HLA-G in the human thymus: a subpopulation of medullary epithelial but not CD83+ dendritic cells expresses HLA-G as a membrane-bound and soluble protein

Mallet, Valérie; Blaschitz, Astrid; Crisá, Laura; Schmitt, C.; Fournel, Sylvie; King, Ashley; Loke, Y.W.; Dohr, Gottfried; Bouteiller, Philippe Le

doi:10.1093/intimm/11.6.889

Cited by 118 publications

(78 citation statements)

References 45 publications

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“…The resulting protein has a novel carboxyl terminus and is able to complex with ␤ 2 -microglobulin, but would be released from the cell due to the lack of a transmembrane domain (12,13). In addition to the placenta (14,34), soluble HLA-G has also been reported in CD4 ϩ T cells (20), activated monocytes (35), thymic epithelium (36), and lung tumor cells (37). It is intriguing that like HLA-G, the Mamu-AG gene also is alternatively spliced to give rise to a soluble molecule.…”

Section: Discussionmentioning

confidence: 99%

A Soluble Isoform of the Rhesus Monkey Nonclassical MHC Class I Molecule Mamu-AG Is Expressed in the Placenta and the Testis

Ryan¹,

Grendell²,

Geraghty

et al. 2002

The Journal of Immunology

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The nonclassical MHC class I locus HLA-G is expressed primarily in the placenta, although other sites of expression have been noted in normal and pathological situations. In addition, soluble HLA-G isoforms have been detected in the serum of pregnant and nonpregnant women as well as men. The rhesus monkey placenta expresses a novel nonclassical MHC class I molecule Mamu-AG, which has features remarkably similar to those of HLA-G. We determined that the rhesus placenta expresses Mamu-AG mRNA (Mamu-AG5), retaining intron 4 as previously noted in HLA-G5. Immunostaining experiments with Ab 16G1 against the soluble HLA-G5 intron 4 peptide demonstrated that an immunoreactive protein(s) was present in the syncytiotrophoblasts of the chorionic villi of the rhesus placenta, within villous cytotrophoblasts, and occasionally within cells of the villous stroma. The Mamu-AG5 mRNA was readily detected in rhesus testis (although not in ejaculated sperm). Whereas an Ab against membrane-bound Mamu-AG stained few cells, primarily in the interstitium of the testis, there was consistent immunostaining for Mamu-AG5 in cells within the seminiferous tubules, which was corroborated by localization of Mamu-AG mRNA by in situ hybridization. While primary spermatocytes were negative, Sertoli cells, spermatocytes, and spermatids were consistently positive for 16G1 immunostaining. The specific recognition of the soluble Mamu-AG isoform was confirmed by Western blotting of Mamu-AG5 expressed in heterologous cells. The results demonstrate that a soluble nonclassical MHC class I molecule is expressed in the rhesus monkey placenta and testis, and confirm and extend the unique homology between HLA-G and the rhesus nonclassical molecule Mamu-AG.

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Section: Discussionmentioning

confidence: 99%

A Soluble Isoform of the Rhesus Monkey Nonclassical MHC Class I Molecule Mamu-AG Is Expressed in the Placenta and the Testis

Ryan¹,

Grendell²,

Geraghty

et al. 2002

The Journal of Immunology

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“…HLA-G expression is highly tissue-restricted: besides being expressed in fetal tissues, such as trophoblast cells (Rizzo et al, 2011), HLA-G constitutive expression was found in adult thymic medulla (Mallet et al, 1999), cornea (Le Discorde et al, 2003), pancreatic islets (Cervera et al, 2010) and erythroid and endothelial-cell precursors (Rebmann et al, 2010). However, HLA-G expression can be induced in cancers (Rouas-Freiss et al, 2005), transplantation (Sheshgiri et al, 2010), multiple sclerosis (Wiendl et al, 2005), inflammatory diseases and viral infections (Fainardi et al, 2011).…”

Section: Serum Human Leukocyte Antigen-g and Soluble Interleukin 2 Rementioning

confidence: 99%

Serum Human Leukocyte Antigen-G and Soluble Interleukin 2 Receptor Levels in Acute Lymphoblastic Leukemic Pediatric Patients

Motawi

Zakhary²,

Salman³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Aims and Background: Human leukocyte antigen-G and interleukin-2 receptor play pivotal roles in the proliferation of lymphocytes, and thus generation of immune responses. Their overexpression has been evidenced in different malignant hematopoietic diseases. This study aimed to validate serum soluble human leukocyte antigen-G (sHLA-G) and serum soluble interleukin-2 receptor (sIL-2R) as an additional tool for the diagnosis and follow up of acute lymphoblastic leukemia (ALL). Subjects and Methods: Both markers were determined by ELISA in the serum of 33 ALL pediatric patients before treatment and after intensification phase of chemotherapy as well as in the serum of 14 healthy donors that were selected as a control group. Results: ALL patients showed abnormal CBC and high serum lactate dehydrogenase, which were improved after chemotherapy. Also, there was a non-significant increase in serum sHLA-G in ALL patients compared with the control group. However, after chemotherapy, sHLA-G was increased significantly compared with before treatment. On the other hand, serum sIL-2R in ALL patients was increased significantly compared with the control group. After chemotherapy, sIL-2R decreased significantly compared with before treatment. Conclusions: From these results it could be suggested that measurement of serum sHLA-G might be helpful in diagnosis of ALL, while sIL-2R might be useful in diagnosis and follow-up of ALL in pediatric patients.Keywords: Soluble human leukocyte antigen-G -soluble interleukin-2 receptor -acute lymphoblastic leukemia

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“…Also, HLA-G is expressed in the thymus and on various dendritic cell subsets. 61 Like HLA-G, HLA-F is also expressed in the trophoblast 62 and also interacts with ILT2 and ILT4 receptors. In general, little is known about HLA-F. HLA-F is known to bind a restricted subset of peptides derived from the leader peptides of other MHC class I molecules.…”

Section: Mhc Class Ia (Classical) Molecules H-2k H-2d and H-2l In Micementioning

confidence: 99%

MHC and MHC‑like molecules: Structural perspectives on the design of molecular vaccines

Apostolopoulos¹,

Yuriev²,

Lazoura³

et al. 2008

Human Vaccines

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© 2 0 0 8 L A N D E S B I O S C I E N C E . D O N O T D I S T R I B U T E .peptide-binding proteins as well as antigen processing molecules, such as TAP and tapasin. The MHC class II locus encodes heterodimeric peptide-binding proteins and proteins that modulate peptide loading onto MHC class II proteins in the lysosomal compartment, such as MHC class II DM, -DQ and -DP. MHC class I proteins are expressed on all nucleated cells and MHC class II are found on only a few specialized cell types; B-cells, neutrophils, dendritic cells and thymic epithelial cells and can be induced on macrophages and human T cells. The MHC class III locus encodes for other immune components, i.e., complement components (C2, C4, factor B), cytokines (TNFα and TNFb) and HSP70. Stimulation of CD8 T CellsMHC, first described more than 70 years ago to control transplant rejection in mice, was initially termed H-2. There are three gene families for murine MHC class I: H-2K, H-2D and H-2L and for human MHC: HLA-A, HLA-B and HLA-C. The first step in CD8 + T cell generation is the uptake and presentation of peptides by antigen presenting cells through their MHC molecules. Peptides bound to MHC class I are usually endogenous and cytosolic although exogenous peptides may also be presented by MHC class I molecules. 4,5 Exogenous antigens are taken up by antigen presenting cells (APCs), primarily dendritic cells, into phagosomes and early and late endosomes and presented to MHC class II molecules. Numerous reports have demonstrated that in early endosomes some antigens can either degrade or escape out of the endosome into the cytosol and enter the proteasome. 4,5 Likewise, endogenous peptides are primarily generated in the cytosol by the proteasome. From this point, exogenous-and endogenous-derived peptides follow the same pathway. The proteasome consists of 24 subunits, half of which contain proteolytic activity. The proteasome degrades antigens (proteins) into small peptides which are released into the cytosol. The peptides are transported from the cytosol into the endoplasmic reticulum (ER) via the transporter associated with antigen processing (TAP1 and TAP2) by ATP. In the ER, peptides bind to the newly synthesized MHC class I molecules following the formation of a large multimeric complex which involves TAP, tapasin, calreticulin, calnexin and ER60. From the ER, the peptide-MHC class I complex is transported to the surface of APCs through the secretory pathway (Golgi) where the complex undergoes several posttranslational modifications. Then the peptide-MHC class I complexes expressed

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HLA-G in the human thymus: a subpopulation of medullary epithelial but not CD83+ dendritic cells expresses HLA-G as a membrane-bound and soluble protein

Cited by 118 publications

References 45 publications

A Soluble Isoform of the Rhesus Monkey Nonclassical MHC Class I Molecule Mamu-AG Is Expressed in the Placenta and the Testis

A Soluble Isoform of the Rhesus Monkey Nonclassical MHC Class I Molecule Mamu-AG Is Expressed in the Placenta and the Testis

Serum Human Leukocyte Antigen-G and Soluble Interleukin 2 Receptor Levels in Acute Lymphoblastic Leukemic Pediatric Patients

MHC and MHC‑like molecules: Structural perspectives on the design of molecular vaccines

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