Cationic ribosomal proteins can inhibit pro‐inflammatory action stimulated by LPS+HMGB1 and are hindered by advanced glycation end products
We previously found that ribosomal protein L9 (RPL9) is a novel advanced glycation end product (AGE)‐binding protein that can decrease pro‐inflammatory TNF‐α expression stimulated by lipopolysaccharide (LPS) plus high‐mobility group box 1 (HMGB1), suggesting that RPL9 has a role in regulating LPS+HM...
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| Veröffentlicht in: | Biotechnology and applied biochemistry 2024-04, Vol.71 (2), p.264-271 |
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| creator | Watanabe, Masahiro Toyomura, Takao Wake, Hidenori Nishinaka, Takashi Hatipoglu, Omer Faruk Takahashi, Hideo Nishibori, Masahiro Mori, Shuji |
| description | We previously found that ribosomal protein L9 (RPL9) is a novel advanced glycation end product (AGE)‐binding protein that can decrease pro‐inflammatory TNF‐α expression stimulated by lipopolysaccharide (LPS) plus high‐mobility group box 1 (HMGB1), suggesting that RPL9 has a role in regulating LPS+HMGB1‐stimulated inflammatory reactions. Among the various ribosomal proteins, it was found that RPS5 reproduced the regulatory activity of RPL9 on LPS+HMGB1‐stimulated TNF‐α expression in macrophage‐like RAW264.7 cells. RPL9 and RPS5 share a common feature as cationic proteins. Polylysine, a cationic polypeptide, and a synthetic peptide of the cationic region from RPL9 also exhibited reducing activity on LPS+HMGB1‐induced TNF‐α expression. By pull‐down assay, RPL9 and RPS5 were confirmed to interact with AGEs. When AGEs coexisted with LPS, HMGB1, plus RPL9 or RPS5, the reducing effect of TNF‐α expression by these cationic ribosomal proteins was shown to be abrogated. The results suggest that cationic ribosomal proteins have a regulatory role in the pro‐inflammatory response induced by LPS+HMGB1, and in the pathophysiological condition of accumulating AGEs, this regulatory effect is abolished, which exacerbates inflammation. |
| doi_str_mv | 10.1002/bab.2538 |
| format | Article |
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Among the various ribosomal proteins, it was found that RPS5 reproduced the regulatory activity of RPL9 on LPS+HMGB1‐stimulated TNF‐α expression in macrophage‐like RAW264.7 cells. RPL9 and RPS5 share a common feature as cationic proteins. Polylysine, a cationic polypeptide, and a synthetic peptide of the cationic region from RPL9 also exhibited reducing activity on LPS+HMGB1‐induced TNF‐α expression. By pull‐down assay, RPL9 and RPS5 were confirmed to interact with AGEs. When AGEs coexisted with LPS, HMGB1, plus RPL9 or RPS5, the reducing effect of TNF‐α expression by these cationic ribosomal proteins was shown to be abrogated. The results suggest that cationic ribosomal proteins have a regulatory role in the pro‐inflammatory response induced by LPS+HMGB1, and in the pathophysiological condition of accumulating AGEs, this regulatory effect is abolished, which exacerbates inflammation.</description><identifier>ISSN: 0885-4513</identifier><identifier>EISSN: 1470-8744</identifier><identifier>DOI: 10.1002/bab.2538</identifier><identifier>PMID: 38010900</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>advanced glycation end products ; Advanced glycosylation end products ; Age ; cationic amino acids ; Cations ; damage‐associated molecular pattern molecules ; high‐mobility group box‐1 ; HMGB1 protein ; Inflammation ; Inflammatory response ; lipopolysaccharide ; Lipopolysaccharides ; Macrophages ; Polylysine ; Polypeptides ; Proteins ; Ribosomal protein L9 ; Ribosomal proteins</subject><ispartof>Biotechnology and applied biochemistry, 2024-04, Vol.71 (2), p.264-271</ispartof><rights>2023 International Union of Biochemistry and Molecular Biology, Inc.</rights><rights>2024 International Union of Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3498-47529a4475a46f0697762554336d7d7654875c030ff4404baeaab9277b1b84bc3</citedby><cites>FETCH-LOGICAL-c3498-47529a4475a46f0697762554336d7d7654875c030ff4404baeaab9277b1b84bc3</cites><orcidid>0000-0002-2826-1937</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbab.2538$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbab.2538$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38010900$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Watanabe, Masahiro</creatorcontrib><creatorcontrib>Toyomura, Takao</creatorcontrib><creatorcontrib>Wake, Hidenori</creatorcontrib><creatorcontrib>Nishinaka, Takashi</creatorcontrib><creatorcontrib>Hatipoglu, Omer Faruk</creatorcontrib><creatorcontrib>Takahashi, Hideo</creatorcontrib><creatorcontrib>Nishibori, Masahiro</creatorcontrib><creatorcontrib>Mori, Shuji</creatorcontrib><title>Cationic ribosomal proteins can inhibit pro‐inflammatory action stimulated by LPS+HMGB1 and are hindered by advanced glycation end products</title><title>Biotechnology and applied biochemistry</title><addtitle>Biotechnol Appl Biochem</addtitle><description>We previously found that ribosomal protein L9 (RPL9) is a novel advanced glycation end product (AGE)‐binding protein that can decrease pro‐inflammatory TNF‐α expression stimulated by lipopolysaccharide (LPS) plus high‐mobility group box 1 (HMGB1), suggesting that RPL9 has a role in regulating LPS+HMGB1‐stimulated inflammatory reactions. Among the various ribosomal proteins, it was found that RPS5 reproduced the regulatory activity of RPL9 on LPS+HMGB1‐stimulated TNF‐α expression in macrophage‐like RAW264.7 cells. RPL9 and RPS5 share a common feature as cationic proteins. Polylysine, a cationic polypeptide, and a synthetic peptide of the cationic region from RPL9 also exhibited reducing activity on LPS+HMGB1‐induced TNF‐α expression. By pull‐down assay, RPL9 and RPS5 were confirmed to interact with AGEs. When AGEs coexisted with LPS, HMGB1, plus RPL9 or RPS5, the reducing effect of TNF‐α expression by these cationic ribosomal proteins was shown to be abrogated. The results suggest that cationic ribosomal proteins have a regulatory role in the pro‐inflammatory response induced by LPS+HMGB1, and in the pathophysiological condition of accumulating AGEs, this regulatory effect is abolished, which exacerbates inflammation.</description><subject>advanced glycation end products</subject><subject>Advanced glycosylation end products</subject><subject>Age</subject><subject>cationic amino acids</subject><subject>Cations</subject><subject>damage‐associated molecular pattern molecules</subject><subject>high‐mobility group box‐1</subject><subject>HMGB1 protein</subject><subject>Inflammation</subject><subject>Inflammatory response</subject><subject>lipopolysaccharide</subject><subject>Lipopolysaccharides</subject><subject>Macrophages</subject><subject>Polylysine</subject><subject>Polypeptides</subject><subject>Proteins</subject><subject>Ribosomal protein L9</subject><subject>Ribosomal proteins</subject><issn>0885-4513</issn><issn>1470-8744</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp1kdFqFTEQhoMo9lgFn0AC3ghl62STbLKXPQfbCqdUUK-XSTZrU3azNdlV9q4vUPAZfRJzeqqC4NWEyTffDPyEvGRwzADKtwbNcSm5fkRWTCgotBLiMVmB1rIQkvED8iylawDQSpdPyQHXwKAGWJG7DU5-DN7S6M2YxgF7ehPHyfmQqMVAfbjyxk-75s_bHz50PQ4DTmNcKNrdKE2TH-YeJ9dSs9Dth49H5xdna0YxtBSjo1c-tC7uf7H9hsHm95d-sfebqctYlrezndJz8qTDPrkXD_WQfD5992lzXmwvz95vTraF5aLWhVCyrFHkgqLqoKqVqkopBedVq1pVSaGVtMCh64QAYdAhmrpUyjCjhbH8kLzZe_Pir7NLUzP4ZF3fY3DjnJpS10KVTFYso6__Qa_HOYZ8XcMhX8N4JeCv0MYxpei65ib6AePSMGh2ETU5omYXUUZfPQhnM7j2D_g7kwwUe-C7793yX1GzPlnfC38Bz1mapw</recordid><startdate>202404</startdate><enddate>202404</enddate><creator>Watanabe, Masahiro</creator><creator>Toyomura, Takao</creator><creator>Wake, Hidenori</creator><creator>Nishinaka, Takashi</creator><creator>Hatipoglu, Omer Faruk</creator><creator>Takahashi, Hideo</creator><creator>Nishibori, Masahiro</creator><creator>Mori, Shuji</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>7TB</scope><scope>7TK</scope><scope>7U5</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>L7M</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-2826-1937</orcidid></search><sort><creationdate>202404</creationdate><title>Cationic ribosomal proteins can inhibit pro‐inflammatory action stimulated by LPS+HMGB1 and are hindered by advanced glycation end products</title><author>Watanabe, Masahiro ; Toyomura, Takao ; Wake, Hidenori ; Nishinaka, Takashi ; Hatipoglu, Omer Faruk ; Takahashi, Hideo ; Nishibori, Masahiro ; Mori, Shuji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3498-47529a4475a46f0697762554336d7d7654875c030ff4404baeaab9277b1b84bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>advanced glycation end products</topic><topic>Advanced glycosylation end products</topic><topic>Age</topic><topic>cationic amino acids</topic><topic>Cations</topic><topic>damage‐associated molecular pattern molecules</topic><topic>high‐mobility group box‐1</topic><topic>HMGB1 protein</topic><topic>Inflammation</topic><topic>Inflammatory response</topic><topic>lipopolysaccharide</topic><topic>Lipopolysaccharides</topic><topic>Macrophages</topic><topic>Polylysine</topic><topic>Polypeptides</topic><topic>Proteins</topic><topic>Ribosomal protein L9</topic><topic>Ribosomal proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Masahiro</creatorcontrib><creatorcontrib>Toyomura, Takao</creatorcontrib><creatorcontrib>Wake, Hidenori</creatorcontrib><creatorcontrib>Nishinaka, Takashi</creatorcontrib><creatorcontrib>Hatipoglu, Omer Faruk</creatorcontrib><creatorcontrib>Takahashi, Hideo</creatorcontrib><creatorcontrib>Nishibori, Masahiro</creatorcontrib><creatorcontrib>Mori, Shuji</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology and applied biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Masahiro</au><au>Toyomura, Takao</au><au>Wake, Hidenori</au><au>Nishinaka, Takashi</au><au>Hatipoglu, Omer Faruk</au><au>Takahashi, Hideo</au><au>Nishibori, Masahiro</au><au>Mori, Shuji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cationic ribosomal proteins can inhibit pro‐inflammatory action stimulated by LPS+HMGB1 and are hindered by advanced glycation end products</atitle><jtitle>Biotechnology and applied biochemistry</jtitle><addtitle>Biotechnol Appl Biochem</addtitle><date>2024-04</date><risdate>2024</risdate><volume>71</volume><issue>2</issue><spage>264</spage><epage>271</epage><pages>264-271</pages><issn>0885-4513</issn><eissn>1470-8744</eissn><abstract>We previously found that ribosomal protein L9 (RPL9) is a novel advanced glycation end product (AGE)‐binding protein that can decrease pro‐inflammatory TNF‐α expression stimulated by lipopolysaccharide (LPS) plus high‐mobility group box 1 (HMGB1), suggesting that RPL9 has a role in regulating LPS+HMGB1‐stimulated inflammatory reactions. Among the various ribosomal proteins, it was found that RPS5 reproduced the regulatory activity of RPL9 on LPS+HMGB1‐stimulated TNF‐α expression in macrophage‐like RAW264.7 cells. RPL9 and RPS5 share a common feature as cationic proteins. Polylysine, a cationic polypeptide, and a synthetic peptide of the cationic region from RPL9 also exhibited reducing activity on LPS+HMGB1‐induced TNF‐α expression. By pull‐down assay, RPL9 and RPS5 were confirmed to interact with AGEs. When AGEs coexisted with LPS, HMGB1, plus RPL9 or RPS5, the reducing effect of TNF‐α expression by these cationic ribosomal proteins was shown to be abrogated. The results suggest that cationic ribosomal proteins have a regulatory role in the pro‐inflammatory response induced by LPS+HMGB1, and in the pathophysiological condition of accumulating AGEs, this regulatory effect is abolished, which exacerbates inflammation.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>38010900</pmid><doi>10.1002/bab.2538</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-2826-1937</orcidid></addata></record> |
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| subjects | advanced glycation end products Advanced glycosylation end products Age cationic amino acids Cations damage‐associated molecular pattern molecules high‐mobility group box‐1 HMGB1 protein Inflammation Inflammatory response lipopolysaccharide Lipopolysaccharides Macrophages Polylysine Polypeptides Proteins Ribosomal protein L9 Ribosomal proteins |
| title | Cationic ribosomal proteins can inhibit pro‐inflammatory action stimulated by LPS+HMGB1 and are hindered by advanced glycation end products |
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