ERp57 interacts with conserved cysteine residues in the MHC class I peptide‐binding groove

Antoniou, Antony N.; Santos, Susana G.; Campbell, Elaine C.; Lynch, Sarah; Arosa, Fernando A.; Powis, Simon J.

doi:10.1016/j.febslet.2007.04.034

Cited by 12 publications

(5 citation statements)

References 23 publications

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“…1a,c). Studies by others have also detected ERp57-MHC class I disulfide-bonded dimers, and implicated ERp57 in the reduction of sub-optimally folded MHC class I prior to its degradation [15,16,17]. In support of this hypothesis, our findings show that the level of the ERp57-D b conjugate (not including tapasin) is enhanced by the absence of β 2 m, likely due to hampered D b folding.…”

Section: Resultssupporting

confidence: 87%

Impact of beta 2-microglobulin on tapasin expression and covalent association

Simone

Smith

Solheim

2012

Cellular Immunology

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Cellular immunity is dependent on major histocompatibility complex (MHC) class I molecules enabling cytotoxic T cell recognition of malignant and infected cells. Loading of antigenic peptides onto MHC class I is assisted by a peptide-loading protein complex including tapasin. We found that tapasin expression is enhanced by beta 2-microglobulin via both transcriptional and post-transcriptional mechanisms. In addition, using conditions which preserve the tapasin-ERp57 disulfide-bonded conjugate, we demonstrated that beta 2-microglobulin increases tapasin-containing protein complexes, and reduces the level of MHC class I/ERp57 complexes lacking tapasin. Overall, our results provide a new perspective on the regulation of tapasin expression and association.

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Section: Resultssupporting

confidence: 87%

Impact of beta 2-microglobulin on tapasin expression and covalent association

Simone

Smith

Solheim

2012

Cellular Immunology

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“…ERp57 is covalently associated with the chaperone tapasin in the peptide‐loading complex, and participates in the stabilization of empty MHC class I molecules and in the selective loading of high‐affinity peptides 43. Antoniou et al 44 discovered that ERp57 had a direct access to the peptide‐binding groove of MHC class I molecules during assembly. MHC class I molecules bind and present short peptides to CD8 + T lymphocytes, enabling the detection and elimination of infected cells.…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of colonic mucosa in a rat model of irritable bowel syndrome

Ding¹,

Lü²,

Chen³

et al. 2010

Proteomics

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Irritable bowel syndrome (IBS) is one of the most common functional disorders of the gastrointestinal tract. It is characterized by abdominal pain and changes in bowel habits. Various studies have investigated the pathophysiologic processes underlying IBS, but the mechanism remains poorly understood. In the present study, we established an IBS model and identified differentially expressed proteins in colon tissue of IBS rats compared with healthy controls by 2-D gel electrophoresis, MALDI-TOF-MS, and Western blot analysis. Our results showed that 13 of the 1396 protein spots on 2-D gel were differently expressed between the IBS and control groups. Ontological analysis of these proteins revealed primary roles in catalytic activity (protein disulfide-isomerase A3, glyoxalase I, cathepsin S, alpha-enolase), structural support (cytokeratin 8), antioxidant activity (peroxiredoxin-6), protein binding (transgelin, serpin peptidase inhibitor B5), and signal transduction (40S ribosomal protein SA). Protein disulfide-isomerase A3 and cytokeratin 8 overexpression in IBS were confirmed by Western blot. The findings indicate that multiple proteins are involved in IBS processes that influence intestinal tract immunity, inflammation, and nerve regulation. Our study provides useful candidate genes and proteins for further investigation.

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“…Recent studies have found that PDIA3 plays an important role in endogenous antigen presentation. Antoniou et al (2007) reported that PDIA3 molecules can directly insert into the peptide binding groove of the MHC class I molecules to bind with them during the course of MHC molecules antigen-presenting, making the antigen binding groove more bindable for antigen peptides (Santos et al, 2007; Stepensky, Bangia & Cresswell, 2007), resulting in increased binding stability between MHC molecules and antigen peptides.…”

Section: Discussionmentioning

confidence: 99%

PDIA3 gene induces visceral hypersensitivity in rats with irritable bowel syndrome through the dendritic cell-mediated activation of T cells

Zhuang

Zhang

Wang

et al. 2016

PeerJ

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This study investigated the mechanism of protein disulfide-isomerase A3 (PDIA3)-induced visceral hypersensitivity in irritable bowel syndrome (IBS). Rats were treated with saline (control), acetic acid and restraint stress (IBS model), empty vector (RNAi control) and PDIA3-RNAi vector (PDIA3-RNAi). Mesenteric lymph node DCs (MLNDCs) and splenic CD4+/CD8+ T cells were isolated for co-cultivation. Compared with control, MLNDCs co-cultured with CD4+ or CD8+ T cells showed an increased ability to promote T cell proliferation and produced more IL-4 or IL-9 secretion. Compared with the RNAi control, MLNDCs from the PDIA3 knockdown models were less effective in promoting the proliferation of CD4+/CD8+ T cells. It is concluded that PDIA3 plays an important role in the development of IBS through the DC-mediated activation of T cells, resulting in degranulation of MCs and visceral hypersensitivity.

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ERp57 interacts with conserved cysteine residues in the MHC class I peptide‐binding groove

Cited by 12 publications

References 23 publications

Impact of beta 2-microglobulin on tapasin expression and covalent association

Impact of beta 2-microglobulin on tapasin expression and covalent association

Proteomic analysis of colonic mucosa in a rat model of irritable bowel syndrome

PDIA3 gene induces visceral hypersensitivity in rats with irritable bowel syndrome through the dendritic cell-mediated activation of T cells

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