The role of Protein Disulfide Isomerase and thiol bonds modifications in activation of integrin subunit alpha11

Popielarski, Marcin; Ponamarczuk, Halszka; Stasiak, Marta; Michalec, Lidia; Bednarek, Radosław; Studzian, Maciej; Pułaski, Łukasz; Świątkowska, Maria

doi:10.1016/j.bbrc.2017.11.186

Cited by 11 publications

(12 citation statements)

References 25 publications

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“…Cell surface Erythrocytes Kallakunta et al (2013) and Prado et al (2013) Neutrophils Cho (2013) and Hahm et al (2013) Lymphocytes Bi et al (2011), Kroning et al (1994), andTager et al (1997) Macrophages Santos et al (2009) Thyrocytes Couet et al (1996) Platelets Burgess et al (2000) Endothelial cells Popescu et al (2010) Vascular smooth muscle cells Fibroblast Popielarski et al (2018) Leukaemia cells Jang & Hanash (2003) Glioblastoma cells Goplen et al (2006) Extracellular milieu…”

Section: Cells Referencementioning

confidence: 99%

“…Furthermore, reported functions of surface PDI on tumour cells are related to its reducing activity (Popielarski et al, 2018(Popielarski et al, , 2019Tager et al, 1997;Vallon et al, 2012). This may be a consequence of hypoxia such that low oxygen level leads to elevated reducing capacity in the tumour extracellular environment (Loscalzo, 2016).…”

Section: The Redox Activity Of Surface and Extracellular Pdimentioning

confidence: 99%

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Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Chiu

Chen

et al. 2021

British J Pharmacology

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Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyses disulfide bond rearrangement. Initially identified in the endoplasmic reticulum as folding catalysts, PDI and other members in its family have also been widely reported to reside on the cell surface and in the extracellular matrix. Although how PDI is exported and retained on the cell surface remains a subject of debate, this unique pool of PDI is developing into an important mechanism underlying the redox regulation of protein sulfhydryls that are critical for the cellular activities under various disease conditions. This review aims to provide an overview of the pathophysiological roles of surface and extracellular PDI and their underlying molecular mechanisms.Understanding the involvement of extracellular PDI in these diseases will advance our knowledge in the molecular aetiology to facilitate the development of novel pharmacological strategies by specifically targeting PDI in extracellular compartments.

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Section: Cells Referencementioning

confidence: 99%

Section: The Redox Activity Of Surface and Extracellular Pdimentioning

confidence: 99%

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Chiu

Chen

et al. 2021

British J Pharmacology

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“…Cell-surface or secreted PDIs regulate platelet adhesion and thrombosis [ 8 , 9 , 10 ] as well as leukocyte adhesion to endothelium [ 7 ]. PDIs are now known to reside not only in the endoplasmic reticulum (ER), regulating protein folding by forming, breaking and rearranging disulphide bonds [ 11 ]; various PDIs have been detected in other cellular locations, including the surface of platelets, leukocytes, endothelial cells and cancer cells, and they regulate various protein functions by modifying extracellular disulphide bonds [ 6 , 11 , 12 , 13 , 14 , 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

Protein Disulphide Isomerase A1 Is Involved in the Regulation of Breast Cancer Cell Adhesion and Transmigration via Lung Microvascular Endothelial Cells

Stojak

Milczarek

Kurpińska

et al. 2020

Cancers

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Cancer cell cross-talk with the host endothelium plays a crucial role in metastasis, but the underlying mechanisms are still not fully understood. We studied the involvement of protein disulphide isomerase A1 (PDIA1) in human breast cancer cell (MCF-7 and MDA-MB-231) adhesion and transendothelial migration. For comparison, the role of PDIA1 in proliferation, migration, cell cycle and apoptosis was also assessed. Pharmacological inhibitor, bepristat 2a and PDIA1 silencing were used to inhibit PDIA1. Inhibition of PDIA1 by bepristat 2a markedly decreased the adhesion of breast cancer cells to collagen type I, fibronectin and human lung microvascular endothelial cells. Transendothelial migration of breast cancer cells across the endothelial monolayer was also inhibited by bepristat 2a, an effect not associated with changes in ICAM-1 expression or changes in cellular bioenergetics. The silencing of PDIA1 produced less pronounced anti-adhesive effects. However, inhibiting extracellular free thiols by non-penetrating blocker p-chloromercuribenzene sulphonate substantially inhibited adhesion. Using a proteomic approach, we identified that β1 and α2 integrins were the most abundant among all integrins in breast cancer cells as well as in lung microvascular endothelial cells, suggesting that integrins could represent a target for PDIA1. In conclusion, extracellular PDIA1 plays a major role in regulating the adhesion of cancer cells and their transendothelial migration, in addition to regulating cell cycle and caspase 3/7 activation by intracellular PDIA1. PDIA1-dependent regulation of cancer–endothelial cell interactions involves disulphide exchange and most likely integrin activation but is not mediated by the regulation of ICAM-1 expression or changes in cellular bioenergetics in breast cancer or endothelial cells.

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“…Enzymes that redox-modify integrins are PDIs and redoxins, as described for α2β1 (Lahav et al 2003) and αIIbβ3 integrin (Essex and Wu. 2018) on platelets, for α11β1 on fibroblasts (Popielarski et al 2018), and for αMβ2 integrin on neutrophil granulocytes (Hahm et al 2013). Each of the different PDIs plays a non-compensatible role (Essex and Wu.…”

Section: Extracellular Pdis Promote Viral Infections and Toxicitymentioning

confidence: 99%

“…2018), physically interacts with the respective integrin (Essex and Wu. 2018;Popielarski et al 2018), and influences integrin ligand binding positively (Essex and Wu. 2018;Hahm et al 2013) or negatively (Passam et al 2018).…”

Section: Extracellular Pdis Promote Viral Infections and Toxicitymentioning

confidence: 99%

Thiol switches in membrane proteins - Extracellular redox regulation in cell biology

Lorenzen

Eble

Hanschmann

2020

Biological Chemistry

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Redox-mediated signal transduction depends on the enzymatic production of second messengers such as hydrogen peroxide, nitric oxide and hydrogen sulfite, as well as specific, reversible redox modifications of cysteine-residues in proteins. So-called thiol switches induce for instance conformational changes in specific proteins that regulate cellular pathways e.g., cell metabolism, proliferation, migration, gene expression and inflammation. Reduction, oxidation and disulfide isomerization are controlled by oxidoreductases of the thioredoxin family, including thioredoxins, glutaredoxins, peroxiredoxins and protein dsisulfide isomerases. These proteins are located in different cellular compartments, interact with substrates and catalyze specific reactions. Interestingly, some of these proteins are released by cells. Their extracellular functions and generally extracellular redox control have been widely underestimated. Here, we give an insight into extracellular redox signaling, extracellular thiol switches and their regulation by secreted oxidoreductases and thiol-isomerases, a topic whose importance has been scarcely studied so far, likely due to methodological limitations. We focus on the secreted redox proteins and characterized thiol switches in the ectodomains of membrane proteins, such as integrins and the metalloprotease ADAM17, which are among the best-characterized proteins and discuss their underlying mechanisms and biological implications.

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The role of Protein Disulfide Isomerase and thiol bonds modifications in activation of integrin subunit alpha11

Cited by 11 publications

References 25 publications

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Protein Disulphide Isomerase A1 Is Involved in the Regulation of Breast Cancer Cell Adhesion and Transmigration via Lung Microvascular Endothelial Cells

Thiol switches in membrane proteins - Extracellular redox regulation in cell biology

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