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10.1039/d1fo00178g http://scihub22266oqcxt.onion/10.1039/d1fo00178g 33900328!ä!33900328 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33900328&cmd=llinks): Failed to open stream: HTTP request failed! 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N-Glycosylated Ganoderma lucidum immunomodulatory protein improved anti-inflammatory activity via inhibition of the p38 MAPK pathway |pdf=|usr=}}{{33900328}} gab.com Text N-Glycosylated Ganoderma lucidum immunomodulatory protein improved anti-inflammatory activity via inhibition of the p38 MAPK pathway JO: Food Funct http://www.kidney.de/pget.php?&tw=1&pmid=33900328 #FOAvip The global health emergency generated by coronavirus disease-2019 has prompted the search for immunomodulatory agents. There are many potential natural products for drug discovery and development to tackle this disease. One of these candidates is the Ganoderma lucidum fungal immunomodulatory protein (FIP-glu). In the present study, we clarify the influences of N-linked glycans on the improvement of anti-inflammatory activity and the potential mechanisms of action. Four proteins, including FIP-glu (WT) and its mutants N31S, T36N and N31S/T36N, were successfully expressed in P. pastoris, of which T36N and N31S/T36N were glycoproteins. After treatment with peptide-N-glycosidase F, the results of SDS-PAGE and Western blot showed that the glycan moiety was removed completely, indicating that the glycan moiety was N-linked. This was also demonstrated by UPLC-qTOF-MS. The cytotoxicity assay showed that N-linked glycans decreased the cytotoxicity of WT; while, the RT-qPCR assay showed that N-glycosylated WT regulated the mRNA expression of IL-6 and TGF-beta1. The Western blot results showed that N-glycosylated WT reduced the phosphorylation level of p38 MAPK. In conclusion, our findings revealed a novel mechanism by which N-glycosylation of FIP-glu improved its anti-inflammatory activity through the regulation of the expression of inflammatory cytokines in RAW264.7 via inhibition of p38 MAPK phosphorylation. It was proved that N-glycosylation significantly improved the functional properties of FIP-glu, providing theoretical and technical support for expanding the application of FIPs in the food and pharmaceutical industries. Twit Text FOAVip N-Glycosylated Ganoderma lucidum immunomodulatory protein improved anti-inflammatory activity via inhibition of the p38 MAPK pathway ????Food Funct http://www.kidney.de/pget.php?&tw=1&pmid=33900328 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33900328 #FOAvip English Wikipedia <ref>{{Cite pmid|33900328}}</ref> N-Glycosylated Ganoderma lucidum immunomodulatory protein improved anti-inflammatory activity via inhibition of the p38 MAPK pathway #MMPMID33900328 Li QZ; Chen X; Mao PW; Jin MY; Wu Q; Zhou XW Food Funct 2021[Apr]; 12 (8): 3393-3404 PMID33900328show ga The global health emergency generated by coronavirus disease-2019 has prompted the search for immunomodulatory agents. There are many potential natural products for drug discovery and development to tackle this disease. One of these candidates is the Ganoderma lucidum fungal immunomodulatory protein (FIP-glu). In the present study, we clarify the influences of N-linked glycans on the improvement of anti-inflammatory activity and the potential mechanisms of action. Four proteins, including FIP-glu (WT) and its mutants N31S, T36N and N31S/T36N, were successfully expressed in P. pastoris, of which T36N and N31S/T36N were glycoproteins. After treatment with peptide-N-glycosidase F, the results of SDS-PAGE and Western blot showed that the glycan moiety was removed completely, indicating that the glycan moiety was N-linked. This was also demonstrated by UPLC-qTOF-MS. The cytotoxicity assay showed that N-linked glycans decreased the cytotoxicity of WT; while, the RT-qPCR assay showed that N-glycosylated WT regulated the mRNA expression of IL-6 and TGF-beta1. The Western blot results showed that N-glycosylated WT reduced the phosphorylation level of p38 MAPK. In conclusion, our findings revealed a novel mechanism by which N-glycosylation of FIP-glu improved its anti-inflammatory activity through the regulation of the expression of inflammatory cytokines in RAW264.7 via inhibition of p38 MAPK phosphorylation. It was proved that N-glycosylation significantly improved the functional properties of FIP-glu, providing theoretical and technical support for expanding the application of FIPs in the food and pharmaceutical industries. |*Reishi[MESH] |Animals[MESH] |Blotting, Western[MESH] |Chromatography, High Pressure Liquid[MESH] |Cytokines[MESH] |Electrophoresis, Polyacrylamide Gel[MESH] |Fungal Proteins/*pharmacology[MESH] |Glycoproteins/metabolism[MESH] |Glycosylation[MESH] |Immunologic Factors/*pharmacology[MESH] |Immunomodulation/*drug effects[MESH] |Mass Spectrometry[MESH] |Mice[MESH] |Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase[MESH] |RAW 264.7 Cells[MESH] |Real-Time Polymerase Chain Reaction[MESH] |Saccharomycetales[MESH]N-Glycosylated Ganoderma lucidum immunomodulatory protein improved an(epmc).pdf DeepDyve Pubget Overpricing