HLA-E is the only class I gene that escapes CpG methylation and is transcriptionally active in the trophoblast-derived human cell line JAR

1993 ◽  
Vol 38 (2) ◽  
pp. 117-130 ◽  
Author(s):  
José Boucraut ◽  
Thierry Guillaudeux ◽  
Mehdi Alizadeh ◽  
Joelle Boretto ◽  
Giovanna Chimini ◽  
...  
1996 ◽  
Vol 93 (1) ◽  
pp. 236-240 ◽  
Author(s):  
K. Toshitani ◽  
V. Braud ◽  
M. J. Browning ◽  
N. Murray ◽  
A. J. McMichael ◽  
...  

2017 ◽  
Vol 40 (6) ◽  
pp. 201-210 ◽  
Author(s):  
Cheol-Hwa Hong ◽  
Hyun-Jung Sohn ◽  
Hyun-Joo Lee ◽  
Hyun-Il Cho ◽  
Tai-Gyu Kim

1991 ◽  
Vol 174 (5) ◽  
pp. 1159-1166 ◽  
Author(s):  
R Lippé ◽  
E Luke ◽  
Y T Kuah ◽  
C Lomas ◽  
W A Jefferies

Major histocompatibility complex (MHC) class I molecules act as peptide receptors to direct the recognition of foreign antigens by cytolytic T cells. The cell surface expression and trafficking of these peptide receptors is thought to be controlled by the conformation of the MHC molecule and possibly by the phosphorylation of the cytoplasmic portion of the heavy chain protein. It is of some interest that adenoviruses (Ads) have evolved proteins that interfere with the expression of MHC molecules. One of these proteins, called E3/19k, binds to newly synthesized MHC molecules in the rough endoplasmic reticulum (RER) and inhibits their trafficking to the cell surface. Here we show that during the infection of a human cell line with Ad2, the phosphorylation of the endogenous MHC molecules is inhibited. We also observe that the phosphorylation of the endogenous HLA molecules is grossly impaired in a human cell line transfected with the Ad2 EcoRI D fragment containing the E3/19k gene. We conclude that the E3/19k protein inhibits the phosphorylation of the MHC heavy chains and that this may be one of the important functions of this protein in infected cells. In addition, we show that a mutant of the E3/19k protein, which lacks an RER retention signal but which retains its ability to bind to HLA molecules, does not inhibit the phosphorylation of HLA molecules and that phosphorylated molecules are not Endo H sensitive. This suggests that HLA molecules are phosphorylated after leaving the medial-Golgi compartment, thus providing the most compelling evidence yet that HLA molecules are phosphorylated at or near the cell surface. Finally, to our knowledge, this is the first study under which the phosphorylation of MHC molecules is shown to be altered and may have some relevance for other pathogenic conditions.


1973 ◽  
Vol 248 (17) ◽  
pp. 6251-6253 ◽  
Author(s):  
Samuel C. Brooks ◽  
Elizabeth R. Locke ◽  
Herbert D. Soule

2021 ◽  
pp. 1-11
Author(s):  
Natalia Santucci ◽  
Rocío Stampone ◽  
Eduardo Brandão Ferreira da Silva ◽  
Silvina Villar ◽  
Silvana Spinelli ◽  
...  

<b><i>Introduction:</i></b> IL-1β, a cytokine from the innate immune response, is well known for its proinflammatory effects and stimulating activity on the hypothalamus-pituitary-adrenal axis, leading to the pituitary synthesis of adrenocorticotropic hormone followed by cortisol (and dehydroepiandrosterone – DHEA) release by the adrenal gland. While IL-1β modulates the adrenal steroidogenesis at the central level, it is unclear whether it also exerts an effect on the adrenal gland. <b><i>Method:</i></b> We studied the effect of IL-1β on adrenal steroid production and steroidogenic enzyme RNA expression in the human cell line NCI-H295R. We also explored eventual changes in the microRNA (miRNA) profile from IL-1β-treated NCI-H295R cells. <b><i>Results:</i></b> Transcripts encoding IL-1β receptors 1 and 2 were noticeable in the cell line, with cortisol and DHEA production showing a subtle increase after cytokine treatment. Transcripts from key enzymes in the steroidogenic pathway were analyzed, with no noticeable changes on them. The miRNA profile was modified by IL-1β treatment to an extent which bears some relationship with the regulatory mechanisms underlying adrenal steroid production. Since orphan nuclear receptors NR4As have emerged as potential key factors for coordinating inflammatory and metabolic responses, cell expression studies were also carried out to show an NR4As transcript augmentation following IL-1β treatment. <b><i>Discussion/Conclusions:</i></b> The subtle increase in adrenal steroid production in response to IL-1β stimulation without any modification in the transcription of the steroidogenic enzymes analyzed suggests an additional inflammatory/anti-inflammatory loop, wherein NR4As receptors may participate. Besides its physiological role, this process might be implied in pathological states accompanied by an unbalanced immune-endocrine relationship.


1988 ◽  
Vol 37 (15) ◽  
pp. 3038-3041 ◽  
Author(s):  
Maria Grandi ◽  
Fernando C. Giuliani

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