Possible involvement of caspase‐7 in cell cycle progression at mitosis

Hashimoto, Toshiaki; Yamauchi, Lisa; Hunter, Tony; Kikkawa, Ushio; Kamada, Shinji

doi:10.1111/j.1365-2443.2008.01192.x

Cited by 28 publications

(30 citation statements)

References 39 publications

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“…Caspases have been implicated in mitotic progression (18), and, in particular, BubR1 is reportedly degraded by the effector caspase-3 during exit from mitosis (17), although we did not observe this effect in T98G cells ( Supplementary Fig. S2).…”

Section: Su6656 and Geraldol Do Not Induce The Degradation Of Cyclin contrasting

confidence: 43%

“…Caspase-3 is upregulated during mitosis (18) and has been shown to increase the formation of micronuclei in response to antimitotic agents (48), but a role for caspase-3 in mitosis remains undefined. This study reveals a novel role for caspase-3: mitotic slippage induced by SU6656 and geraldol is caspase-3 dependent.…”

Section: Discussionmentioning

confidence: 99%

“…Caspases have well-characterized apoptotic functions, but caspase-3 and caspase-7 have both recently been observed to play a role, yet to be defined, in mitotic progression (17,18). Their activities are tightly regulated and must be restrained during mitotic stress to prevent extensive cell death, most notably through survivin, which inhibits caspase activation during mitotic arrest and functions as part of the mitotic checkpoint machinery (19).…”

Section: Introductionmentioning

confidence: 99%

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Caspase-3–Dependent Mitotic Checkpoint Inactivation by the Small-Molecule Inducers of Mitotic Slippage SU6656 and Geraldol

Riffell

Jänicke²,

Roberge³

2011

Molecular Cancer Therapeutics

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Microtubule-targeting cancer drugs such as paclitaxel block cell-cycle progression at mitosis by prolonged activation of the mitotic checkpoint. Cells can spontaneously escape mitotic arrest and enter interphase without chromosome segregation by a process termed mitotic slippage that involves the degradation of cyclin B1 without mitotic checkpoint inactivation. Inducing mitotic slippage with chemicals causes cells to die after multiple rounds of DNA replication without cell division, which may enhance the antitumor activity of microtubule-targeting drugs. Here, we explore pathways leading to mitotic slippage by using SU6656 and geraldol, two recently identified chemical inducers of mitotic slippage. Mitotic slippage induced by SU6656 or geraldol was blocked by the proteasome inhibitor MG-132 and involved proteasome-dependent degradation of cyclin B1 and the mitotic checkpoint proteins budding uninhibited by benzimidazole related 1 (BubR1) and cell division cycle 20 (Cdc20) in T98G cells. Mitotic slippage and the degradation of BubR1 and Cdc20 were also inhibited by the caspase-3 and -7 inhibitor DEVD-CHO.

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Section: Su6656 and Geraldol Do Not Induce The Degradation Of Cyclin contrasting

confidence: 43%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Caspase-3–Dependent Mitotic Checkpoint Inactivation by the Small-Molecule Inducers of Mitotic Slippage SU6656 and Geraldol

Riffell

Jänicke²,

Roberge³

2011

Molecular Cancer Therapeutics

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“…Caspase-1 is responsible for both the inflammatory and innate immune responses (Nadiri et al 2006), Caspase-7 knockdown specifically inhibits cell cycle progression during apoptosis (Hashimoto et al 2008). Caspase-8 can regulate lymphocyte proliferation (Salmena et al 2003).…”

Section: Discussionmentioning

confidence: 99%

Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

Tapadia

Gautam

2011

J Biosci

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Drosophila metamorphosis is characterized by the histolysis of larval structures by programmed cell death, which paves the way for the establishment of adult-specific structures under the influence of the steroid hormone ecdysone. Malpighian tubules function as an excretory system and are one of the larval structures that are not destroyed during metamorphosis and are carried over to adulthood. The pupal Malpighian tubules evade destruction in spite of expressing apoptotic proteins, Reaper, Hid, Grim, Dronc and Drice. Here we show that in the Malpighian tubules expression of apoptotic proteins commences right from embryonic development and continues throughout the larval stages. Overexpression of these proteins in the Malpighian tubules causes larval lethality resulting in malformed tubules. The number and regular organization of principal and stellate cells of Malpighian tubules is disturbed, in turn disrupting the physiological functioning of the tubules as well. Strikingly, the localization of beta-tubulin, F-actin and Disclarge (Dlg) is also disrupted. These results suggest that the apoptotic proteins could be having non-apoptotic function in the development of Malpighian tubules.

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“…Treatment of HeLa cells with a caspase inhibitor, however, did not interfere with proliferation but rather with the mitotic check-point control [169]. Recently, also caspases-7 and -8 were shown to be periodically activated during mitosis of cultured tumor cell lines, and specific interference with caspase-7 expression led to mitotic arrest, raising the possibility that caspase-7 might be crucial for the proliferation of tumor cells in vivo [170]. In transgenic mice, loss of caspase-3 abrogated the c-myc-induced hyper-proliferation of pancreatic beta cells, suggesting that caspase-3 activity might be important in the cell cycle of tumor cells [64].…”

Section: Non-apoptotic Functions Of Caspases Possibly Involved In mentioning

confidence: 99%

The Enigmatic Roles of Caspases in Tumor Development

Jäger

Zwacka

2010

Cancers

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One function ascribed to apoptosis is the suicidal destruction of potentially harmful cells, such as cancerous cells. Hence, their growth depends on evasion of apoptosis, which is considered as one of the hallmarks of cancer. Apoptosis is ultimately carried out by the sequential activation of initiator and executioner caspases, which constitute a family of intracellular proteases involved in dismantling the cell in an ordered fashion. In cancer, therefore, one would anticipate caspases to be frequently rendered inactive, either by gene silencing or by somatic mutations. From clinical data, however, there is little evidence that caspase genes are impaired in cancer. Executioner caspases have only rarely been found mutated or silenced, and also initiator caspases are only affected in particular types of cancer. There is experimental evidence from transgenic mice that certain initiator caspases, such as caspase-8 and -2, might act as tumor suppressors. Loss of the initiator caspase of the intrinsic apoptotic pathway, caspase-9, however, did not promote cellular transformation. These data seem to question a general tumor-suppressive role of caspases. We discuss several possible ways how tumor cells might evade the need for alterations of caspase genes. First, alternative splicing in tumor cells might generate caspase variants that counteract apoptosis. Second, in tumor cells caspases might be kept in check by cellular caspase inhibitors such as c-FLIP or XIAP. Third, pathways upstream of caspase activation might be disrupted in tumor cells. Finally, caspase-independent cell death mechanisms might abrogate the selection pressure for caspase inactivation during tumor development. These scenarios, however, are hardly compatible with the considerable frequency of spontaneous apoptosis occurring in several cancer types. Therefore, alternative concepts might come into play, such as compensatory proliferation. Herein, apoptosis and/or non-apoptotic functions of caspases may even promote tumor development. Moreover, experimental evidence suggests that caspases might play non-apoptotic roles in processes that are crucial for tumorigenesis, such as cell proliferation, migration, or invasion. We thus propose a model wherein caspases are preserved in tumor cells due to their functional contributions to development and progression of tumors.

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Possible involvement of caspase‐7 in cell cycle progression at mitosis

Cited by 28 publications

References 39 publications

Caspase-3–Dependent Mitotic Checkpoint Inactivation by the Small-Molecule Inducers of Mitotic Slippage SU6656 and Geraldol

Caspase-3–Dependent Mitotic Checkpoint Inactivation by the Small-Molecule Inducers of Mitotic Slippage SU6656 and Geraldol

Non-apoptotic function of apoptotic proteins in the development of Malpighian tubules of Drosophila melanogaster

The Enigmatic Roles of Caspases in Tumor Development

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