Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity 1 1Edited by M. Yaniv

Jäschke, Anja; Mi, Huaifeng; Tropschug, Maximilian

doi:10.1006/jmbi.1998.1644

Cited by 62 publications

(54 citation statements)

References 47 publications

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“…An involvement of PPIase activity in oxygen defense has been reported for cyclophilin 18 in rabbit blastocysts (51). The thiol-specific antioxidant protein Aop1 has also been reported to bind human cyclophilin 18 (52). Taken together, these reports and our data indicate that cyclophilins are important components of our oxygen defense system.…”

Section: Discussionsupporting

confidence: 80%

Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization

Lin

Lechleiter

2002

Journal of Biological Chemistry

168

121

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Cyclophilin D (CyPD) is thought to sensitize opening of the mitochondrial permeability transition pore (mPTP) based on the findings that cyclosporin A (CsA), a pseudo-CyPD substrate, hyperpolarizes the mitochondrial membrane potential (⌬⌿) and inhibits apoptosis. We provide evidence that contrasts with this model. Using live cell imaging and two photon microscopy, we report that overexpression of CyPD desensitizes HEK293 and rat glioma C6 cells to apoptotic stimuli. By site-directed mutagenesis of CyPD that compromises peptidyl-prolyl cis-trans isomerase (PPIase) activity, we demonstrate that the mechanism involved in this protective effect requires PPIase activity. Furthermore, we show that, under resting conditions, ⌬⌿ is hyperpolarized in CyPD wild type-overexpressing cells but not in cells overexpressing mutant forms of CyPD that lack PPIase activity. Finally, in glutathione S-transferase (GST) pull-down assays, we demonstrate that CyPD binding to the adenine nucleotide translocator (ANT), which is considered to be the core component of the mPTP, is not affected by the loss of PPIase activity. Collectively, our data suggest that CyPD should be viewed as a cell survival-signaling molecule and indicate a protective role of CyPD against apoptosis that is mediated by one or more targets other than the ANT.

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Section: Discussionsupporting

confidence: 80%

Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization

Lin

Lechleiter

2002

Journal of Biological Chemistry

168

121

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“…Furthermore we detected an additional dimer signal of Prx II after exposure of INS-1 cells to a combination of three cytokines, probably caused by the interaction with cytoplasmic proteins. Several lines of evidence support the view that cyclophilins with molecular masses around 20 K are able to bind to peroxiredoxins and could enhance their antioxidant activity [56,57].…”

Section: Discussionmentioning

confidence: 80%

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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Aims/hypothesis. Insulin-producing beta cells are destroyed by oxidative and nitrosative stress during the pathogenesis of Type I (insulin-dependent) diabetes mellitus. These cells are more sensitive than others due to their deficiency of well known antioxidant enzymes like superoxide dismutase, glutathione peroxidase and catalase. However the peroxiredoxins discovered in the past decade form a large family of highly conserved thioredoxin-dependent peroxide reductases, which are present in most tissues. We investigated whether peroxiredoxins I and II are present in pancreatic beta cells and if they are inducible by oxidative and nitrosative stress. Methods. To detect these enzymes in insulin-producing beta cells we used semiquantitative RT-PCR, western blots and immunohistochemistry. The expression of peroxiredoxins I and II was analysed after treatment with cytokines, hydrogen peroxide, alloxan or streptozotocin in the rat insulinoma cells INS-1 using RT-PCR and western blots. Results. We show that peroxiredoxins I and II are present in the cytoplasm of pancreatic islet cells as well as in insulinoma cell lines βTC6-F7 and INS-1. Peroxiredoxins I and II were up-regulated by all stress agents used. Conclusion/interpretation. Beta cells, undersupplied with well characterized antioxidant enzymes, possess an additional antioxidant system which is inducible by oxidative as well as nitrosative stress. [Diabetologia (2002) 45:867-876]

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“…3, upon reducing conditions the association was remarkably decreased in a dose-dependent manner, suggesting that the in vivo association of MIF and PAG may be mediated through disulfide linkages of cysteine residues. Recent studies have suggested that MIF and thiol antioxidants could be bridged through inter-chain disulfides (24,37,38). It is necessary to determine whether the conserved cysteine residues of PAG could influence homo-and heterodimerization and whether this complex formation contributes toward the regulation of functional activities of interacting partners.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Macrophage Migration Inhibitory Factor and Thiol-specific Antioxidant Protein PAG by Direct Interaction

Jung

Kim

Chae

et al. 2001

Journal of Biological Chemistry

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Macrophage migration inhibitory factor (MIF) is an important mediator that plays a central role in the control of the host immune and inflammatory response. To investigate the molecular mechanism of MIF action, we have used the yeast two-hybrid system and identified PAG, a thiol-specific antioxidant protein, as an interacting partner of MIF. Association of MIF with PAG was found in 293T cells transiently expressing MIF and PAG. The use of PAG mutants (C52S, C71S, and C173S) revealed that this association was significantly affected by C173S, but not C52S and C71S, indicating that a disulfide involving Cys 173 of PAG is responsible for the formation of MIF⅐PAG complex. In addition, the interaction was highly dependent on the reducing conditions such as dithiothreitol or ␤-mercaptoethanol but not in the presence of H 2 O 2 . Analysis of the activities of the interacting proteins showed that the D-dopachrome tautomerase activity of MIF was decreased in a dose-dependent manner by coexpression of wild-type PAG, C52S, and C71S, whereas C173S was almost ineffective, suggesting that the direct interaction may be involved in the control of D-dopachrome tautomerase activity of MIF. Moreover, MIF has been shown to bind to PAG and it also inhibits the antioxidant activity of PAG.

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Human T cell cyclophilin18 binds to thiol-specific antioxidant protein Aop1 and stimulates its activity 1 1Edited by M. Yaniv

Cited by 62 publications

References 47 publications

Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization

Mitochondrial Targeted Cyclophilin D Protects Cells from Cell Death by Peptidyl Prolyl Isomerization

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Regulation of Macrophage Migration Inhibitory Factor and Thiol-specific Antioxidant Protein PAG by Direct Interaction

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