Caspase-Mediated Fragmentation of Calpain Inhibitor Protein Calpastatin during Apoptosis

Wang, Kevin; Posmantur, Rand; Nadimpalli, Ravi; Nath, Rathna; Mohan, Panaiyur S.; Nixon, Ralph A.; Talanian, Robert V.; Keegan, Martha G.; Herzog, Linda; Allen, Hamish

doi:10.1006/abbi.1998.0748

Cited by 237 publications

(186 citation statements)

References 45 publications

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“…41 Calpain has been shown to positively regulate caspase 3 and caspase 7 activities independently of caspase 8. 46,90 In turn, caspase activation leads to proteolytic cleavage of numerous intracellular targets, including CSP, which upregulates calpain activity, 91 and the adhesion molecules desmogleins, desmocollins, and ␤-and ␥-catenins. [92][93][94] The extracellular domains of desmoglein 3 and desmocollin 3 are released from the cell surface by a metalloproteinase activity, because in the presence of caspase and/or metalloproteinase inhibitors, both cleavage reactions are almost completely inhibited.…”

Section: Discussionmentioning

confidence: 99%

Novel Mechanisms of Target Cell Death and Survival and of Therapeutic Action of IVIg in Pemphigus

Arredondo

Chernyavsky

Karaouni

et al. 2005

The American Journal of Pathology

111

139

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Section: Discussionmentioning

confidence: 99%

Novel Mechanisms of Target Cell Death and Survival and of Therapeutic Action of IVIg in Pemphigus

Arredondo

Chernyavsky

Karaouni

et al. 2005

The American Journal of Pathology

111

139

View full text Add to dashboard Cite

show abstract

“…For instance, calpains have been described by some to act upstream of caspase processing, but others implicated them downstream of caspase activation. [49][50][51][52][53][54] Likewise, some found apoptosis induced by FAS ligand to be independent of calpains, but others implicated them in FAS receptormediated apoptosis of neutrophils. 55,56 Our observation that Bfl-1 sensitizes cells to TNF/CHX-induced death, coincident with its proteolytic processing by m-calpain or a calpain-like activity in vivo, is consistent with reports indicating that caspases and calpains can cleave prosurvival Bcl-xL or Bcl-2 proteins leading to the emergence of a prodeath fragment.…”

Section: Discussionmentioning

confidence: 99%

“…56 Moreover, previous work showed that calpastatin is sensitive to proteolysis by recombinant caspase-1, -3 and -7 and that FAS-induced cell death in Jurkat T-cells or in human neuroblastoma cells converges on calpastatin degradation. 54 Thus, by converging on caspase activation, death receptor pathways might activate calpain via degradation of calpastatin. A model positioning caspase-8 upstream of calpastatin and m-calpain activation is supported by the inability of recombinant caspase-8 to cleave directly GFP-Bfl-1 in our in vitro assays (Figure 7 and data not shown).…”

Section: Discussionmentioning

confidence: 99%

Constitutive proteasome-mediated turnover of Bfl-1/A1 and its processing in response to TNF receptor activation in FL5.12 pro-B cells convert it into a prodeath factor

et al. 2005

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Bfl-1/A1 is generally recognized as a Bcl-2-related inhibitor of apoptosis. We show that Bfl-1 undergoes constitutive ubiquitin/proteasome-mediated turnover. Moreover, while Bfl-1 suppresses apoptosis induced by staurosporine or cytokine withdrawal, it is proapoptotic in response to tumor necrosis factor (TNF) receptor activation in FL5.12 pro-B cells. Its anti-versus proapoptotic effect is regulated by two proteolytic events: (1) its constitutive proteasome-mediated turnover and (2) its TNF/cycloheximide (CHX)-induced cleavage by l-calpain, or a calpain-like activity, coincident with acquisition of a proapoptotic phenotype. In vitro studies suggest that calpain-mediated cleavage of Bfl-1 occurs between its Bcl-2 homology (BH)4 and BH3 domains. This would be consistent with the generation of a proapoptotic Bax-like BH1-3 molecule. Overall, our studies uncovered two new regulatory mechanisms that play a decisive role in determining Bfl-1's prosurvival versus prodeath activities. These findings might provide important clues to counteract chemoresistance in tumor cells that highly express Bfl-1.

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“…26 There is also evidence that caspases can upregulate calpain activity through direct cleavage of calpastatin, the endogenous protein inhibitor of calpains. 88 Therefore, caspases were suggested to indirectly upregulate calpain activity. Most cell death systems leading to activation of calpains seem to produce an apoptotic-like morphology.…”

Section: Calpainsmentioning

confidence: 99%

Death penalty for keratinocytes: apoptosis versus cornification

et al. 2005

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Homeostasis implies a balance between cell growth and cell death. This balance is essential for the development and maintenance of multicellular organisms. Homeostasis is controlled by several mechanisms including apoptosis, a process by which cells condemned to death are completely eliminated. However, in some cases, total destruction and removal of dead cells is not desirable, as when they fulfil a specific function such as formation of the skin barrier provided by corneocytes, also known as terminally differentiated keratinocytes. In this case, programmed cell death results in accumulation of functional cell corpses. Previously, this process has been associated with apoptotic cell death. In this overview, we discuss differences and similarities in the molecular regulation of epidermal programmed cell death and apoptosis. We conclude that despite earlier confusion, apoptosis and cornification occur through distinct molecular pathways, and that possibly antiapoptotic mechanisms are implicated in the terminal differentiation of keratinocytes.

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Caspase-Mediated Fragmentation of Calpain Inhibitor Protein Calpastatin during Apoptosis

Cited by 237 publications

References 45 publications

Novel Mechanisms of Target Cell Death and Survival and of Therapeutic Action of IVIg in Pemphigus

Novel Mechanisms of Target Cell Death and Survival and of Therapeutic Action of IVIg in Pemphigus

Constitutive proteasome-mediated turnover of Bfl-1/A1 and its processing in response to TNF receptor activation in FL5.12 pro-B cells convert it into a prodeath factor

Death penalty for keratinocytes: apoptosis versus cornification

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