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  1. Article ; Online: Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex.

    Hillert-Richter, Laura K / Lavrik, Inna N

    Journal of visualized experiments : JoVE

    2021  , Issue 174

    Abstract: Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ... ...

    Abstract Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ligands leads to the assembly of the death-inducing signaling complex (DISC). DISC comprises DR, the adaptor protein Fas-associated protein with death domain (FADD), procaspases-8/-10, and cellular FADD-like interleukin (IL)-1β-converting enzyme-inhibitory proteins (c-FLIPs). The DISC serves as a platform for procaspase-8 processing and activation. The latter occurs via its dimerization/oligomerization in the death effector domain (DED) filaments assembled at the DISC. Activation of procaspase-8 is followed by its processing, which occurs in several steps. In this work, an established experimental workflow is described that allows the measurement of DISC formation and the processing of procaspase-8 in this complex. The workflow is based on immunoprecipitation techniques supported by western blot analysis. This workflow allows careful monitoring of different steps of procaspase-8 recruitment to the DISC and its processing and is highly relevant for investigating molecular mechanisms of extrinsic apoptosis.
    MeSH term(s) Apoptosis ; Caspase 8/metabolism ; Death Domain Receptor Signaling Adaptor Proteins/metabolism ; Signal Transduction ; fas Receptor/metabolism
    Chemical Substances Death Domain Receptor Signaling Adaptor Proteins ; fas Receptor ; Caspase 8 (EC 3.4.22.-)
    Language English
    Publishing date 2021-08-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/62842
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Measuring composition of cd95 death-inducing signaling complex and processing of procaspase-8 in this complex

    Hillert-Richter, Laura K. / Lavrik, Inna N.

    Journal of visualized experiments. 2021 Aug. 02, , no. 174

    2021  

    Abstract: Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ... ...

    Abstract Extrinsic apoptosis is mediated by the activation of death receptors (DRs) such as CD95/Fas/APO-1 or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-receptor 1/receptor 2 (TRAIL-R1/R2). Stimulation of these receptors with their cognate ligands leads to the assembly of the death-inducing signaling complex (DISC). DISC comprises DR, the adaptor protein Fas-associated protein with death domain (FADD), procaspases-8/-10, and cellular FADD-like interleukin (IL)-1β-converting enzyme-inhibitory proteins (c-FLIPs). The DISC serves as a platform for procaspase-8 processing and activation. The latter occurs via its dimerization/oligomerization in the death effector domain (DED) filaments assembled at the DISC. Activation of procaspase-8 is followed by its processing, which occurs in several steps. In this work, an established experimental workflow is described that allows the measurement of DISC formation and the processing of procaspase-8 in this complex. The workflow is based on immunoprecipitation techniques supported by western blot analysis. This workflow allows careful monitoring of different steps of procaspase-8 recruitment to the DISC and its processing and is highly relevant for investigating molecular mechanisms of extrinsic apoptosis.
    Keywords Western blotting ; apoptosis ; death ; dimerization ; interleukins ; ligands ; necrosis ; neoplasms ; oligomerization ; precipitin tests ; protein domains
    Language English
    Dates of publication 2021-0802
    Size p. e62842.
    Publishing place Journal of Visualized Experiments
    Document type Article
    ZDB-ID 2259946-0
    ISSN 1940-087X
    ISSN 1940-087X
    DOI 10.3791/62842
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Pharmacological targeting of c-FLIP

    König, Corinna / Hillert-Richter, Laura K / Ivanisenko, Nikita V / Ivanisenko, Vladimir A / Lavrik, Inna N

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 20823

    Abstract: The development of efficient combinatorial treatments is one of the key tasks in modern anti-cancer therapies. An apoptotic signal can either be induced by activation of death receptors (DR) (extrinsic pathway) or via the mitochondria (intrinsic pathway). ...

    Abstract The development of efficient combinatorial treatments is one of the key tasks in modern anti-cancer therapies. An apoptotic signal can either be induced by activation of death receptors (DR) (extrinsic pathway) or via the mitochondria (intrinsic pathway). Cancer cells are characterized by deregulation of both pathways. Procaspase-8 activation in extrinsic apoptosis is controlled by c-FLIP proteins. We have recently reported the small molecules FLIPinB/FLIPinBγ targeting c-FLIP
    MeSH term(s) Aniline Compounds/pharmacology ; Antineoplastic Combined Chemotherapy Protocols/pharmacology ; Apoptosis/drug effects ; CASP8 and FADD-Like Apoptosis Regulating Protein/antagonists & inhibitors ; Caspase 8/metabolism ; Cell Survival/drug effects ; Death Domain Receptor Signaling Adaptor Proteins/metabolism ; Drug Delivery Systems ; Fas Ligand Protein/pharmacology ; HeLa Cells ; Humans ; Proto-Oncogene Proteins c-bcl-2/antagonists & inhibitors ; Sulfonamides/pharmacology
    Chemical Substances Aniline Compounds ; BCL2 protein, human ; CASP8 and FADD-Like Apoptosis Regulating Protein ; CFLAR protein, human ; Death Domain Receptor Signaling Adaptor Proteins ; Fas Ligand Protein ; Proto-Oncogene Proteins c-bcl-2 ; Sulfonamides ; CASP8 protein, human (EC 3.4.22.-) ; Caspase 8 (EC 3.4.22.-) ; navitoclax (XKJ5VVK2WD)
    Language English
    Publishing date 2020-11-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-76079-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Regulation of extrinsic apoptotic signaling by c-FLIP: towards targeting cancer networks.

    Ivanisenko, Nikita V / Seyrek, Kamil / Hillert-Richter, Laura K / König, Corinna / Espe, Johannes / Bose, Kakoli / Lavrik, Inna N

    Trends in cancer

    2021  Volume 8, Issue 3, Page(s) 190–209

    Abstract: The extrinsic pathway is mediated by death receptors (DRs), including CD95 (APO-1/Fas) or TRAILR-1/2. Defects in apoptosis regulation lead to cancer and other malignancies. The master regulator of the DR networks is the cellular FLICE inhibitory protein ( ...

    Abstract The extrinsic pathway is mediated by death receptors (DRs), including CD95 (APO-1/Fas) or TRAILR-1/2. Defects in apoptosis regulation lead to cancer and other malignancies. The master regulator of the DR networks is the cellular FLICE inhibitory protein (c-FLIP). In addition to its key role in apoptosis, c-FLIP may exert other cellular functions, including control of necroptosis, pyroptosis, nuclear factor κB (NF-κB) activation, and tumorigenesis. To gain further insight into the molecular mechanisms of c-FLIP action in cancer networks, we focus on the structure, isoforms, interactions, and post-translational modifications of c-FLIP. We also discuss various avenues to target c-FLIP in cancer cells for therapeutic benefit.
    MeSH term(s) Apoptosis/physiology ; CASP8 and FADD-Like Apoptosis Regulating Protein/genetics ; CASP8 and FADD-Like Apoptosis Regulating Protein/metabolism ; Humans ; Neoplasms/drug therapy ; Neoplasms/genetics ; Signal Transduction ; fas Receptor/genetics ; fas Receptor/metabolism
    Chemical Substances CASP8 and FADD-Like Apoptosis Regulating Protein ; fas Receptor
    Language English
    Publishing date 2021-12-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2852626-0
    ISSN 2405-8025 ; 2405-8033 ; 2405-8033
    ISSN (online) 2405-8025 ; 2405-8033
    ISSN 2405-8033
    DOI 10.1016/j.trecan.2021.12.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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