Bergmann glia utilize active caspase-3 for differentiation

Oomman, Sowmini; Strahlendorf, Howard K.; Strahlendorf, Jean C.

doi:10.1016/j.brainres.2006.01.041

Cited by 51 publications

(41 citation statements)

References 72 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Muscle development and osteoblast differentiation are compromised in the absence of caspase-3 (17,33,34). Caspase-3 also plays important functions in neurogenesis, synaptic activity, neuronal growth cone guidance, and glial development (7,16,37). Histological analyses of muscle, bone, and brain tissues did not reveal any defect in the KI mice (data now shown).…”

Section: Discussionmentioning

confidence: 81%

Caspase-3 Protects Stressed Organs against Cell Death

Khalil

Peltzer

Walicki

et al. 2012

Molecular and Cellular Biology

View full text Add to dashboard Cite

The ability to generate appropriate defense responses is crucial for the survival of an organism exposed to pathogenesis-inducing insults. However, the mechanisms that allow tissues and organs to cope with such stresses are poorly understood. Here we show that caspase-3-knockout mice or caspase inhibitor-treated mice were defective in activating the antiapoptotic Akt kinase in response to various chemical and environmental stresses causing sunburns, cardiomyopathy, or colitis. Defective Akt activation in caspase-3-knockout mice was accompanied by increased cell death and impaired survival in some cases. Mice homozygous for a mutation in RasGAP that prevents its cleavage by caspase-3 exhibited a similar defect in Akt activation, leading to increased apoptosis in stressed organs, marked deterioration of their physiological functions, and stronger disease development. Our results provide evidence for the relevance of caspase-3 as a stress intensity sensor that controls cell fate by either initiating a RasGAP cleavage-dependent cell resistance program or a cell suicide response. Executioner caspases mediate cell death during apoptosis (45). Of these, caspase-3 has the ability to cleave the majority of the caspase substrates (43), and its activity is required for the induction of cell death in response to many apoptotic stimuli (1). While executioner caspases are indispensable for apoptosis, there are situations when their activation does not lead to death. For example, healthy dividing cells can weakly activate caspase-3 in response to mild stresses (47). Caspase-3 also participates, in an apoptosisindependent manner, in T and B cell homeostasis (35,46), in microglia activation (6), in long-term depression (26), and in muscle (17), monocyte (44), embryonic stem cell (18), and erythroid cell (13) differentiation. However, it remains unclear how activation of caspase-3 under these conditions does not eventually lead to cell death (1, 24). Cells could have an intrinsic ability to tolerate low caspase activity by constitutively expressing antiapoptotic molecules, such as members of the inhibitors of the apoptosis protein family, or may stimulate antiapoptotic pathways in parallel to caspase activation (24). Alternatively, the caspases themselves might activate prosurvival pathways, in particular, when they are mildly stimulated. Indeed, there is evidence in cultured cells that caspase-3 mediates neuroprotection after preconditioning (30) and that caspase-3 activity turns on the antiapoptotic Akt kinase following partial cleavage of the RasGAP protein (47). Other caspase substrates that could potentially induce protective signals once cleaved include p27 kip1 (14), Lyn (28), synphilin-1 (19), and Rb (42), yet the physiological importance of these cleaved substrates has not been evaluated to date.In the present study, we have investigated the role played by caspase-3 and its substrate p120 RasGAP in the induction of the antiapoptotic Akt kinase in stressed tissues in vivo. MATERIALS AND METHODS Caspase-3-KO mice. B6.129S1...

show abstract

Section: Discussionmentioning

confidence: 81%

Caspase-3 Protects Stressed Organs against Cell Death

Khalil

Peltzer

Walicki

et al. 2012

Molecular and Cellular Biology

View full text Add to dashboard Cite

show abstract

“…Although the preponderance of data has emerged from work in the immune system and peripheral organs, several studies have also suggested non-apoptotic roles of caspase-3 in the CNS. Under physiological conditions, caspase-3 has been implicated in neuronal cytoskeletal changes (Rohn et al, 2004), in synaptic remodeling (Dash et al, 2000;Shimohama et al, 2001), in neuronal survival associated with preconditioning (Garnier et al 2003;McLaughlin et al, 2003;Tanaka et al, 2004), in the differentiation of cerebellar Bergmann glial cells (Oomman et al, 2004(Oomman et al, , 2005(Oomman et al, , 2006, and as a marker of astroglial subpopulations (Noyan-Ashraf et al, 2005). Accordingly, following excitotoxic damage in the neonatal brain we have demonstrated that presence of cleaved caspase-3 in nitrated reactive astrocytes in the absence of cell death (Acarin et al, 2005).…”

Section: Introductionmentioning

confidence: 79%

“…With regards to glial cell differentiation, Oomann and coworkers, who have described cleaved caspase-3 in Bergmann glia during postnatal development in the absence of apoptotic or proliferation markers, have demonstrated a role of this protease in differentiation processes (Oomman et al, 2004(Oomman et al, , 2005(Oomman et al, , 2006. In addition, it was recently shown that constitutive non-apoptotic expression of the cleaved form of caspase-3 occurs in the nuclei of a subpopulation of astrocytes in the cerebellar cortex, hippocampus, and spinal cord of adult rats of different strains, which show expression of the sodium dependent glutamate transporter (EAAT1, GLAST) (Noyan-Ashraf et al, 2005).…”

Section: Presence Of Caspase-cleaved Gfapmentioning

confidence: 99%

Caspase‐3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation

Acarín¹,

Villapol²,

Faiz³

et al. 2007

Glia

View full text Add to dashboard Cite

Caspase-3 has classically been defined as the main executioner of programmed cell death. However, recent data supports the participation of this protease in non-apoptotic cellular events including cell proliferation, cell cycle regulation, and cellular differentiation. In this study, astroglial cleavage of caspase-3 was analyzed following excitotoxic damage in postnatal rats to determine if its presence is associated with apoptotic cell death, cell proliferation, or cytoskeletal remodeling. A well-characterized in vivo model of excitotoxicity was studied, where damage was induced by intracortical injection of N-methyl-D-asparate (NMDA) in postnatal day 9 rats. Our results demonstrate that cleaved caspase-3 was mainly observed in the nucleus of activated astrocytes in the lesioned hemisphere as early as 4 h postlesion and persisted until the glial scar was formed at 7-14 days, and it was not associated with TUNEL labeling. Caspase-3 enzymatic activity was detected at 10 h and 1 day postlesion in astrocytes, and co-localized with caspasecleaved fragments of glial fibrillary acidic protein (CCP-GFAP). However, at longer survival times, when astroglial hypertrophy was observed, astroglial caspase-3 did not generally correlate with GFAP cleavage, but instead was associated with de novo expression of vimentin. Moreover, astroglial caspase-3 cleavage was not associated with BrdU incorporation. These results provide further evidence for a nontraditional role of caspases in cellular function that is independent of cell death and suggest that caspase activation is important for astroglial cytoskeleton remodeling following cellular injury. V V C 2007 Wiley-Liss, Inc.

show abstract

“…keratinocytes, Bergmann glia (Fernando et al, 2002;Okuyama et al, 2004;Oomman et al, 2006). Interestingly, Gross et al reported that LH and FSH induced increases in caspases-3 and -7 activities in GCs while these increases were accompanied by a decrease in apoptosis (Yacobi et al, 2004).…”

Section: Journal Of Cellular Physiologymentioning

confidence: 99%

Arsenic induced progesterone production in a caspase‐3‐dependent manner and changed redox status in preovulatory granulosa cells

Yuan

Yao

et al. 2011

Journal Cellular Physiology

View full text Add to dashboard Cite

Arsenic contamination is a principal environmental health threat throughout the world. However, little is known about the effect of arsenic on steroidogenesis in granulosa cells (GCs). We found that the treatment of preovulatory GCs with arsenite stimulated progesterone production. A significant increase in serum level of progesterone was observed in female Sprague-Dawley rats following arsenite treatment at a dose of 10 mg/L/rat/day for 7 days. Further experiments demonstrated that arsenite treatment did not change the level of intracellular cyclic AMP (cAMP) or phosphorylated ERK1/2 in preovulatory GCs; however, progesterone production was significantly decreased when cAMP-dependent protein kinase (PKA) or ERK1/2 pathway was inhibited. This implied that the effect of arsenite on progesterone production may require cAMP/PKA and ERK1/2 signaling but not depend on them. Furthermore, we found that arsenite decreased intracellular reactive oxygen species (ROS) but increased the antioxidant glutathione (GSH) levels and mitochondrial membrane potential (ΔΨm) in parallel to the changes in progesterone production. Progesterone antagonist blocked the arsenic-stimulated increase of GSH levels. Arsenite treatment induced caspase-3 activation, although no apoptosis was observed. Inhibition of caspase-3 activity significantly decreased progesterone production stimulated by arsenite or follicle-stimulating hormone (FSH). GSH depletion with buthionine sulfoximine led to cell apoptosis in response to arsenite treatment. Collectively, this study demonstrated for the first time that arsenite stimulates progesterone production through cleaved/active caspase-3-dependent pathway, and the increase of GSH level promoted by progesterone production may protect GCs against apoptosis and maintain the steroidogenesis of GCs in response to arsenite treatment.

show abstract

Bergmann glia utilize active caspase-3 for differentiation

Cited by 51 publications

References 72 publications

Caspase-3 Protects Stressed Organs against Cell Death

Caspase-3 Protects Stressed Organs against Cell Death

Caspase‐3 activation in astrocytes following postnatal excitotoxic damage correlates with cytoskeletal remodeling but not with cell death or proliferation

Arsenic induced progesterone production in a caspase‐3‐dependent manner and changed redox status in preovulatory granulosa cells

Contact Info

Product

Resources

About