotoxic signal. Currently, five different such death receptors are known including tumor necrosis factor (TNF) receptor-1, CD95 (Fas/ APO-1), TNF-receptor-related apoptosis-mediated protein (TRAMP) and TNF-related apoptosis-inducing ligand (TRAIL) receptor-1 and -2. The signaling pathways by which these receptors induce apoptosis are rather similar. Ligand binding induces receptor oligomerization, followed by the recruitment of an adaptor protein to the death domain through homophilic interaction. The adaptor protein then binds a proximal caspase, thereby connecting receptor signaling to the apoptotic effector machinery. In addition, further pathways have been linked to death receptor-mediated apoptosis, such as sphingomyelinases, JNK kinases and oxidative stress. These pro-apoptotic signals are counteracted by several mechanisms which inhibit apoptosis at different levels. This review summarizes the current and rapidly expanding knowledge about the biological functions of death receptors and the mechanisms to trigger or to counteract cell death.Keywords : apoptosis; Bcl-2; caspase; CD95 (APO-1/Fas) ; death receptor; inhibitor of apoptosis protein; nuclear factor-κB ; tumor-necrosis factor; tumor-necrosis-factor-related apoptosis-inducing ligand; tumornecrosis-factor-receptor-related apoptosis-mediating protein.Apoptosis or programmed cell death is the innate mechanism modelling, immune regulation and tumor regression. Cells undergoing apoptosis show a sequence of cardinal morphological by which the organism eliminates unwanted cells. In contrast to necrosis, apoptosis is the most common physiological form of features including membrane blebbing, cellular shrinkage and condensation of chromatin. Biochemically, these alterations are cell death and occurs during embryonic development, tissue reassociated with the translocation of phosphatidylserine to the duced following traumatic injury or exposure to high concentra-

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“…4 The Fas receptor is a 45-kd cell surface type 1 plasma membrane protein that is expressed in lymphoid and many other tissues. [4][5][6][7] The receptor is activated through oligomerization upon binding of its ligand (FasL) to its extracellular domain, and the apoptotic signal is transduced through the so-called ''death domain.'' Recent work has revealed that the death domain of Fas interacts with the death domain found in other proteins, such as FADD/MORT-1 8,9 and Daxx, 10 which in turn activate caspase-8 (MACH/FLICE/Mch5) and Jun N-terminal kinase, [10][11][12] respectively.…”

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confidence: 99%