Stress fibres–a Ca2+-independent store for annexins?

Babiychuk, Eduard B.; Babiychuk, Victoriia S.; Danilova, V. M.; Tregubov, V. S.; Сагач, В. Ф.; Draeger, Annette

doi:10.1016/s1570-9639(02)00456-9

Cited by 10 publications

(5 citation statements)

References 26 publications

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“…Cultures of human myometrium (passages 2-4) were performed as described earlier. 29 All cells were grown in 5% CO 2 at 371C in a humidified incubator. They were transiently transfected with plasmids using electroporation (BioRad) at 0.25 kV and analysed after incubating at 371C for 48 h.…”

Section: Methodsmentioning

confidence: 99%

Intracellular Ca2+ operates a switch between repair and lysis of streptolysin O-perforated cells

et al. 2009

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Pore-forming (poly)peptides originating from invading pathogens cause plasma membrane damage in target cells, with consequences as diverse as proliferation or cell death. However, the factors that define the outcome remain unknown. We show that in cells maintaining an intracellular Ca 2 þ concentration [Ca 2 þ ] i below a critical threshold of 10 lM, repair mechanisms seal off 'hot spots' of Ca 2 þ entry and shed them in the form of microparticles, leading to [ Plasma membrane pores formed by cytotoxic proteins and peptides disrupt the permeability barrier in a target cell. Pathogens gain access and kill host cells by secreting pore-forming toxins, whereas the blood complement system utilises the pore-forming proteins of membrane attack complexes to eliminate both pathogens and the pathogen-invaded cells. 1,2 As in particular, cells of the blood and the vascular systems are permanently exposed to potential deadly attacks by a variety of pore-forming (poly)peptides, it is not surprising that mechanisms repairing the damaged plasma membrane have evolved. [3][4][5][6] Biological effects occurring in the wake of membrane permeabilisation and its subsequent repair are multifaceted. Apart from the two obvious end points, complete recovery or death, recovering cells can newly acquire numerous (patho)physiological functions. 3,7,8 A rise in intracellular Ca 2 þ concentration [Ca 2 þ ] i is critical for successful plasma membrane repair and cell recovery, 9,10 whereas an intracellular Ca 2 þ overload is held responsible for the death of pore-bearing cells. 11 In addition, Ca 2 þ influx, followed by transcriptional activation, is thought to induce a variety of biological responses associated with sublytic effects of pore-forming toxins. 3,4,7,8 Thus, it appears that the extent of [Ca 2 þ ] i elevation following pore formation determines the fate of a targeted cell. Consequently, Morgan et al. 11 suggested that in nucleated cells, an initial increase in [Ca 2 þ ] i stimulates the recovery processes, allowing the cell to withstand a limited complement attack. The recovery might be associated with cellular activation and the production of inflammatory modulators, which, in turn, amplify an ongoing inflammatory response. 3,11 The authors further hypothesised that a more severe membrane damage causes a sharp rise in [Ca 2 þ ] i , which overwhelms all recovery processes. 11 However, how [Ca 2 þ ] i determines cell fate, how the acquisition of novel functions is initiated and how the 'point of no return' is defined remain unknown.In this study, we have undertaken a simultaneous, real-time characterisation of [Ca 2 þ ] i and plasma membrane dynamics in living cells permeabilised with the bacterial pore-forming toxin streptolysin O (SLO). Our data show that the fate of SLOperforated cells is dependent on their ability to control the extent of a pore-induced elevation in [Ca 2 þ ] i . We detail Ca 2 þ -dependent mechanisms that elicit either repair or irreversible structural changes in the plasma membrane and show how intracellula...

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Section: Methodsmentioning

confidence: 99%

Intracellular Ca2+ operates a switch between repair and lysis of streptolysin O-perforated cells

et al. 2009

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“…These annexins can also associate with F-actincontaining stress fibers in cultured smooth-muscle cells or fibroblasts in a Ca 2? -independent manner [112]. A complex of annexin A6 with actin has been suggested to stabilize the cardiomyocyte sarcolemma during cell stimulation [113].…”

Section: Annexins and The Cytoskeletonmentioning

confidence: 99%

The annexins: spatial and temporal coordination of signaling events during cellular stress

Monastyrskaya

Babiychuk

Draeger

2009

Cell. Mol. Life Sci.

125

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Annexins are a family of structurally related, Ca2+-sensitive proteins that bind to negatively charged phospholipids and establish specific interactions with other lipids and lipid microdomains. They are present in all eukaryotic cells and share a common folding motif, the "annexin core", which incorporates Ca2+- and membrane-binding sites. Annexins participate in a variety of intracellular processes, ranging from the regulation of membrane dynamics to cell migration, proliferation, and apoptosis. Here we focus on the role of annexins in cellular signaling during stress. A chronic stress response triggers the activation of different intracellular pathways, resulting in profound changes in Ca2+ and pH homeostasis and the production of lipid second messengers. We review the latest data on how these changes are sensed by the annexins, which have the ability to simultaneously interact with specific lipid and protein moieties at the plasma membrane, contributing to stress adaptation via regulation of various signaling pathways.

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“…However, these observations are at odds with studies showing that endocytosis occurs normally in cells lacking annexin 6 (47), and indeed the absence of any harmful phenotype in annexin 6 null mutant mice argues against any important regulatory role for annexin 6 in endocytosis (48). Calcium‐dependent shuttling of annexin 6, annexin 2 and actomyosin into lipid microdomains has been demonstrated in smooth muscle cells (49) and the authors suggest that annexin 2 may be able to translocate from actin stress fibres to the cell periphery in response to changes in cell plasticity.…”

Section: Organization Of the Membrane‐cytoskeletonmentioning

confidence: 99%

Annexin–Actin Interactions

Hayes

Rescher²,

Gerke³

et al. 2004

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238

187

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The actin cytoskeleton is a malleable framework of polymerised actin monomers that may be rapidly restructured to enable diverse cellular activities such as motility, endocytosis and cytokinesis. The regulation of actin dynamics involves the coordinated activity of numerous proteins, among which members of the annexin family of Ca 2+ -and phospholipid-binding proteins play an important role. Although the roles of annexins in actin dynamics are not understood at a mechanistic level, annexins have the requisite properties to integrate Ca 2+ -signaling with actin dynamics at membrane contact sites. In this review we discuss the current state of knowledge on this topic, and consider how and where annexins may fit into the complex molecular machinery that regulates the actin cytoskeleton.

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Stress fibres–a Ca2+-independent store for annexins?

Cited by 10 publications

References 26 publications

Intracellular Ca2+ operates a switch between repair and lysis of streptolysin O-perforated cells

Intracellular Ca2+ operates a switch between repair and lysis of streptolysin O-perforated cells

The annexins: spatial and temporal coordination of signaling events during cellular stress

Annexin–Actin Interactions

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