Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation

FEBS Letters ◽  
1997 ◽  
Vol 406 (3) ◽  
pp. 291-295 ◽  
Author(s):  
Jörg Volkmer ◽  
Silvia Guth ◽  
Wolfgang Nastainczyk ◽  
Peter Knippel ◽  
Peter Klappa ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Specific Protein ◽  
Secretory Proteins ◽  
Disulfide Isomerase ◽  
Transient Contact ◽  
Protein Disulfide ◽  
Late Stages

scholarly journals Localisation and expression of a testis‐specific protein disulfide isomerase, PDILT

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Marcel Van Lith ◽  
Dave Bown ◽  
John Gatehouse ◽  
Adam M Benham
Keyword(s):  
Protein Disulfide Isomerase ◽  
Specific Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals PDI Family Members as Guides for Client Folding and Assembly

2020 ◽  
Vol 21 (24) ◽  
pp. 9351
Author(s):  
Shingo Kanemura ◽  
Motonori Matsusaki ◽  
Kenji Inaba ◽  
Masaki Okumura
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Viability ◽  
Molecular Chaperones ◽  
Protein Disulfide Isomerase ◽  
Family Members ◽  
Secretory Proteins ◽  
Efficient Production ◽  
Protein Homeostasis ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins.

scholarly journals Functional Relationship between Protein Disulfide Isomerase Family Members during the Oxidative Folding of Human Secretory Proteins

2010 ◽  
Vol 21 (18) ◽  
pp. 3093-3105 ◽  
Author(s):  
Lori A. Rutkevich ◽  
Myrna F. Cohen-Doyle ◽  
Ulf Brockmeier ◽  
David B. Williams
Keyword(s):  
Protein Disulfide Isomerase ◽  
High Efficiency ◽  
Family Members ◽  
Secretory Proteins ◽  
Human Hepatoma Cells ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
The Impact ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

To examine the relationship between protein disulfide isomerase family members within the mammalian endoplasmic reticulum, PDI, ERp57, ERp72, and P5 were depleted with high efficiency in human hepatoma cells, either singly or in combination. The impact was assessed on the oxidative folding of several well-characterized secretory proteins. We show that PDI plays a predominant role in oxidative folding because its depletion delayed disulfide formation in all secretory proteins tested. However, the phenotype was surprisingly modest suggesting that other family members are able to compensate for PDI depletion, albeit with reduced efficacy. ERp57 also exhibited broad specificity, overlapping with that of PDI, but with preference for glycosylated substrates. Depletion of both PDI and ERp57 revealed that some substrates require both enzymes for optimal folding and, furthermore, led to generalized protein misfolding, impaired export from the ER, and degradation. In contrast, depletion of ERp72 or P5, either alone or in combination with PDI or ERp57 had minimal impact, revealing a narrow substrate specificity for ERp72 and no detectable role for P5 in oxidative protein folding.

scholarly journals Characterization of a Foldase, Protein Disulfide Isomerase A, in the Protein Secretory Pathway ofAspergillus niger

2000 ◽  
Vol 66 (2) ◽  
pp. 775-782 ◽  
Author(s):  
Celina Ngiam ◽  
David J. Jeenes ◽  
Peter J. Punt ◽  
Cees A. M. J. J. Van Den Hondel ◽  
David B. Archer
Keyword(s):  
Protein Disulfide Isomerase ◽  
Secretory Pathway ◽  
Functional Characterization ◽  
Killer Toxin ◽  
Rnase A ◽  
Secretory Proteins ◽  
Mrna Levels ◽  
Western Blots ◽  
Disulfide Isomerase ◽  
Protein Disulfide

ABSTRACT Protein disulfide isomerase (PDI) is important in assisting the folding and maturation of secretory proteins in eukaryotes. A gene,pdiA, encoding PDIA was previously isolated fromAspergillus niger, and we report its functional characterization here. Functional analysis of PDIA showed that it catalyzes the refolding of denatured and reduced RNase A.pdiA also complemented PDI function in aSaccharomyces cerevisiae Δpdi1 mutant in a yeast-based killer toxin assay. Levels of pdiA mRNA and PDIA protein were raised by the accumulation of unfolded proteins in the endoplasmic reticulum. This response of pdiA mRNA levels was slower and lower in magnitude than that of A. niger bipA, suggesting that the induction of pdiA is not part of the primary stress response. An increased level of pdiA transcripts was also observed in two A. niger strains overproducing a heterologous protein, hen egg white lysozyme (HEWL). Although overexpression of PDI has been successful in increasing yields of some heterologous proteins in S. cerevisiae, overexpression of PDIA did not increase secreted yields of HEWL in A. niger, suggesting that PDIA itself is not limiting for secretion of this protein. Downregulation of pdiA by antisense mRNA reduced the levels of microsomal PDIA activity by up to 50%, lowered the level of PDIA as judged by Western blots, and lowered the secreted levels of glucoamylase by 60 to 70%.

scholarly journals Identification of the physiological substrates of PDIp, a pancreas-specific protein-disulfide isomerase family member

2018 ◽  
Vol 293 (48) ◽  
pp. 18421-18433 ◽  
Author(s):  
Takushi Fujimoto ◽  
Orie Nakamura ◽  
Michiko Saito ◽  
Akio Tsuru ◽  
Masaki Matsumoto ◽  
...  
Keyword(s):  
Family Member ◽  
Protein Disulfide Isomerase ◽  
Specific Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family ◽  
Physiological Substrates

scholarly journals Distribution of protein disulfide isomerase in rat epiphyseal chondrocytes.

1989 ◽  
Vol 37 (12) ◽  
pp. 1835-1844 ◽  
Author(s):  
S Akagi ◽  
A Yamamoto ◽  
T Yoshimori ◽  
R Masaki ◽  
R Ogawa ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Protein A ◽  
Secretory Proteins ◽  
Disulfide Isomerase ◽  
Gold Particles ◽  
Golgi Compartment ◽  
Preferential Binding ◽  
Protein Disulfide

We investigated the intracellular distribution of protein disulfide isomerase (PDI) in rat epiphyseal chondrocytes by immunocytochemistry, using a post-embedding protein A-gold technique. Gold particles were localized primarily in the cisternal space of the rough endoplasmic reticulum (ER) and nuclear envelopes. The ER cisternae of the chondrocytes in all the differentiating epiphyseal zones--resting, proliferative, pre-hypertrophic, and hypertrophic--were equally and highly labeled. The labeling density of the cisternal space of the dilated ER, probably reflecting marked accumulation of secretory proteins such as procollagen, was always higher than that of the non-dilated ER. In the dilated cisternal space, gold particles were freely and evenly distributed, without preferential binding to the luminal surface of the ER membranes. We suggest that PDI catalyzes the formation of disulfide bonds of various secretory proteins, perhaps type II procollagen, in the cisternal space of the ER in epiphyseal chondrocytes. The exclusive localization of gold particles in the cisternal space of the ER and nuclear envelopes and the lack of gold particles in the Golgi apparatus, including cis-Golgi cisternae, indicate that PDI is an ER-soluble protein in the chondrocytes and is presumably sorted out in some pre-Golgi compartment and not transported to the Golgi apparatus.

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