scholarly journals Arabidopsis Protein Disulfide Isomerase-5 Inhibits Cysteine Proteases during Trafficking to Vacuoles before Programmed Cell Death of the Endothelium in Developing Seeds

2008 ◽  
Vol 20 (8) ◽  
pp. 2205-2220 ◽  
Author(s):  
Christine Andème Ondzighi ◽  
David A. Christopher ◽  
Eun Ju Cho ◽  
Shu-Choeng Chang ◽  
L. Andrew Staehelin
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Protein Disulfide Isomerase ◽  
Cysteine Proteases ◽  
Disulfide Isomerase ◽  
Developing Seeds ◽  
Arabidopsis Protein ◽  
Protein Disulfide

scholarly journals Identification and Characterization of a Novel Protein Disulfide Isomerase Gene (MgPDI2) from Meloidogyne graminicola

2020 ◽  
Vol 21 (24) ◽  
pp. 9586
Author(s):  
Zhongling Tian ◽  
Zehua Wang ◽  
Maria Munawar ◽  
Jingwu Zheng
Keyword(s):  
Cell Death ◽  
Protein Disulfide Isomerase ◽  
Catalytic Domain ◽  
Root Knot Nematode ◽  
Transient Expression Assay ◽  
Disulfide Isomerase ◽  
Meloidogyne Graminicola ◽  
Promising Target ◽  
Nematode Parasitism ◽  
Protein Disulfide

Protein disulfide isomerase (PDI) is a multifunctional enzyme that catalyzes rate-limiting reactions such as disulfide bond formation, isomerization, and reduction. There is some evidence that indicates that PDI is also involved in host-pathogen interactions in plants. In this study, we show that the rice root-knot nematode, Meloidogyne graminicola, has evolved a secreted effector, MgPDI2, which is expressed in the subventral esophageal glands and up-regulated during the early parasitic stage of M. graminicola. Purified recombinant MgPDI2 functions as an insulin disulfide reductase and protects plasmid DNA from nicking. As an effector, MgPDI2 contributes to nematode parasitism. Silencing of MgPDI2 by RNA interference in the pre-parasitic second-stage juveniles (J2s) reduced M. graminicola multiplication and also increased M. graminicola mortality under H2O2 stress. In addition, an Agrobacterium-mediated transient expression assay found that MgPDI2 caused noticeable cell death in Nicotiana benthamiana. An intact C-terminal region containing the first catalytic domain (a) with an active motif (Cys-Gly-His-Cys, CGHC) and the two non-active domains (b and b′) is required for cell death induction in N. benthamiana. This research may provide a promising target for the development of new strategies to combat M. graminicola infections.

Involvement of protein disulfide isomerase in subtilase cytotoxin-induced cell death in HeLa cells

2020 ◽  
Vol 525 (4) ◽  
pp. 1068-1073 ◽  
Author(s):  
Hiroyasu Tsutsuki ◽  
Tianli Zhang ◽  
Ayaka Harada ◽  
Azizur Rahman ◽  
Katsuhiko Ono ◽  
...  
Keyword(s):  
Cell Death ◽  
Hela Cells ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Subtilase Cytotoxin

scholarly journals Role of Transglutaminase 2 in Cell Death, Survival, and Fibrosis

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1842
Author(s):  
Hideki Tatsukawa ◽  
Kiyotaka Hitomi
Keyword(s):  
Cell Death ◽  
Protein Disulfide Isomerase ◽  
Tissue Repair ◽  
Transglutaminase 2 ◽  
Cell Type ◽  
Disulfide Isomerase ◽  
Open Conformation ◽  
Splicing Variants ◽  
Protein Disulfide

Transglutaminase 2 (TG2) is a ubiquitously expressed enzyme catalyzing the crosslinking between Gln and Lys residues and involved in various pathophysiological events. Besides this crosslinking activity, TG2 functions as a deamidase, GTPase, isopeptidase, adapter/scaffold, protein disulfide isomerase, and kinase. It also plays a role in the regulation of hypusination and serotonylation. Through these activities, TG2 is involved in cell growth, differentiation, cell death, inflammation, tissue repair, and fibrosis. Depending on the cell type and stimulus, TG2 changes its subcellular localization and biological activity, leading to cell death or survival. In normal unstressed cells, intracellular TG2 exhibits a GTP-bound closed conformation, exerting prosurvival functions. However, upon cell stimulation with Ca2+ or other factors, TG2 adopts a Ca2+-bound open conformation, demonstrating a transamidase activity involved in cell death or survival. These functional discrepancies of TG2 open form might be caused by its multifunctional nature, the existence of splicing variants, the cell type and stimulus, and the genetic backgrounds and variations of the mouse models used. TG2 is also involved in the phagocytosis of dead cells by macrophages and in fibrosis during tissue repair. Here, we summarize and discuss the multifunctional and controversial roles of TG2, focusing on cell death/survival and fibrosis.

Sign in / Sign up

Export Citation Format

Share Document