Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Morishima, Nobuhiro

doi:10.1046/j.1365-2443.1999.00270.x

Cited by 102 publications

(85 citation statements)

References 55 publications

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“…Y. Eguchi and Y. Tsujimoto (Osaka University, Osaka, Japan). Apoptosis induction was performed as described previously (9). Briefly, cells (5 ϫ 10 5 cells/ml) were treated with 200 ng/ml anti-Fas monoclonal antibody (clone CH-11, Medical and Biological Laboratories, Nagoya, Japan) and 20 g/ml cycloheximide (Calbiochem) or 1 M staurosporine (Calbiochem).…”

Section: Methodsmentioning

confidence: 99%

“…Several lines of evidence, including the order of the multiple cleavages on the vimentin polypeptide, indicate that the initial cut is made at Asp 259 by an initiator caspase, probably either caspase-8 or caspase-9. The Asp 259 cleavage occurs in the absence of the activities of effector caspases (9). The sequence around the cleavage site (Ile-Asp-Val-Asp 259 -Val) matches the sequence preferences of both caspases-8 and -9 in having an aliphatic amino acid residue at the P4 position (10).…”

mentioning

confidence: 87%

“…We have recently found that one of the major components of intermediate filaments, vimentin, can be a substrate for an initiator caspase (9). Vimentin is cleaved at the Asp 85 , Asp 259 , and Asp 429 residues by caspases during apoptosis of human T cells (9).…”

mentioning

confidence: 99%

“…Vimentin is cleaved at the Asp 85 , Asp 259 , and Asp 429 residues by caspases during apoptosis of human T cells (9). Several lines of evidence, including the order of the multiple cleavages on the vimentin polypeptide, indicate that the initial cut is made at Asp 259 by an initiator caspase, probably either caspase-8 or caspase-9.…”

mentioning

confidence: 99%

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Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development

Nakanishi¹,

Maruyama²,

Shibata³

et al. 2001

Journal of Biological Chemistry

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The caspase family of proteases represents the main machinery by which apoptosis occurs. In vitro studies have revealed that upstream caspases are activated in response to apoptotic stimuli, and the active caspases in turn process downstream effector caspases that are involved in the destruction of cellular structure. Caspase-9 is an upstream caspase that can become active in response to cellular damage, including deprivation of growth factors and exposure to oxidative stress in vitro. Little is known, however, about how activation of caspase-9 is temporally and spatially regulated in vivo, e.g. during development. We have identified vimentin as the first example of a caspase-9 substrate that is not a downstream procaspase. Immunohistochemical analysis, using a specific antibody against the vimentin fragments generated by caspase-9, showed that caspase-9 cleaves vimentin in apoptotic cells in the embryonic nervous system and the interdigital regions. This result is consistent with observations that gene knockouts of caspase-9 and its activator, Apaf-1, result in developmental defects in these tissues. Our results show that the specific antibody is useful for in situ detection of caspase-9 activation in programmed cell death.

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Section: Methodsmentioning

confidence: 99%

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confidence: 87%

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confidence: 99%

mentioning

confidence: 99%

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Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development

Nakanishi¹,

Maruyama²,

Shibata³

et al. 2001

Journal of Biological Chemistry

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“…In support of this, we found that a majority of the reactive astrocytes expressing vimentin also were positive for cleaved caspase-3. Vimentin is specifically cleaved by caspase-3, irreversibly dismantling intermediate filaments (Byun et al, 2001), which may impact the integrity and dynamics of intracellular structures (Morishima, 1999). Similarly, the GFAP sequence contains a single caspase consensus sequence, DLTD 266 , based on the general tetrapeptide motif DXXD recognized by caspases, and the antibody CCP-GFAP used in this study was synthesized to the downstream neoepitope that would be generated after caspase cleavage of full length GFAP (Mouser et al, 2006).…”

Section: Presence Of Caspase-cleaved Gfapmentioning

confidence: 99%

Caspase‐3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation

Acarín¹,

Villapol²,

Faiz³

et al. 2007

Glia

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Caspase-3 has classically been defined as the main executioner of programmed cell death. However, recent data supports the participation of this protease in non-apoptotic cellular events including cell proliferation, cell cycle regulation, and cellular differentiation. In this study, astroglial cleavage of caspase-3 was analyzed following excitotoxic damage in postnatal rats to determine if its presence is associated with apoptotic cell death, cell proliferation, or cytoskeletal remodeling. A well-characterized in vivo model of excitotoxicity was studied, where damage was induced by intracortical injection of N-methyl-D-asparate (NMDA) in postnatal day 9 rats. Our results demonstrate that cleaved caspase-3 was mainly observed in the nucleus of activated astrocytes in the lesioned hemisphere as early as 4 h postlesion and persisted until the glial scar was formed at 7-14 days, and it was not associated with TUNEL labeling. Caspase-3 enzymatic activity was detected at 10 h and 1 day postlesion in astrocytes, and co-localized with caspasecleaved fragments of glial fibrillary acidic protein (CCP-GFAP). However, at longer survival times, when astroglial hypertrophy was observed, astroglial caspase-3 did not generally correlate with GFAP cleavage, but instead was associated with de novo expression of vimentin. Moreover, astroglial caspase-3 cleavage was not associated with BrdU incorporation. These results provide further evidence for a nontraditional role of caspases in cellular function that is independent of cell death and suggest that caspase activation is important for astroglial cytoskeleton remodeling following cellular injury. V V C 2007 Wiley-Liss, Inc.

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The Aberrant Expressions of Nuclear Matrix Proteins During the Apoptosis of Human Osteosarcoma Cells

Zhao

Zheng

et al. 2010

The Anatomical Record

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The objective of this study was to investigate altered expressions of nuclear matrix proteins (NMPs) of human osteosarcoma (OS) MG-63 cells during curcumin-induced apoptosis of human OS MG-63 cells. MG-63 cells were cultured with curcumin (7.5 mg/L) for 72 hr. Morphological alterations of cells were captured using light microscopy and transmission electron microscopy, and cell cycle distribution was estimated by flow cytometry. NMPs were selectively extracted and subjected to two-dimensional gel electrophoresis (2-DE) analysis. Western blots were performed to determine changes in the expression levels of specific NMPs. The results demonstrated that typical characteristics of apoptosis were observed. Cellular chromatin agglutinated, cell nuclei condensed, and apoptotic bodies were formed after treatment with curcumin. The 2-DE results displayed 27 NMPs, 21 of which were identified to have change in expression levels significantly during apoptosis. The altered expressions of three of these NMPs (nucleophosmin, prohibitin, and vimentin) were further confirmed by immunoblotting. These findings indicated that the apoptosis of MG-63 cells was accompanied by the expression alteration of NMPs. Our results might help to reveal the relationship between NMPs and the regulation of gene expression in the process of apoptosis, as well as provide the basic concepts for future studies on the mechanisms of apoptosis and the therapy for bone diseases. Anat Rec,

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Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl‐2 action

Cited by 102 publications

References 55 publications

Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development

Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development

Caspase‐3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation

The Aberrant Expressions of Nuclear Matrix Proteins During the Apoptosis of Human Osteosarcoma Cells

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