Changes of endoplasmic reticulum chaperone complexes, redox state, and impaired protein disulfide reductase activity in misfolding αi‐antitrypsin transgenic mice

2006 ◽  
Vol 20 (7) ◽  
pp. 1018-1020 ◽  
Author(s):  
Eszter Papp ◽  
Péter Száiraz ◽  
Tamás Korcsmáiros ◽  
Peter Csermely ◽  
Eszter Papp ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Transgenic Mice ◽  
Redox State ◽  
Reductase Activity ◽  
Disulfide Reductase ◽  
Endoplasmic Reticulum Chaperone ◽  
Protein Disulfide

scholarly journals The Archaeon Methanosarcina acetivorans Contains a Protein Disulfide Reductase with an Iron-Sulfur Cluster

2007 ◽  
Vol 189 (20) ◽  
pp. 7475-7484 ◽  
Author(s):  
Daniel J. Lessner ◽  
James G. Ferry
Keyword(s):  
Aromatic Compounds ◽  
Stress Proteins ◽  
Reductase Activity ◽  
Strictly Anaerobic ◽  
Methanosarcina Acetivorans ◽  
Gene Encoding ◽  
Iron Sulfur Cluster ◽  
Disulfide Reductase ◽  
Regulate Protein ◽  
Protein Disulfide

ABSTRACT Methanosarcina acetivorans, a strictly anaerobic methane-producing species belonging to the domain Archaea, contains a gene cluster annotated with homologs encoding oxidative stress proteins. One of the genes (MA3736) is annotated as a gene encoding an uncharacterized carboxymuconolactone decarboxylase, an enzyme required for aerobic growth with aromatic compounds by species in the domain Bacteria. Methane-producing species are not known to utilize aromatic compounds, suggesting that MA3736 is incorrectly annotated. The product of MA3736, overproduced in Escherichia coli, had protein disulfide reductase activity dependent on a C67XXC70 motif not found in carboxymuconolactone decarboxylase. We propose that MA3736 be renamed mdrA (methanosarcina disulfide reductase). Further, unlike carboxymuconolactone decarboxylase, MdrA contained an Fe-S cluster. Binding of the Fe-S cluster was dependent on essential cysteines C67 and C70, while cysteines C39 and C107 were not required. Loss of the Fe-S cluster resulted in conversion of MdrA from an inactive hexamer to a trimer with protein disulfide reductase activity. The data suggest that MdrA is the prototype of a previously unrecognized protein disulfide reductase family which contains an intermolecular Fe-S cluster that controls oligomerization as a mechanism to regulate protein disulfide reductase activity.

Structural and Biochemical Characterizations of Methanoredoxin fromMethanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity

Biochemistry ◽  
2015 ◽  
Vol 55 (2) ◽  
pp. 313-321 ◽  
Author(s):  
Deepa Yenugudhati ◽  
Divya Prakash ◽  
Adepu K. Kumar ◽  
R. Siva Sai Kumar ◽  
Neela H. Yennawar ◽  
...  
Keyword(s):  
Reductase Activity ◽  
Coenzyme M ◽  
Disulfide Reductase ◽  
Dependent Protein ◽  
Protein Disulfide

scholarly journals Alterations of the Platelet Proteome in Lung Cancer: Accelerated F13A1 and ER Processing as New Actors in Hypercoagulability

Cancers ◽  
2021 ◽  
Vol 13 (9) ◽  
pp. 2260
Author(s):  
Huriye Ercan ◽  
Lisa-Marie Mauracher ◽  
Ella Grilz ◽  
Lena Hell ◽  
Roland Hellinger ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Endoplasmic Reticulum ◽  
Brain Cancer ◽  
Lung Cancer Patients ◽  
Differential Behaviour ◽  
Endoplasmic Reticulum Chaperone ◽  
Platelet Proteome ◽  
Altered Proteins ◽  
Related Proteins ◽  
Protein Disulfide

In order to comprehensively expose cancer-related biochemical changes, we compared the platelet proteome of two types of cancer with a high risk of thrombosis (22 patients with brain cancer, 19 with lung cancer) to 41 matched healthy controls using unbiased two-dimensional differential in-gel electrophoresis. The examined platelet proteome was unchanged in patients with brain cancer, but considerably affected in lung cancer with 15 significantly altered proteins. Amongst these, the endoplasmic reticulum (ER) proteins calreticulin (CALR), endoplasmic reticulum chaperone BiP (HSPA5) and protein disulfide-isomerase (P4HB) were significantly elevated. Accelerated conversion of the fibrin stabilising factor XIII was detected in platelets of patients with lung cancer by elevated levels of a F13A1 55 kDa fragment. A significant correlation of this F13A1 cleavage product with plasma levels of the plasmin–α-2-antiplasmin complex and D-dimer suggests its enhanced degradation by the fibrinolytic system. Protein association network analysis showed that lung cancer-related proteins were involved in platelet degranulation and upregulated ER protein processing. As a possible outcome, plasma FVIII, an immediate end product for ER-mediated glycosylation, correlated significantly with the ER-executing chaperones CALR and HSPA5. These new data on the differential behaviour of platelets in various cancers revealed F13A1 and ER chaperones as potential novel diagnostic and therapeutic targets in lung cancer patients.

scholarly journals Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm

Animals ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 3487
Author(s):  
Katarzyna Dyrda ◽  
Aleksandra Orzołek ◽  
Joanna Ner-Kluza ◽  
Paweł Wysocki
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Maturation Process ◽  
Epididymal Sperm ◽  
Post Translational Modifications ◽  
Disulfide Isomerase ◽  
Sperm Proteins ◽  
Epididymal Maturation ◽  
Endoplasmic Reticulum Chaperone ◽  
Protein Disulfide

Epididymal maturation can be defined as a scope of changes occurring during epididymal transit that prepare spermatozoa to undergo capacitation. One of the most common post-translational modifications involved in the sperm maturation process and their ability to fertilise an oocyte is the phosphorylation of sperm proteins. The aim of this study was to compare tyrosine, serine, and threonine phosphorylation patterns of sperm proteins isolated from three subsequent segments of the stallion epididymis, during and out of the breeding season. Intensities of phosphorylation signals and phosphoproteins profiles varied in consecutive regions of the epididymis. However, significant differences in the phosphorylation status were demonstrated in case of endoplasmic reticulum chaperone BiP (75 and 32 kDa), protein disulfide-isomerase A3 (50 kDa), nesprin-1 (23 kDa), peroxiredoxin-5 (17 kDa), and protein bicaudal D homolog (15 kDa) for season x type of phosphorylated residues variables. Significant differences in the phosphorylation status were also demonstrated in case of endoplasmic reticulum chaperone BiP and albumin (61 kDa), protein disulfide-isomerase A3 (50 kDa), and protein bicaudal D homolog (15 kDa) for region x type of phosphorylated residues variables.

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