Intermediate filament proteins during carcinogenesis and apoptosis (Review).

Prasad, Sarada C.; Soldatenkov, Viatcheslav A.; Srinivasarao, Geetha Y.; Dritschilo, Anatoly

doi:10.3892/ijo.14.3.563

Cited by 37 publications

(37 citation statements)

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“…Lamins are well-known caspase substrates (Croft et al 2005), and it is possible that the lamin alterations observed in this study are a reflection of apoptosis (Lieberman and Fan 2003;Prasad et al 1999). von Harsdorf et al (1999 detected lamin degradation induced by oxidative stress in isolated cardiac cells, suggesting a link between Dox-induced oxidative stress and degradation of the nuclear lamins.…”

Section: Discussionmentioning

confidence: 99%

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

et al. 2008

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Doxorubicin (Dox) is a very potent antineoplastic agent used against several types of cancer, despite a cumulative cardiomyopathy that reduces the therapeutic index for treatment. H9c2 myoblast cells have been used as an in vitro model to study biochemical alterations induced by Dox treatment on cardiomyocyte cells. Despite the extensive work already published, few data are available regarding morphological alterations of H9c2 cells during Dox treatment. The purpose of the present work was to evaluate Doxinduced morphological alterations in H9c2 myoblasts, focusing especially on the nuclei, mitochondria, and structural fibrous proteins. Treatment of H9c2 cell with low concentrations of Dox causes alterations in fibrous structural proteins including the nuclear lamina and sarcomeric cardiac myosin, as well as mitochondrial depolarization and fragmentation, membrane blebbing with cell shape changes, and phosphatidylserine externalization. For higher Dox concentrations, more profound alterations are evident, including nuclear swelling with disruption of nuclear membrane structure, mitochondrial swelling, and extensive cytoplasm vacuolization. The results obtained indicate that Dox causes morphological alterations in mitochondrial, nuclear, and fibrous protein structures in H9c2 cells, which are dependent on the drug concentration. Data obtained with the present study allow for a better characterization of the effects of Dox on H9c2 myoblasts, used as a model to study Dox-induced cardiotoxicity. The results obtained also provide new and previously unknown targets that can contribute to understand the mechanisms involved in the cardiotoxicity of Dox.

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Section: Discussionmentioning

confidence: 99%

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

et al. 2008

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“…The VEMD caspase recognition sequence in the linker L1-2 region is also found in keratins 13, 14 and 16, however, their cleavage during apoptosis could not be experimentally determined until now. 22 The caspase cleavage motifs VEMD (K13, K14, K15, K16, K17), VEVD (K18, K19, lamin B1, and lamin B2) and VEID (lamins A and C) are well conserved in the L1-2 subdomain of types I and V intermediate filaments implying that this is an important structural feature. Type II keratins (K1 ± 8) do not contain a similar sequence motif, and they do not seem to be cleaved during apoptosis.…”

Section: Cell Death and Differentiationmentioning

confidence: 99%

Apoptosis-induced cleavage of keratin 15 and keratin 17 in a human breast epithelial cell line

Badock

Steinhusen²,

Bommert³

et al. 2001

Cell Death Differ

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Keratin 15 (K15) and keratin 17 (K17) are intermediate filament (IF) type I proteins that are responsible for the mechanical integrity of epithelial cells. By analyzing the human breast epithelial cell line H184A1 before and after induction of apoptosis by high-resolution two-dimensional gel electrophoresis (2-DE) we identified the caspase-mediated cleavage of keratins 15 and 17. After induction of apoptosis three fragments of both K15 and K17 could be observed by 2 -DE. K15 and K17 proteolysis was observed during staurosporineinduced apoptosis and anoikis (anchorage-dependent apoptosis) as well and was shown to be caspase-dependent. By using mass spectrometry we could determine the caspase cleavage sites, one in K15 and two in K17. The sequence VEMD/A at the cleavage site located in the conserved linker region was found in K15 and K17. A further cleavage site was identified in the tail region of K17 with the recognition motif EVQD/G. Cell Death and Differentiation (2001) 8, 308 ± 315.

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“…IF proteins represent one of the most important type of substrates for caspase activity (Prasad et al, 1999). They are thin filaments (actin) and microtubules that frequently work together to enhance both structural integrity, cell shape, and cell and organelle motility.…”

Section: Third Stage: Protein Crosslinking and Apoptotic Body Formationmentioning

confidence: 99%

Role of caspases in the regulation of apoptotic pancreatic islet beta‐cells death

Hui

Dotta

Mario

et al. 2004

Journal Cellular Physiology

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The homeostatic control of beta-cell mass in normal and pathological conditions is based on the balance of proliferation, differentiation, and death of the insulinsecreting cells. A considerable body of evidence, accumulated during the last decade, has emphasized the significance of the disregulation of the mechnanisms regulating the apoptosis of beta-cells in the sequence of events that lead to the development of diabetes. The identification of agents capable of interfering with this process needs to be based on a better understanding of the beta-cell specific pathways that are activated during apoptosis. The aim of this article is fivefold: (1) a review of the evidence for beta-cell apoptosis in Type I diabetes, Type II diabetes, and islet transplantation, (2) to review the common stimuli and their mechanisms in pancreatic beta-cell apoptosis, (3) to review the role of caspases and their activation pathway in beta-cell apoptosis, (4) to review the caspase cascade and morphological cellular changes in apoptotic beta-cells, and (5) to highlight the putative strategies for preventing pancreatic beta-cells from apoptosis.

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Intermediate filament proteins during carcinogenesis and apoptosis (Review).

Cited by 37 publications

References 0 publications

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

Apoptosis-induced cleavage of keratin 15 and keratin 17 in a human breast epithelial cell line

Role of caspases in the regulation of apoptotic pancreatic islet beta‐cells death

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