Induction of expression of protein disulphide‐isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide

Paver, Jan L.; Freedman, Robert B.; Michael, R.; Parkhouse, R. M. E.

doi:10.1016/0014-5793(89)80501-0

Cited by 14 publications

(9 citation statements)

References 29 publications

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“…The expression of Trx and PDI is known to be induced by various stimuli including oxidative stresses (24,25), cytokines (26), lipopolysaccharide (27,28) and hormones (29,30). In contrast, there are only a few reports documenting the effect of estrogens on the expression of the protein thiol/disulfide oxidoreductases.…”

Section: Discussionmentioning

confidence: 99%

17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress

Ejima

Nanri

Araki

et al. 1999

European Journal of Endocrinology

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Objective: To examine whether or not estrogens induced the expression of protein thiol/disulfide oxidoreductases such as protein disulfide isomerase (PDI), thioredoxin (Trx), Trx reductase, and glutaredoxin (Grx) in vascular endothelial cells. Methods:The regenerative effects of the protein thiol/disulfide oxidoreductases, PDI, Trx and Grx, on oxidatively damaged proteins were assayed using H 2 O 2 -inactivated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a reporter enzyme. The induction of protein thiol/disulfide oxidoreductases and the accumulation of protein adducts generated by lipid peroxidation were examined by Western blotting in estrogen-treated bovine aortic endothelial cells (BAECs). Results: Reduced PDI, Trx and Grx regenerated the H 2 O 2 -inactivated GAPDH in vitro. The levels of these protein disulfide oxidoreductases in BAECs were increased by pretreatment with 0.01-10 mmol/l 17b-estradiol, the largest increase (about fourfold of the control) being found for PDI. Other sex hormones such as progesterone and testosterone did not affect the contents of these oxidoreductases in BAECs. 4-Hydroxy-2-nonenal (HNE)-protein adducts, which are generated by lipid peroxidation, were accumulated in BAECs exposed to paraquat, whereas the pretreatment of BAECs with 17b-estradiol suppressed their accumulation. Conclusions:The estrogen-mediated induction of the protein thiol/disulfide oxidoreductases such as PDI, Trx, Trx reductase and Grx suggested a possible involvement of these oxidoreductases in the antioxidant protection of estrogen observed in the vascular system.

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Section: Discussionmentioning

confidence: 99%

17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress

Ejima

Nanri

Araki

et al. 1999

European Journal of Endocrinology

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“…merase (PDI)-related protein for which the structures of all domains have been determined [60]. PDI expression is induced by LPS in splenic B cells and BCL1 cells [61], and its up-regulation renders protection against apoptotic cell death [62]. However, unlike ERP60, ERP29 does not seem to exhibit PDI activity [42,60].…”

Section: Proteins With Reduced Intensity During Lps-induced Apoptosismentioning

confidence: 99%

Proteomic analysis of lipopolysaccharide-induced apoptosis in PC12 cells

et al. 2002

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We employed rat pheochromocytoma PC12 cells as our model system to identify cellular proteins that accompany Escherichia coli lipopolysaccharide (LPS)-induced apoptosis, based on a proteomic approach. Cell viability tests revealed that naïve PC12 cells underwent cell death in a dose-dependent manner after treatment with LPS. Flow cytometric analysis confirmed that apoptosis was primarily responsible for the observed cell death. Two-dimensional electrophoresis in conjunction with N-terminal sequencing, immunoblot, matrix-assisted laser desorption/ionization-time of flight analysis or computer matching with protein databases further revealed that the LPS-induced apoptosis is accompanied by an augmented level of calreticulin, calcium binding protein 50, endoplasmic reticulum protein 60 (ERP60), heat shock protein 60 (HSP60) or HSP90, and a reduced level of amphoterin, cytochrome c oxidase polypeptide VIa-liver or ERP29. These proteins are associated with endoplasmic reticulum, mitochondria or cell membrane, and are with known or potential roles in apoptosis. Their identification therefore provides an impetus for further delineation of the cellular and molecular basis of apoptotic cell death and sepsis based on proteomic profiling of PC12 cells.

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“…Microsomes were reconstituted with purified PDI as described by Bulleid and Freedman (1988a). ELISA Protein disulphide isomerase was quantitated in microsomal preparations by ELISA as outlined by Paver et al (1989b) using purified bovine PDI as standard.…”

Section: Methodsmentioning

confidence: 99%

Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase.

Bulleid

Freedman

1990

The EMBO Journal

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The role of protein disulphide isomerase (PDI) and other resident proteins of the endoplasmic reticulum (ER) lumen in co‐ and post‐translational modification of secretory proteins has been studied in experiments on translation in vitro. We have devised procedures for extracting the lumenal content proteins of dog pancreas microsomal vesicles by alkaline buffer, or detergent washing, and for reconstitution of the depleted membrane fraction. When microsomal membranes are depleted of content by washing at pH 9.1, they are able to co‐translationally glycosylate human interferon‐gamma (IFN‐gamma) and yeast pro‐alpha‐factor and the products appear to be identical to those produced by control microsomes. However, when microsomal membranes are depleted of content by washing with saponin they are still able to co‐translationally translocate and glycosylate human IFN‐gamma, but the products were of higher apparent Mr than those generated by control microsomes. When saponin‐washed microsomal membranes were reconstituted with homogeneous protein disulphide isomerase (PDI), the generated vesicles gave the same pattern of co‐translationally glycosylated IFN‐gamma as saponin‐washed microsomal membranes lacking PDI. These results are discussed in relation to the roles of resident ER proteins in co‐translational modification; they suggest that PDI is not an essential component of the machinery of co‐translational N‐glycosylation, but that detergent washing may inactivate or remove some ER glycosidases.

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Induction of expression of protein disulphide‐isomerase during lymphocyte maturation stimulated by bacterial lipopolysaccharide

Cited by 14 publications

References 29 publications

17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress

17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress

Proteomic analysis of lipopolysaccharide-induced apoptosis in PC12 cells

Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase.

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