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MeSH:(Histocompatibility Antigens Class II/*genetics/metabolism)

1.Experimental study on H2-Ab1 gene expression in the nasal mucosa of mice with allergic rhinitis.

Yu ZHANG ; Juan FENG ; Jun YONG ; Jie SUN ; Hua ZHANG

Journal of Clinical Otorhinolaryngology Head and Neck Surgery 2014;28(5):327-331

OBJECTIVE: To investigate the level of H2-Ab1 in the nasal mucosa of mice with allergic rhinitis. METHOD: Twenty-four female 129/sv mice were divided into 2 groups: ovalbumin (OVA) group and control. The allergic rhinitis models were induced by classical method with OVA. After the last challenge, the pathological differences between the two groups were surveyed. The levels of H2-AB1 were measured by ELISA and quantitative real time PCR. RESULT: The expression of H2-Ab1 is higher in subjects with AR than that in controls (P < 0.05). CONCLUSION The levels of H2-Ab1 were highly increased in allergic rhinitis group, which might be associated with the pathogenesis of allergic rhinitis.
Animals ; Female ; Gene Expression ; Histocompatibility Antigens Class II ; genetics ; metabolism ; Mice ; Nasal Mucosa ; metabolism ; Rhinitis, Allergic ; metabolism

2.Inhibitory effect of anti-C II TA RNase P on MHC II expression in Jurkat cells.

Fei HE ; Shu-Lin WU ; Ming SUN ; Rong GUO

Journal of Experimental Hematology 2007;15(3):607-611

This study was purposed to investigate the inhibitory effect of anti-C II TA M1-RNA on MHC II expression. The M1-RNA with guide sequences (GS) recognizing C II TA at 3408 site (M1-3408-GS) and C II TA target RNA (3176 - 3560) were constructed, then cloned into the pUC19 and pGEM-7zf (+) vector respectively. The recombinant M1-RNA and its target RNA were incubated in cell-free conditions. It showed that M1-3408-GS could exclusively cleave target RNA, then it was cloned into the psNAV vector. Stable transfectants of Jurkat cells with M1-3408-GS were analyzed for classical MHC II (HLA-DR, -DP, -DQ) induction in response to IFN-gamma by flow cytometry. The level of C II TA mRNA was measured by RT-PCR. The results showed that after IFN-gamma treatment, the expression of HLA-DR, HLA-DP, HLA-DQ on M1-3408-GS positive Jurkat cells decreased 83.17%, 94.12% and 84.31% respectively as compared with control. At the same time the mRNA contents of C II TA also markedly decreased (P < 0.05, t = 4.89). It is concluded that anti-C II TA M1-RNA (M1-3408-GS) inhibits C II TA, decreases itself mRNA content and so suppresses expression of MHC II molecules regulated by C II TA.
Down-Regulation ; Histocompatibility Antigens Class II ; metabolism ; Humans ; Jurkat Cells ; Major Histocompatibility Complex ; genetics ; Nuclear Proteins ; metabolism ; RNA, Messenger ; metabolism ; Ribonuclease P ; metabolism ; Trans-Activators ; metabolism

3.Several indirect methods for analysis of CD4 self-association and its function in stable CD4-MHC-II binding.

He XIAO ; Song LI ; Bei-Fen SHEN ; Yan LI

Chinese Journal of Biotechnology 2005;21(2):239-243

To examine the self-association of CD4 molecules and preliminary studies on its biological function by several indirect methods. A series of CD4 chimeras were generated including truncated CD4 lacking the short cytoplasmic tail, deleted mutantsD1/D2 devoid of D3 and D4 and D3/D4 devoid of D1 and D2 by PCR techniques, as well as another three CD4 chimeric genes by fused human Fas cytoplasmic death domain to the downstream of the above chimeras respectively. All these molecules were subcloned into pEGFP-N1, forming the corresponding expression vectors. After introducing into HEK293 cells, gene-modified cell morphological changes and target protein subcellular localization were observed and analyzed by a confocal microscopy. Moreover, stable 293/CD4 clones were obtained by transfecting the truncated CD4 recombinant plasmid into the HEK293 cell line and selected by G418. The fluorescene intensity and rosette formation of different clones was each analyzed by a confocal microscopy and cell adhesive assays. It's seen that CD4-Fas fusion gene could induce approximately 80% cell apoptosis of transfected HEK293 cells, compared to FKBP12-Fas is about 30% and CD4 gene only is 7%. Furthermore, both D1/D2-Fas and D3/D4 Fas chimeras could trigger nearly all transfected HEK293 cells to death. Cell adhesion assays showed that neither the D1/D2 nor D3/D4 chimeras when expression in HEK293 cells binds to MHC class II + Raji B cells. Interestedly, there were two type stable clones among 293/CD4. Fluorescence intensity analysis displayed that one' mean fluorescence intensity value is about twice of the other while cell-cell binding examination showed that the former is capable of forming rosette with Raji cells but the latter. All these results suggest that CD4 molecules most likely could exist as a dimer or even an oligomer on transfected HEK293 cell surface, which constitute a functional form for stable binding to MHC class II molecules.
Antigen-Presenting Cells ; immunology ; metabolism ; CD4 Antigens ; chemistry ; genetics ; metabolism ; CD4-Positive T-Lymphocytes ; immunology ; metabolism ; Cell Line ; Dimerization ; Fas Ligand Protein ; metabolism ; Histocompatibility Antigens Class II ; genetics ; immunology ; metabolism ; Humans ; Mutagenesis, Site-Directed ; Protein Binding ; genetics ; Protein Multimerization