Prolyl Hydroxylase, Protein Disulfide Isomerase, and Other Structurally Related Proteins Edited by Norberto Guzman (The R.W. Johnson Pharmaceutical Research Institute). Marcel Dekker, Inc.:  New York, Basel, and Hong Kong. 1998. xvii + 530 pp. $185. ISBN 0-8247-9831-7.

1998 ◽  
Vol 120 (21) ◽  
pp. 5354-5354
Author(s):  
John Bushweller
Keyword(s):  
New York ◽  
Hong Kong ◽  
Protein Disulfide Isomerase ◽  
Pharmaceutical Research ◽  
Prolyl Hydroxylase ◽  
Disulfide Isomerase ◽  
Pharmaceutical Research Institute ◽  
Johnson Pharmaceutical Research ◽  
Related Proteins ◽  
Protein Disulfide

The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase

1992 ◽  
Vol 12 (10) ◽  
pp. 4601-4611
Author(s):  
C Tachibana ◽  
T H Stevens
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Yeast Cells ◽  
Disulfide Isomerase ◽  
Protein Levels ◽  
Growth Defects ◽  
Endoplasmic Reticulum Protein ◽  
Related Proteins ◽  
Protein Disulfide

The product of the EUG1 gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) and the yeast PDI homolog encoded by the essential PDI1 gene. Deletion or overexpression of EUG1 causes no growth defects under a variety of conditions. EUG1 mRNA and protein levels are dramatically increased in response to the accumulation of native or unglycosylated proteins in the endoplasmic reticulum. Overexpression of the EUG1 gene allows yeast cells to grow in the absence of the PDI1 gene product. Depletion of the PDI1 protein in Saccharomyces cerevisiae causes a soluble vacuolar glycoprotein to accumulate in its endoplasmic reticulum form, and this phenotype is only partially relieved by the overexpression of EUG1. Taken together, our results indicate that PDI1 and EUG1 encode functionally related proteins that are likely to be involved in interacting with nascent polypeptides in the yeast endoplasmic reticulum.

scholarly journals The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase.

1992 ◽  
Vol 12 (10) ◽  
pp. 4601-4611 ◽  
Author(s):  
C Tachibana ◽  
T H Stevens
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Yeast Cells ◽  
Disulfide Isomerase ◽  
Protein Levels ◽  
Growth Defects ◽  
Endoplasmic Reticulum Protein ◽  
Related Proteins ◽  
Protein Disulfide

The product of the EUG1 gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) and the yeast PDI homolog encoded by the essential PDI1 gene. Deletion or overexpression of EUG1 causes no growth defects under a variety of conditions. EUG1 mRNA and protein levels are dramatically increased in response to the accumulation of native or unglycosylated proteins in the endoplasmic reticulum. Overexpression of the EUG1 gene allows yeast cells to grow in the absence of the PDI1 gene product. Depletion of the PDI1 protein in Saccharomyces cerevisiae causes a soluble vacuolar glycoprotein to accumulate in its endoplasmic reticulum form, and this phenotype is only partially relieved by the overexpression of EUG1. Taken together, our results indicate that PDI1 and EUG1 encode functionally related proteins that are likely to be involved in interacting with nascent polypeptides in the yeast endoplasmic reticulum.

scholarly journals Silibinin Ameliorates O-GlcNAcylation and Inflammation in a Mouse Model of Nonalcoholic Steatohepatitis

2018 ◽  
Vol 19 (8) ◽  
pp. 2165 ◽  
Author(s):  
Su Lee ◽  
Min Nam ◽  
Da Lee ◽  
Jeen-Woo Park ◽  
Beom Kang ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Protein Disulfide Isomerase ◽  
Therapeutic Agent ◽  
Hepatic Inflammation ◽  
Disulfide Isomerase ◽  
Nash Model ◽  
Comparative Proteomic Analysis ◽  
Related Proteins ◽  
Protein Disulfide ◽  
Promising Therapeutic Agent

The mechanisms underlying the progression to non-alcoholic steatohepatitis (NASH) remain to be elucidated. In the present study, we aimed to identify the proteins involved in the pathogenesis of liver tissue inflammation and to investigate the effects of silibinin, a natural polyphenolic flavonoid, on steatohepatitis. We performed comparative proteomic analysis using methionine and choline-deficient (MCD) diet-induced NASH model mice. Eighteen proteins were identified from the two-dimensional proteomic analysis, which are not only differentially expressed, but also significantly improved, by silibinin treatment. Interestingly, seven of these proteins, including keratin cytoskeletal 8 and 18, peroxiredoxin-4, and protein disulfide isomerase, are known to undergo GlcNAcylation modification, most of which are related to structural and stress-related proteins in NASH model animals. Thus, we primarily focused on how the GlcNAc modification of these proteins is involved in the progression to NASH. Remarkably, silibinin treatment alleviates the severity of hepatic inflammation along with O-GlcNAcylation in steatohepatitis. In particular, the reduction of inflammation by silibinin is due to the inhibition of the O-GlcNAcylation-dependent NF-κB-signaling pathway. Therefore, silibinin is a promising therapeutic agent for hyper-O-GlcNAcylation as well as NASH.

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