Heat Shock and Apoptosis: The Two Defense Systems of the Organism May Have Overlapping Molecular Elements

Punyiczki, Mária; Fésüs, László

doi:10.1111/j.1749-6632.1998.tb08978.x

Cited by 46 publications

(33 citation statements)

References 72 publications

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“…It is likely that TCP-16 acts in combination with other macromolecules, which are activated by DA in order to induce neuronal death. It is possible that under conditions of severe stress , when increasing amounts of damaged proteins accumulate in the cells, stress proteins serve as tags to mark and route the unfolded proteins to the cellular degradation machinery (Punyiczki and Fesus , 1998). Indeed, we observed increased protein degradation following DA treatment (data not shown).…”

Section: Discussionmentioning

confidence: 68%

The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity

Barzilai

Zilkha‐Falb

Daily

et al. 2000

Advances in Research on Neurodegeneration

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Summary. Parkinson 's disease (PD) is a progressive neurological disorder caused by rather selective degeneration of the dopaminergic (DA) neurons in the substantia nigra . Though subject to intensive research, the etiology of this nigral neuronal loss is still enigmatic and treatment is basically symptomatic. The current major hypothesis suggests that nigraI neuronal death in PD is due to excessive oxidative stress generated by auto-and enzymatic oxidation of the endogenous neurotransmitter dopamine (DA ), the formation of neuromelanin and presence of high concentrations of iron.We have found that DA toxicity is mediated through its oxidative metabolites. Whereas thiol-containing antioxidants provided marked protection against DA toxicity, ascorbic acid accelerated DA-induced death. Using the differential display approach, we sought to isolate and characterize genes whose expression is altered in response to DA toxicity. We found an upregulation of the collapsin response mediator protein (CRM) and TCP-lb in sympathetic neurons, which undergo dopamine-induced apoptosis. The isolation of these genes led us to examine the expression and activity of CRM and TCP-lb related genes. Indeed, we found a significant induction of mRNAs of the secreted collapsin-l and the mitochondrial stress protein HSP60. Antibodies directed against collapsin -l provided marked and prolonged protection of several neuronal cell types from dopamine-induced apoptosis. In a parallel study, using antisense technology, we found that inhibition of TCP-lb expression significantly reduced DA-induced neuronal death. These findings suggest a functional role for collapsin-l and TCP-lb as positive mediators of DA-induced neuronal apoptosis.

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Section: Discussionmentioning

confidence: 68%

The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity

Barzilai

Zilkha‐Falb

Daily

et al. 2000

Advances in Research on Neurodegeneration

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“…In addition, NOS can act on arginine to produce NO, which generates free radicals that are harmful to the body. Lipid peroxide can damage the plasma membrane, whereas normal cells do not release LDH from the cytoplasm, making LDH release a useful indicator of plasma membrane damage (Davila et al 1998;Punyiczki and Fesus 1998;Jin 2007). Methionine inhibited the heat-induced LDH leakage.…”

Section: Discussionmentioning

confidence: 99%

Methionine protects against hyperthermia-induced cell injury in cultured bovine mammary epithelial cells

Han

Yang

2015

Cell Stress and Chaperones

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The aim of this study was to investigate the effects of methionine on cell proliferation, antioxidant activity, apoptosis, the expression levels of related genes (HSF-1, HSP70, Bax and Bcl-2) and the expression levels of protein (HSP70) in mammary epithelial cells, after heat treatment. Methionine (60 mg/L) increased the viability and attenuated morphological damage in hyperthermia-treated bovine mammary epithelial cells (BMECs). Additionally, methionine significantly reduced lactate dehydrogenase leakage, malondialdehyde formation, nitric oxide, and nitric oxide synthase activity. Superoxide dismutase, catalase, and glutathione peroxidase enzymatic activity was increased significantly in the presence of methionine. Bovine mammary epithelial cells also exhibited a certain amount of HSP70 reserve after methionine pretreatment for 24 h, and the expression level of the HSP70 gene and protein further increased with incubation at 42°C for 30 min. Compared to the control, the expression of HSF-1 mRNA increased, and there was a significantly reduced expression of Bax/Bcl-2 mRNA and a reduced activity of caspase-3 against heat stress. Methionine also increased survival and decreased early apoptosis of hyperthermia-treated BMECs. Thus, methionine has cytoprotective effects on hyperthermia-induced damage in BMECs.

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“…Hsp70 upregulation correlates with improved survival of stressed cells, but the mechanism of action remains unclear (Latchman, 1995;Punyiczki and Fesus, 1998;Samali and Orrenius, 1998;Vayssier and Polla, 1998). Caspase-3 activation is one of the intracellular events mediating spinal motoneuron death after trophic factor deprivation in vitro and during naturally occurring motoneuron death in vivo (Li et al, , 2001.…”

Section: Caspase-3 Activation Is Reduced When Motoneurons Are Treatedmentioning

confidence: 99%

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

Robinson¹,

Tidwell²,

Gould³

et al. 2005

J. Neurosci.

111

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The dependence of developing spinal motoneuron survival on a soluble factor(s) from their target, muscle tissue is well established both in vivo and in vitro. Considering this apparent dependence, we examined whether a specific component of the stress response mediates motoneuron survival in trophic factor-deprived environments. We demonstrate that, although endogenous expression of heat shock protein 70 (HSP70) did not change during trophic factor deprivation, application of e-rhHsp70 (exogenous recombinant human Hsp70) promoted motoneuron survival. Conversely, depletion of HSP70 from chick muscle extract (MEx) potently reduces the survivalpromoting activity of MEx. Additionally, exogenous treatment with or spinal cord overexpression of Hsp70 enhances motoneuron survival in vivo during the period of naturally occurring cell death [programmed cell death (PCD)]. Hindlimb muscle cells and lumbar spinal astrocytes readily secrete HSP70 in vitro, suggesting potential physiological sources of extracellular Hsp70 for motoneurons. However, in contrast to exogenous treatment with or overexpression of Hsp70 in vivo, muscle-targeted injections of this factor in an ex vivo preparation fail to attenuate motoneuron PCD. These data (1) suggest that motoneuron survival requirements may extend beyond classical trophic factors to include HSP70, (2) indicate that the source of this factor is instrumental in determining its trophic function, and (3) may therefore influence therapeutic strategies designed to increase motoneuron Hsp70 signaling during disease or injury.

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Heat Shock and Apoptosis: The Two Defense Systems of the Organism May Have Overlapping Molecular Elements

Cited by 46 publications

References 72 publications

The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity

The molecular mechanism of dopamine-induced apoptosis: identification and characterization of genes that mediate dopamine toxicity

Methionine protects against hyperthermia-induced cell injury in cultured bovine mammary epithelial cells

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

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