Stress Response of Lysosomal Cysteine Proteinases in Rat C6 Glioma Cells

Xu, Chi; Fracella, Franco; Richter‐Landsberg, Christiane; Rensing, Ludger

doi:10.1016/s0305-0491(96)00326-4

Cited by 4 publications

(6 citation statements)

References 25 publications

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“…A comparison of the N-terminal amino acid sequence and the total amino acid contents of this proteinase with protein data bases revealed no homology to other known proteinases. A comparison of the proteinase with the heat-induced sulfate proteinases in tomato [28], cathepsin B in CHO cells [17], as well as other heat-induced proteinases [7], [10], [11], showed that the heat-induced 65 kDa ATP-BPase of C6 cells has no similarity with them in their N-terminal 1-9 amino acid sequence, pH optimum, molecular weight and the effect of inhibitors. But it was reported that the heat shock (44 for 1 h and recovery for 1 h) could induce Neurospora crassa to express a 65 kDa ATP-BPase [20].…”

Section: Discussionmentioning

confidence: 99%

“…The proteinases were incubated in a buffer (0.1 M glycine, 5 mM CaCl 2 , 4 mM MgCl 2 , 1 mM ATP, different pH) with serum albumin (0.5 g/L) at 37 for 6 h. The proteinase activity was calculated by determining the undegraded serum albumin in the buffer [7].…”

Section: Atp-bpase Activity Analysismentioning

confidence: 99%

“…There are many reports on their culture, growth and metabolism [3][4][5]. However, up to now, we know nothing about their ATP-BPases except calpain [6] and acidic lysosomal proteinases [7].…”

Section: Introductionmentioning

confidence: 99%

“…Proteolysis is essential to life [7], [9] and it is also an essential component in the cellular response to starvation and stress [10]. It is now well established that important pathways of the cellular proteolytic systems are the ubiquitin-dependent selective proteinases in cytoplasmic proteasomes [11] and the selective and non-selective proteinases in lysosomes [12][13][14].…”

Section: Introductionmentioning

confidence: 99%

“…The ubiquitin-dependent and lysosomal selective proteolytic systems all require ATP to degrade proteins [15], [16]. It has been shown that heat shock can activate the multicatalytic proteinases (proteasomes) [11] and lysosomal enzymes [7], [17] in mammalian cells. And another group of proteinases, named ATP-DPases, have been discovered in recent years.…”

Section: Introductionmentioning

confidence: 99%

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Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells

Zhang

Techel

et al. 1999

Cell Res

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The 45, 55, 65 and 100 kDa ATP-binding proteinases (ATPBPases) of the heat-shocked (44 for 30 min, recovery for 12 h) rat C6 glioma cells were purified by DEAE-ionexchange and ATP-affinity chromatography. Their molecular masses, isoelectric points (pI), pH-optima and other properties were analyzed by native proteinase gels. It was shown that the 65 kDa ATPBPase is specifically induced by heat shock and not detectable in control cells. Its N-terminal 1-9 amino acid sequence was determined by Edman degradation, but no homologies to other proteins in the protein data bases were found. 30 and 31 kDa proteinases can be cleaved from the 45, 55 and 65 kDa proteinases to which they are linked. A possible relationship of the heat-induced 65 kDa ATP-BPase with the ATP-dependent proteinases (ATP-DPases) in prokaryotes and eukaryotes is discussed. 136

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Section: Discussionmentioning

confidence: 99%

Section: Atp-bpase Activity Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells

Zhang

Techel

et al. 1999

Cell Res

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Exertional heat illness and human gene expression

Sonna

Sawka

Lilly

2007

Progress in Brain Research

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Selected Contribution: Effect of acute heat shock on gene expression by human peripheral blood mononuclear cells

Sonna

Gaffin

Pratt

et al. 2002

Journal of Applied Physiology

105

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We studied the effect of heat shock on gene expression by normal human cells. Peripheral blood mononuclear cells (PBMCs) were obtained from healthy adults. Paired samples from each subject were subjected to either 20 min of heat shock (43 degrees C) or control (37 degrees C) conditions and then returned to 37 degrees C. RNA was isolated 160 min later, and five representative samples were analyzed on Affymetrix gene chip arrays containing approximately 12,600 probes. A biologically meaningful effect was defined as a statistically significant, twofold or greater difference in expression of sequences that were detected in all five experiments under control (downregulated sequences) or heat shock (upregulated sequences) conditions. Changes occurred in 395 sequences (227 increased by heat shock, 168 decreased), representing 353 Unigene numbers, in every functional category previously implicated in the heat shock response. By RT-PCR, we confirmed the findings for one upregulated sequence (Rad, a G protein) and one downregulated sequence (osteopontin, a cytokine). We conclude that heat shock causes extensive gene expression changes in PBMCs, affecting all functional categories of the heat shock response.

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Stress Response of Lysosomal Cysteine Proteinases in Rat C6 Glioma Cells

Cited by 4 publications

References 25 publications

Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells

Heat shock induction of a 65 kDa ATP-binding proteinase in rat C6 glioma cells

Exertional heat illness and human gene expression

Selected Contribution: Effect of acute heat shock on gene expression by human peripheral blood mononuclear cells

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