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1

Gene expression profiles for mitochondria sirtuins and poly(ADP-ribose) polymerases in amyloid Beta toxicity

100%
Strosznajder R., Wencel P.
Acta Neurobiologiae Experimentalis
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2015
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tom 75
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nr Supl.
BACKGROUND AND AIMS: Sirtuins (SIRTs) and poly(ADPribose) polymerases (PARPs) are NAD dependent enzymes engaged in the regulation of energy metabolism, transcription, DNA replication and repair. SIRTs type III histone deacetylases (HDAC) target histone and many other proteins in nucleus, cytoplasm and mitochondria. PARP-1 is responsible for over 90% of poly (ADPribosylation) in the brain. However, the role of these NAD dependent enzymes in neurodegeneration /neuroprotection is till now not fully elucidated. In many neurodegenerative disorders metabolism of amyloid precursor protein (APP) is altered, amyloid beta (Aβ) is released and NAD dependent metabolic pathways are affected. This study focused on gene expression profiles for SIRTs and PARPs and on their functional relationship in cells survival/death under Aβ toxicity. METHODS: PC-12 cells after exposition on exogenous Aβ1-42 oligomers (ABO -1 mM, 24 h) were used. Moreover, the effect of endogenously liberated Aβ in PC12 cells transfected with human gene for APP wild type (APPwt) and bearing Swedish mutation (APPsw) was investigated. The both served as experimental models. RESULTS: Our data indicated that ABO suppressed alpha secretase and enhanced gene expression for beta and gamma secretases. Moreover, ABO upregulated the gene expression for PARP-1, PARP-2 and SIRT4 which is responsible for monoADPribosylation of several mitochondrial proteins. The endogenously liberated Aβ in APPwt cells upregulated gene expression for PARP-1, -2 and decreased for SIRT5. In APPsw cells activation of genes for PARP -1,-2,-9 and for SIRT3 was observed. In our previous study we observed significant suppression of PARP activity in APPsw cells. CONCLUSIONS: These results suggest that NAD is not used by PARPs in APPsw cells and it may be available for Sirt3 which is involved in regulation of antioxidative enzymes. The functional interactions between these NAD dependent enzymes may play crucial role in regulation of cell survival under Aβ peptide toxicity. Supported by MRC.
2

Effect of 3-aminobenzamide on Bcl-2, Bax and AIF localization in hippocampal neurons altered by ischemia reperfusion injury. The immunocytochemical study

100%
Strosznajder R., Gajkowska B.
Acta Neurobiologiae Experimentalis
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2006
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tom 66
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nr 1
Poly(ADP-ribose) polymerase plays an important role in cell survival and death. Our previous histological and ultrastructural studies showed that PARP inhibitor 3-aminobenzamide (3-AB) protected neurons against death after ischemia. In this study we investigated the effect of 3-AB on the localization and expression of apoptosis inducing factor (AIF) and on two proteins from Bcl-2 family: Bcl-2 and Bax in hippocampal area CA1, on the 4th day after 3 min of forebrain ischemia in gerbils. Our results indicated that after ischemia AIF is preferentially translocated from the mitochondria to the cytoplasm and to the nucleus. Intravenous administration of 3-AB (30 mg/kg b.w.) prevents AIF translocation to the nucleus. AIF was mainly seen in the structurally unchanged mitochondria and Golgi complex. Moreover, after 3-AB administration overexpression of Bcl-2 protein was observed in mitochondrial membranes, rough endoplasmatic reticulum, Golgi complex, nuclear envelopes, and also in cytoplasm and in nucleus. These data suggest that inhibition of PARP activity may have a beneficial effect on hippocampal neurons through overexpression of Bcl-2 protein and suppression of AIF translocation to the nucleus.
3
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ATP activates phospholipase C in the cat carotid body in vitro

100%
Pokorski M., Strosznajder R.
Journal of Physiology and Pharmacology
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1997
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tom 48
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nr 3
4

Sphingosine-1-phosphate and its receptors signaling in neurodegeneration/neuroprotection

81%
Strosznajder J. B., Motyl J., Czubowicz K., Strosznajder R.
Acta Neurobiologiae Experimentalis
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2015
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tom 75
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nr Supl.
Sphingosine -1-phosphate (S1P) is synthesized by sphingosine kinases (SphK1/2E.C. 2.7.1.91) and exerts its function as intracellular messenger or acts in an autocrine or paracrine fashion through specific G protein operated receptors (S1P1-S1P5). Depending on SphK type and its localization S1P may influence different cell functions. S1P synthesized by SphK1 is involved in cell survival while produced by SphK2 may activate death signaling. S1P is degraded by phosphohydrolyses and irreversibly by S1P lyase (SPL, E.C.4.1.2.27) which appears to be very important in sphingolipid homeostasis. The alterations of sphingolipid rheostat is suggested to be crucial in pathogenesis/pathomechanism of neurodegenerative disorders. In our study we have evaluated the SphKs and SPL expression/activity as well as the role of S1P in different types of oxidative stress involved in neurodegenerative disorders. Moreover, the implications of SphK/S1P in the cell models of Alzheimer’s disease induced by amyloid peptides (AB) and alfa synuclein (ASN) were determined. Oxidative stress alters SphKs and SPL expression, activity and cells viability. In AD model significant decrease of SphK expression and activity/lower S1P synthesis leads to series of the following consecutive events: oxidative stress, down regulation of antiapoptotic protein Bcl-2, up-regulation of pro-apoptotic BAX and HrK and finally to cell’s death. Exogenous S1P and the agonist(s) of S1P1 or S1P3 receptors exert cytoprotective effects which are mediated by PI3/ Akt signaling pathway and by regulation of Bcl2 proteins. Summarizing, our data suggest that S1P, its receptor(s) agonists and inhibitors of SPL should be considered in therapy of neurodegenerative disorders. Supported by NCN grant 5870/P01/2011/40
5

Molecular mechanism of amyloid beta evoked alteration of cholinergic signaling in brain

81%
Srosznajder J., Zambrzycka A., Strosznajder R.
Acta Biochimica Polonica
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2003
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tom 50
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nr Supplement 1
6

Nitric oxide and poly(ADP- ribose) polymerase in signal transduction and neurodegeneration

71%
Strosznajder J., Jesko H., Chalimoniuk M., Zambrzycka A., Strosznajder R.
Acta Biochimica Polonica
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2003
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tom 50
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nr Supplement 1
7

Mitochondrial and nuclear targets of amyloid wita-evoked oxidative stress

71%
Jesko H., Strosznajder J., Cieslik M., Cakala M., Strosznajder R.
Acta Neurobiologiae Experimentalis
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2009
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tom 69
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nr 3
Amyloid β (Aβ) is responsible for mitochondrial failure and biochemical alterations linked to Alzheimer`s disease (AD). To better understand mechanisms of Aβ toxicity we investigated its mitochondrial and nuclear targets, apoptosis-inducing factor (AIF) and Poly(ADP-ribose) polymerase-1 (PARP-1) in PC12 cells transfected with wild type (APPwt) or double Swedish-mutated human Amyloid Precursor Protein gene (APPsw) characterized by different Aβ concentrations. We found close relationship between Aβ level and cyclooxygenase (COX)- and lipoxygenase (LOX)-related free radical formation leading to p65/NF-κB nuclear translocation. COX and LOX inhibitors protected APPsw cells against p65 translocation. Aβ-evoked oxidative stress enhanced mitochondrial AIF level and inhibited PARP-1 in APPsw cells. Nitrosative stress evoked by 0.5 mM sodium nitroprusside (SNP) had no further effect on Aβ-altered PARP-1 activity and mitochondrial AIF level in APPsw cells. However, SNP evoked death of 70–80% of all cell types after 24 h. COX and LOX inhibitors had ameliorating effect in these conditions. Our data indicated that double Swedish mutation in APP signifi cantly increased cell vulnerability to oxidative stress. Enhanced mitochondrial AIF level and PARP-1 inhibition might be responsible for cell survival under oxidative stress evoked by accumulating Aβ in APPsw cells. COX and LOX inhibitors protected the cells against death caused by simultaneous Aβ toxicity and nitrosative stress.
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