The protective effect of hypoxic preconditioning on cortical neuronal cultures is associated with increases in the activity of several antioxidant enzymes

Arthur, Peter G.; Lim, Sang-Cheol; Meloni, Bruno P.; Munns, Shane E.; Chan, Audrey S.; Knuckey, Neville W.

doi:10.1016/j.brainres.2004.05.031

Cited by 71 publications

(54 citation statements)

References 35 publications

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“…Liu XQ et al Acta Pharmacologica Sinica npg Hypoxia-inducible factor (HIF) Arthur et al developed two in vitro models of ischemia/reperfusion: OGD, in which neuronal cell death was predominantly by necrosis (necrotic model) and programmed cell death (PCD model). Hypoxic preconditioning 24 h prior to OGD significantly reduced cell death from 83% to 22% in the necrotic model and 68% to 11% in the PCD model [64] . In this IPC model, the activity of the antioxidant enzymes glutathione peroxidase, glutathione reductase, and Mn superoxide dismutase were significantly increased, whereas superoxide and hydrogen peroxide concentrations following OGD were significantly lower in the IPC group.…”

Section: Heat Shock Proteins (Hsps)mentioning

confidence: 87%

The neuroprotective mechanism of brain ischemic preconditioning

2009

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Brain ischemia is one of the most common causes of death and the leading cause of adult disability in the world. Brain ischemic preconditioning (BIP) refers to a transient, sublethal ischemia which results in tolerance to later, otherwise lethal, cerebral ischemia. Many attempts have been made to understand the molecular and cellular mechanisms underlying the neuroprotection offered by ischemic preconditioning. Many studies have shown that neuroprotective mechanisms may involve a series of molecular regulatory pathways including activation of the N-methyl-D-aspartate (NMDA) and adenosine receptors; activation of intracellular signaling pathways such as mitogen activated protein kinases (MAPK) and other protein kinases; upregulation of Bcl-2 and heat shock proteins (HSPs); and activation of the ubiquitin-proteasome pathway and the autophagic-lysosomal pathway. A better understanding of the processes that lead to cell death after stroke as well as of the endogenous neuroprotective mechanisms by which BIP protects against brain ischemic insults could help to develop new therapeutic strategies for this devastating neurological disease. The purpose of the present review is to summarize the neuroprotective mechanisms of BIP and to discuss the possibility of mimicking ischemic preconditioning as a new strategy for preventive treatment of ischemia.

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Section: Heat Shock Proteins (Hsps)mentioning

confidence: 87%

The neuroprotective mechanism of brain ischemic preconditioning

2009

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“…Dermcidin may subsequently influence survival via two or more mechanisms. Preconditioning to oxidative stress by enzymatic induction is well described in hepatic cells, is active in neuronal cells (in which Y-P30 is protective) (Arthur et al, 2004), and may be one mechanism by which dermcidin acts in HuH7 cells. Alternatively, expression might protect cells from oxidative stress by induction of the proteasome system, which is known to be activated by glycosylated PIF (Smith and Tisdale, 2003;Whitehouse and Tisdale, 2003).…”

Section: Discussionmentioning

confidence: 99%

Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues

et al. 2006

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Proteolysis-inducing factor, a cachexia-inducing tumour product, is an N-glycosylated peptide with homology to the unglycosylated neuronal survival peptide Y-P30 and a predicted product of the dermcidin gene, a pro-survival oncogene in breast cancer. We aimed to investigate whether dermcidin is pro-survival in liver cells, in which proteolysis-inducing factor induces catabolism, and to determine the role of potentially glycosylated asparagine residues in this function. Reverse cloning of proteolysis-inducing factor demonstrated B100% homology with the dermcidin cDNA. This cDNA was cloned into pcDNA3.1 þ and both asparagine residues removed using site-directed mutagenesis. In vitro translation demonstrated signal peptide production, but no difference in molecular weight between the products of native and mutant vectors. Immunocytochemistry of HuH7 cells transiently transfected with V5-His-tagged dermcidin confirmed targeting to the secretory pathway. Stable transfection conferred protection against oxidative stress. This was abrogated by mutation of both asparagines in combination, but not by mutation of either asparagine alone. These findings suggest that dermcidin may function as an oncogene in hepatic as well as breast cells. Glycosylation does not appear to be required, but the importance of asparagine residues suggests a role for the proteolysis-inducing factor core peptide domain.

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“…In rats previously subjected to focal ischemic preconditioning, there was a significant reduction in the volume of the cortical lesion produced by a subsequent MCAO, and this ischemic tolerance was associated with a significant reduction of lipid peroxidation (69). In cultured neurons subjected to hypoxic preconditioning, the activity of the antioxidant enzymes glutathione peroxidase, glutathione reductase, and Mn-SOD were significantly increased, and superoxide and hydrogen peroxide concentrations following a subsequent episode of oxygenglucose deprivation were lower in preconditioned cultures (14). However, according to the numerous studies dedicated to the key antioxidant enzymes SODs, catalase, and glutathione peroxidase, brain tolerance is not always associated with increased activities or upregulation of these enzymes.…”

Section: Defense Mechanisms Against Oxidative Stressmentioning

confidence: 99%

Molecular Physiology of Preconditioning-Induced Brain Tolerance to Ischemia

Obrenovitch¹

2008

Physiological Reviews

230

176

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Ischemic tolerance describes the adaptive biological response of cells and organs that is initiated by preconditioning (i.e., exposure to stressor of mild severity) and the associated period during which their resistance to ischemia is markedly increased. This topic is attracting much attention because preconditioning-induced ischemic tolerance is an effective experimental probe to understand how the brain protects itself. This review is focused on the molecular and related functional changes that are associated with, and may contribute to, brain ischemic tolerance. When the tolerant brain is subjected to ischemia, the resulting insult severity (i.e., residual blood flow, disruption of cellular transmembrane gradients) appears to be the same as in the naive brain, but the ensuing lesion is substantially reduced. This suggests that the adaptive changes in the tolerant brain may be primarily directed against postischemic and delayed processes that contribute to ischemic damage, but adaptive changes that are beneficial during the subsequent test insult cannot be ruled out. It has become clear that multiple effectors contribute to ischemic tolerance, including: 1) activation of fundamental cellular defense mechanisms such as antioxidant systems, heat shock proteins, and cell death/survival determinants; 2) responses at tissue level, especially reduced inflammatory responsiveness; and 3) a shift of the neuronal excitatory/inhibitory balance toward inhibition. Accordingly, an improved knowledge of preconditioning/ischemic tolerance should help us to identify neuroprotective strategies that are similar in nature to combination therapy, hence potentially capable of suppressing the multiple, parallel pathophysiological events that cause ischemic brain damage.

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The protective effect of hypoxic preconditioning on cortical neuronal cultures is associated with increases in the activity of several antioxidant enzymes

Cited by 71 publications

References 35 publications

The neuroprotective mechanism of brain ischemic preconditioning

The neuroprotective mechanism of brain ischemic preconditioning

Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues

Molecular Physiology of Preconditioning-Induced Brain Tolerance to Ischemia

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