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LINK . SPRINGER . COM {}

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  2. Matching Content Categories
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We are analyzing https://link.springer.com/article/10.1007/s10495-006-0491-0.

Title:
Combretastatin CA-4 and combretastatin derivative induce mitotic catastrophe dependent on spindle checkpoint and caspase-3 activation in non-small cell lung cancer cells | Apoptosis
Description:
Combretastatin A-4 (CA-4), a natural stilbenoid isolated from Combretum caffrum, is a new vascular targeting agent (VTA) known for its antitumor activity due to its anti-tubulin properties. We investigated the molecular mechanisms leading to cell death in non-small cell lung cancer H460 cells induced by natural (CA-4) and synthetic stilbenoids (ST2151) structurally related to CA-4. We found that both compounds induced depolymerization and rearrangement of spindle microtubules, as well as an increasingly aberrant organization of metaphase chromosomes in a dose- and time-dependent manner. Prolonged exposition to ST2151 led cells to organize multiple sites of tubulin repolymerization, whereas tubulin repolymerization was observed only after CA-4 washout. H460 cells were arrested at a pro-metaphase stage, with condensed chromosomes and a triggered spindle assembly checkpoint, as evaluated by kinetochore localization of Bub1 and Mad1 antibodies. Persistent checkpoint activation led to mitochondrial membrane permeabilization (MMP) alterations, cytochrome c release, activation of caspase-9 and -3, PARP cleavage and DNA fragmentation. On the other hand, caspase-2, and -8 were not activated by the drug treatment. The ability of cells to reassemble tubulin in the presence of an activated checkpoint may be responsible for ST2151-induced multinucleation, a recognized sign of mitotic catastrophe. In conclusion, we believe that discovery of new agents able to trigger mitotic catastrophe cell death as a result of mitotic block and prolonged spindle checkpoint activation is particularly worthwhile, considering that tumor cells have a high proliferative rate and mitotic failure occurs irrespective of p53 status.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 7,734,772 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We don’t know how the website earns money.

While many websites aim to make money, others are created to share knowledge or showcase creativity. People build websites for various reasons. This could be one of them. Link.springer.com could be secretly minting cash, but we can't detect the process.

Keywords {🔍}

pubmed, google, scholar, article, cas, cell, mitotic, apoptosis, cancer, cells, death, checkpoint, spindle, catastrophe, caspase, res, activation, combretastatin, agents, oncogene, lung, access, biol, nonsmall, induced, privacy, cookies, content, vitale, antoccia, mitochondrial, clin, information, publish, search, arancia, tanzarella, membrane, cleavage, dna, fragmentation, open, induces, independent, nat, rev, mol, nature, hela, broker,

Topics {✒️}

month download article/chapter diazepam-induced mitotic failure inhibits p-glycoprotein action p53-dependent postmitotic checkpoint microtubule-targeted anticancer agents mitotic spindle damage caspase-independent cell death multidrug-resistance tumor cells spindle assembly checkpoint mitotic catastrophe induced trigger dna fragmentation full article pdf cell death independent st2151 led cells vascular targeting agent dna-damaging agents mitotic catastrophe constitutes human lung cancers article apoptosis aims related subjects cancer cell death abnormal mitotic exit st2151-induced multinucleation privacy choices/manage cookies stefania meschini apoptotic cell death apoptotic cell death death receptor-independent anti-tubulin properties spindle checkpoint signaling spindle damage time-dependent manner mitotic block induced dynamic signalling combretastatin analogues endowed normal mitotic timing hela s3 cells broker le microtubule stabilizing agents microtubule-interfering agents anti-microtubule agents bjab cells proceeds spindle checkpoint function compounds induced depolymerization caspase-independent routes article vitale h460 cells polyploid cell formation apoptotic pathways plays mitochondrial membrane permeabilization

Questions {❓}

  • Roninson IB, Broude EV, Chang BD (2001) If not apoptosis, then what?
  • Zamzami N, Kroemer G (2003) Apoptosis: mitochondrial membrane permeabilization—the (w)hole story?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Combretastatin CA-4 and combretastatin derivative induce mitotic catastrophe dependent on spindle checkpoint and caspase-3 activation in non-small cell lung cancer cells
         description:Combretastatin A-4 (CA-4), a natural stilbenoid isolated from Combretum caffrum, is a new vascular targeting agent (VTA) known for its antitumor activity due to its anti-tubulin properties. We investigated the molecular mechanisms leading to cell death in non-small cell lung cancer H460 cells induced by natural (CA-4) and synthetic stilbenoids (ST2151) structurally related to CA-4. We found that both compounds induced depolymerization and rearrangement of spindle microtubules, as well as an increasingly aberrant organization of metaphase chromosomes in a dose- and time-dependent manner. Prolonged exposition to ST2151 led cells to organize multiple sites of tubulin repolymerization, whereas tubulin repolymerization was observed only after CA-4 washout. H460 cells were arrested at a pro-metaphase stage, with condensed chromosomes and a triggered spindle assembly checkpoint, as evaluated by kinetochore localization of Bub1 and Mad1 antibodies. Persistent checkpoint activation led to mitochondrial membrane permeabilization (MMP) alterations, cytochrome c release, activation of caspase-9 and -3, PARP cleavage and DNA fragmentation. On the other hand, caspase-2, and -8 were not activated by the drug treatment. The ability of cells to reassemble tubulin in the presence of an activated checkpoint may be responsible for ST2151-induced multinucleation, a recognized sign of mitotic catastrophe. In conclusion, we believe that discovery of new agents able to trigger mitotic catastrophe cell death as a result of mitotic block and prolonged spindle checkpoint activation is particularly worthwhile, considering that tumor cells have a high proliferative rate and mitotic failure occurs irrespective of p53 status.
         datePublished:2006-11-21T00:00:00Z
         dateModified:2006-11-21T00:00:00Z
         pageStart:155
         pageEnd:166
         sameAs:https://doi.org/10.1007/s10495-006-0491-0
         keywords:
            CA-4
            ST2151
            Spindle assembly checkpoint
            Mitotic catastrophe
            Caspase-3
            Cancer Research
            Cell Biology
            Oncology
            Biochemistry
            general
            Virology
         image:
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            name:Apoptosis
            issn:
               1573-675X
            volumeNumber:12
            type:
               Periodical
               PublicationVolume
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            name:Kluwer Academic Publishers
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                        type:PostalAddress
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                     address:
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ScholarlyArticle:
      headline:Combretastatin CA-4 and combretastatin derivative induce mitotic catastrophe dependent on spindle checkpoint and caspase-3 activation in non-small cell lung cancer cells
      description:Combretastatin A-4 (CA-4), a natural stilbenoid isolated from Combretum caffrum, is a new vascular targeting agent (VTA) known for its antitumor activity due to its anti-tubulin properties. We investigated the molecular mechanisms leading to cell death in non-small cell lung cancer H460 cells induced by natural (CA-4) and synthetic stilbenoids (ST2151) structurally related to CA-4. We found that both compounds induced depolymerization and rearrangement of spindle microtubules, as well as an increasingly aberrant organization of metaphase chromosomes in a dose- and time-dependent manner. Prolonged exposition to ST2151 led cells to organize multiple sites of tubulin repolymerization, whereas tubulin repolymerization was observed only after CA-4 washout. H460 cells were arrested at a pro-metaphase stage, with condensed chromosomes and a triggered spindle assembly checkpoint, as evaluated by kinetochore localization of Bub1 and Mad1 antibodies. Persistent checkpoint activation led to mitochondrial membrane permeabilization (MMP) alterations, cytochrome c release, activation of caspase-9 and -3, PARP cleavage and DNA fragmentation. On the other hand, caspase-2, and -8 were not activated by the drug treatment. The ability of cells to reassemble tubulin in the presence of an activated checkpoint may be responsible for ST2151-induced multinucleation, a recognized sign of mitotic catastrophe. In conclusion, we believe that discovery of new agents able to trigger mitotic catastrophe cell death as a result of mitotic block and prolonged spindle checkpoint activation is particularly worthwhile, considering that tumor cells have a high proliferative rate and mitotic failure occurs irrespective of p53 status.
      datePublished:2006-11-21T00:00:00Z
      dateModified:2006-11-21T00:00:00Z
      pageStart:155
      pageEnd:166
      sameAs:https://doi.org/10.1007/s10495-006-0491-0
      keywords:
         CA-4
         ST2151
         Spindle assembly checkpoint
         Mitotic catastrophe
         Caspase-3
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
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         name:Apoptosis
         issn:
            1573-675X
         volumeNumber:12
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Kluwer Academic Publishers
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
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      author:
            name:Ilio Vitale
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                  name:University “Roma Tre”
                  address:
                     name:Department of Biology, University “Roma Tre”, Rome, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Antonio Antoccia
            affiliation:
                  name:University “Roma Tre”
                  address:
                     name:Department of Biology, University “Roma Tre”, Rome, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Chiara Cenciarelli
            affiliation:
                  name:University “Roma Tre”
                  address:
                     name:Department of Biology, University “Roma Tre”, Rome, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Pasqualina Crateri
            affiliation:
                  name:Istituto Superiore di Sanità
                  address:
                     name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Stefania Meschini
            affiliation:
                  name:Istituto Superiore di Sanità
                  address:
                     name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
                     type:PostalAddress
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                     name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
                     type:PostalAddress
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            name:Claudio Pisano
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                     name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A., Pomezia, Italy
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                  name:University “Roma Tre”
                  address:
                     name:Department of Biology, University “Roma Tre”, Rome, Italy
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      name:University “Roma Tre”
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      address:
         name:Department of Biology, University “Roma Tre”, Rome, Italy
         type:PostalAddress
      name:University “Roma Tre”
      address:
         name:Department of Biology, University “Roma Tre”, Rome, Italy
         type:PostalAddress
      name:Istituto Superiore di Sanità
      address:
         name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
         type:PostalAddress
      name:Istituto Superiore di Sanità
      address:
         name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
         type:PostalAddress
      name:Istituto Superiore di Sanità
      address:
         name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
         type:PostalAddress
      name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A.
      address:
         name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A., Pomezia, Italy
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      address:
         name:Department of Biology, University “Roma Tre”, Rome, Italy
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               name:Department of Biology, University “Roma Tre”, Rome, Italy
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      name:Antonio Antoccia
      affiliation:
            name:University “Roma Tre”
            address:
               name:Department of Biology, University “Roma Tre”, Rome, Italy
               type:PostalAddress
            type:Organization
      name:Chiara Cenciarelli
      affiliation:
            name:University “Roma Tre”
            address:
               name:Department of Biology, University “Roma Tre”, Rome, Italy
               type:PostalAddress
            type:Organization
      name:Pasqualina Crateri
      affiliation:
            name:Istituto Superiore di Sanità
            address:
               name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
               type:PostalAddress
            type:Organization
      name:Stefania Meschini
      affiliation:
            name:Istituto Superiore di Sanità
            address:
               name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
               type:PostalAddress
            type:Organization
      name:Giuseppe Arancia
      affiliation:
            name:Istituto Superiore di Sanità
            address:
               name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
               type:PostalAddress
            type:Organization
      name:Claudio Pisano
      affiliation:
            name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A.
            address:
               name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A., Pomezia, Italy
               type:PostalAddress
            type:Organization
      name:Caterina Tanzarella
      affiliation:
            name:University “Roma Tre”
            address:
               name:Department of Biology, University “Roma Tre”, Rome, Italy
               type:PostalAddress
            type:Organization
      email:[email protected]
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      name:Department of Biology, University “Roma Tre”, Rome, Italy
      name:Department of Biology, University “Roma Tre”, Rome, Italy
      name:Department of Biology, University “Roma Tre”, Rome, Italy
      name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
      name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
      name:Department of Technology and Health, Istituto Superiore di Sanità, Rome, Italy
      name:SIGMA-TAU Industrie Farmaceutiche Riunite S.p.A., Pomezia, Italy
      name:Department of Biology, University “Roma Tre”, Rome, Italy
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External Links {🔗}(153)

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