ArticleThe American journal of pathology2004
Intermediate filaments control the intracellular distribution of caspases during apoptosis.
Article in The American journal of pathology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 65 citations in OpenAlex.
- F-actin-rich territories coordinate apoptosome assembly and caspase activation during DNA damage-induced intrinsic apoptosis.Molecular biology of the cell · 2023Article
- APEX2-Mediated Proximity Labeling Resolves the DDIT4-Interacting Proteome.International journal of molecular sciences · 2022Article
- Pathophysiological Role of Vimentin Intermediate Filaments in Lung Diseases.Frontiers in cell and developmental biology · 2022Review
- Susceptibility of cytoskeletal-associated proteins for tumor progression.Cellular and molecular life sciences : CMLS · 2021Review
- Site-specific phosphorylation and caspase cleavage of GFAP are new markers of Alexander disease severity.eLife · 2019Article
- Vimentin modulates apoptosis and inflammatory cytokine release by a human monocytic cell line (THP-1) in response to lipopolysaccharides in vitro.Chinese medical journal · 2019Article
- Intermediate filaments and IF-associated proteins: from cell architecture to cell proliferation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Vimentin regulates activation of the NLRP3 inflammasome.Nature communications · 2015Article
- Low-dose etoposide-treatment induces endoreplication and cell death accompanied by cytoskeletal alterations in A549 cells: Does the response involve senescence? The possible role of vimentin.Cancer cell international · 2013Article
- Article
- Withaferin A effectively targets soluble vimentin in the glaucoma filtration surgical model of fibrosis.PloS one · 2013Article
- Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.The Journal of biological chemistry · 2012Article
- Caspase-mediated apoptosis of trophoblasts in term human placental villi is restricted to cytotrophoblasts and absent from the multinucleated syncytiotrophoblast.Reproduction (Cambridge, England) · 2012Article
- Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation.Journal of the American Chemical Society · 2011Article
- Features of senescence and cell death induced by doxorubicin in A549 cells: organization and level of selected cytoskeletal proteins.Journal of cancer research and clinical oncology · 2010Article
- Caspase-6 activation in familial alzheimer disease brains carrying amyloid precursor protein or presenilin i or presenilin II mutations.Journal of neuropathology and experimental neurology · 2009Article
- Introducing intermediate filaments: from discovery to disease.The Journal of clinical investigation · 2009Review
- FLASH is an essential component of Cajal bodies.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Regulatory mechanisms and functions of intermediate filaments: a study using site- and phosphorylation state-specific antibodies.Cancer science · 2006Review
- Biological Entanglement-Like Effect After Communication of Fish Prior to X-Ray Exposure.Dose-response : a publication of International Hormesis SocietyArticle
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caspases are responsible for a cascade of events controlling the disassembly of apoptotic cells. We now demonstrate that caspase-9 is activated at an early stage of apoptosis in epithelial cells and all its detectable, catalytically active large subunits (both the p35 and p37) are concentrated on cytokeratin fibrils. Immunolabeling of distinctive neoepitopes, exposed by cleavage of procaspase-9 at either Asp315 or Asp330, was co-localized on these fibrils with active caspase-3, caspase-cleaved cytokeratin-18, death-effector-domain containing DNA-binding protein and ubiquitin. Cytokeratin filaments may thus provide a scaffold whereby active subunits of caspase-9 can activate caspase-3 which, in turn, can activate more caspase-9 so forming an amplification loop to facilitate cleavage of cytokeratin-18, disruption of the cytoskeleton and the ensuing formation of cytoplasmic inclusions. These inclusions, formed from the collapse of fibrils, together with their associated components, also contain ubiquitinated proteins, vimentin, heat-shock protein 72, and tumor necrosis factor receptor type-1-associated death domain protein. Many of their constituents, including active caspases, remain sequestered within these inclusions, even after detergent treatment and isolation. Thus, such inclusions do not merely accumulate disrupted cytokeratins but also sequestrate potentially noxious proteins that could injure healthy neighboring cells.
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