Beta 3 Integrin Expression on T Cells From Renal Allograft Recipients

Wierzbicki, Piotr; Kłosowska, D; Wyzgał, Janusz; Nowaczyk, M; Przerwa, Anna; Kniotek, Monika; Górski, Andrzej

doi:10.1016/j.transproceed.2005.12.009

Cited by 8 publications

(5 citation statements)

References 6 publications

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“…β3 integrins regulate platelet adhesion; β3 is also known as CD61, and on platelets, PDI reduces disulfide bonds in CD61 to promote binding to ligands (7,28). CD61 expression has also been reported on specific T-cell subsets (30)(31)(32)(33)(34). We confirmed that PhaRST6 and primary Th2 cells express cell surface CD61 ( Fig.…”

Section: Pdi-associated Cd61 Promotes T-cell Migration Enhanced Bysupporting

confidence: 79%

Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry

Bi¹,

Hong

Lee

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

212

215

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Interaction of cell surface glycoproteins with endogenous lectins on the cell surface regulates formation and maintenance of plasma membrane domains, clusters signaling complexes, and controls the residency time of glycoproteins on the plasma membrane. Galectin-9 is a soluble, secreted lectin that binds to glycoprotein receptors to form galectin-glycoprotein lattices on the cell surface. Whereas galectin-9 binding to specific glycoprotein receptors induces death of CD4 Th1 cells, CD4 Th2 cells are resistant to galectin-9 death due to alternative glycosylation. On Th2 cells, galectin-9 binds cell surface protein disulfide isomerase (PDI), increasing retention of PDI on the cell surface and altering the redox status at the plasma membrane. Cell surface PDI regulates integrin function on platelets and also enhances susceptibility of T cells to infection with HIV. We find that galectin-9 binding to PDI on Th2 cells results in increased cell migration through extracellular matrix via β3 integrins, identifying a unique mechanism to regulate T-cell migration. In addition, galectin-9 binding to PDI on T cells potentiates infection with HIV. We identify a mechanism for regulating cell surface redox status via a galectin-glycoprotein lattice, to regulate distinct T-cell functions.

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Section: Pdi-associated Cd61 Promotes T-cell Migration Enhanced Bysupporting

confidence: 79%

Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry

Bi¹,

Hong

Lee

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

212

215

View full text Add to dashboard Cite

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“…Also regulates dendritic cell differentiation and Toll receptor signalling (Chorny et al, 2006;Arranz et al, 2008) Miscellaneous DDX17 NP_001091974.1| DEAD (Asp-Glu-Ala-Asp) box polypeptide 17 P72: cross-reacts with the murine leukaemia virus p15-gag antigen (Rucheton et al, 1992) Regulates oestrogen receptor alpha transcription (Wortham et al, 2009). Oestrogens play an important role in T lymphocyte function and inflammation (Weitzmann & Pacifici, 2005;Arnal et al, 2009;Wortham et al, 2009) ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61 cross-reactive antibodies between HIV-gp120 and CD61 (Bettaieb et al, 1996) Expressed in dendritic cells and involved in the clearance of apoptotic cells and immune tolerance (Parcina et al, 2009): also expressed on T cells (Wierzbicki et al, 2006) MBP myelin basic protein NP_001020252 Intrathecal autoantibodies (Maimone et al, 1994) Primary constituent of myelin SERPINA1 alpha(1) proteinase inhibitor [alpha(1)PI; alpha(1) antitrypsin] (Bristow et al, 2001) Serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin and plasminogen activator (RefSeq). Also a potent anti-inflammatory agent (Janciauskiene et al, 2007) SNRPB small nuclear ribonucleoprotein polypeptides B and B1: cross-reactive with the p24 gag protein of HIV-1 (De Keyser et al, 1992) Involved in pre-mRNA splicing and the encoded protein may also play a role in pre-mRNA splicing or snRNP structure.…”

Section: Autoantigens and Reference Functionmentioning

confidence: 99%

Extensive viral mimicry of 22 AIDS-related autoantigens by HIV-1 proteins and pathway analysis of 561 viral/human homologues suggest an initial treatable autoimmune component of AIDS

Carter

2011

FEMS Immunol Med Microbiol

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HIV-1 viral proteins, particularly the env protein, are homologous to 22 AIDS autoantigens, suggesting their creation by antiviral antibodies subsequently targeting human homologues. They include antibodies to T-cell receptors, CD4 and CD95, complement components, IgG, TNF and other immune-related proteins. Autoantibodies may compromise the immune system via knockdown of these key proteins, and autoimmune attack on the immune system itself, as supported by immune activation in early stages of infection and during the transition to AIDS. Over 500 human proteins contain pentapeptides or longer consensi, identical to viral peptides. Such homology explains the extensive viral/human interactome, likely related to the ability of viral homologues to compete with human counterparts as binding partners. Pathway analysis of these homologous proteins revealed their involvement in immune-related networks (e.g. natural killer cell toxicity/toll, T-cell/B-cell receptor signalling/antigen processing) and viral and bacterial entry and defence pathways (phagosome/lysosome pathways, DNA sensing/NOD/RIG-1 pathways) relevant to AIDS pathogenesis. At its inception, AIDS may have an autoimmune component selectively targeting the immune system. Immunosuppressive therapy or antibody removal, which has already achieved some success, might be therapeutically beneficial, particularly if targeted at removal of the culpable antibodies, via affinity dialysis.

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“…7 Integrin avb3 is expressed not only in the endometrium but also in the embryo, endothelium, and other cell-types including T lymphocytes. [8][9][10][11][12][13][14] However, the mechanisms regulating expression of this integrin by lymphocytes are still not well understood.…”

Section: Introductionmentioning

confidence: 99%

Correlation of the Expression of Integrin αvβ3 in Endometrium and Peripheral Blood Lymphocytes in Infertile Patients

2010

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Integrin alphavbeta3 is an adhesion molecule thought to be relevant to blastocyst attachment. It is expressed by endometrial epithelial cells at the time of ''implantation window,'' and its expression may be altered in women with implantation failure. Integrin alphavbeta3 is also expressed by T lymphocytes. Because immune cells interact with endometrial tissues via integrins, we hypothesized that expression of integrin alphavbeta3 in endometrium and in peripheral blood lymphocytes may correlate. A total of 41 women with implantation failure underwent endometrial biopsy and blood collection at the time of implantation window. Integrin alphavbeta3 expression was evaluated in fresh frozen endometrial specimens using immunohistochemistry and on T lymphocytes using flow cytometry. Statistically significant negative correlation was found between integrin alphavbeta3 in endometrium and T lymphocytes. Integrin alphavbeta3 expression on T lymphocytes does not predict its endometrial expression.

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Beta 3 Integrin Expression on T Cells From Renal Allograft Recipients

Cited by 8 publications

References 6 publications

Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry

Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry

Extensive viral mimicry of 22 AIDS-related autoantigens by HIV-1 proteins and pathway analysis of 561 viral/human homologues suggest an initial treatable autoimmune component of AIDS

Correlation of the Expression of Integrin αvβ3 in Endometrium and Peripheral Blood Lymphocytes in Infertile Patients

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