Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein
Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflam...
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| Veröffentlicht in: | Journal of dental research 2005-02, Vol.84 (2), p.149-153 |
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| creator | Geetha, C. Venkatesh, S.G. Bingle, L. Bingle, C.D. Gorr, S.-U. |
| description | Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNFα from RAW 264.7 macrophage cells. At 200 μg/mL, the peptide GK-7 exhibited inhibition similar to that achieved with 10 μg/mL of polymyxin B. PSP peptides directly inhibited the binding of LPS to LPS-binding protein. The cationic peptide Substance P had no inhibitory effect in these assays, confirming the specificity of the PSP peptides. These findings suggest that PSP peptides can serve as templates for the design of novel anti-inflammatory peptides. |
| doi_str_mv | 10.1177/154405910508400208 |
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Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNFα from RAW 264.7 macrophage cells. At 200 μg/mL, the peptide GK-7 exhibited inhibition similar to that achieved with 10 μg/mL of polymyxin B. PSP peptides directly inhibited the binding of LPS to LPS-binding protein. The cationic peptide Substance P had no inhibitory effect in these assays, confirming the specificity of the PSP peptides. These findings suggest that PSP peptides can serve as templates for the design of novel anti-inflammatory peptides.</description><identifier>ISSN: 0022-0345</identifier><identifier>EISSN: 1544-0591</identifier><identifier>DOI: 10.1177/154405910508400208</identifier><identifier>PMID: 15668332</identifier><identifier>CODEN: JDREAF</identifier><language>eng</language><publisher>United States: SAGE Publications</publisher><subject>Amino Acid Sequence ; Analysis of Variance ; Anti-Bacterial Agents - chemistry ; Antimicrobial Cationic Peptides - chemical synthesis ; Antimicrobial Cationic Peptides - pharmacology ; Blood Proteins - chemistry ; Blood Proteins - genetics ; Cell Line ; Cloning, Molecular ; Dentistry ; Glycoproteins - chemistry ; Glycoproteins - genetics ; Glycoproteins - pharmacology ; Humans ; Macrophages - cytology ; Macrophages - drug effects ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Molecular Sequence Data ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - pharmacology ; Protein Engineering - methods ; RNA - analysis ; Salivary Proteins and Peptides - chemistry ; Salivary Proteins and Peptides - genetics ; Salivary Proteins and Peptides - pharmacology ; Sequence Alignment ; Sequence Analysis, Protein ; Tumor Necrosis Factor-alpha - drug effects</subject><ispartof>Journal of dental research, 2005-02, Vol.84 (2), p.149-153</ispartof><rights>International and American Associations for Dental Research</rights><rights>Copyright American Association for Dental Research/American Academy of Implant Dentistry Feb 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-baed091f88ef73c6c83d0462464d0fc00e33eb8c9709d6e3d820d31e29bf3e1c3</citedby><cites>FETCH-LOGICAL-c397t-baed091f88ef73c6c83d0462464d0fc00e33eb8c9709d6e3d820d31e29bf3e1c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://journals.sagepub.com/doi/pdf/10.1177/154405910508400208$$EPDF$$P50$$Gsage$$H</linktopdf><linktohtml>$$Uhttps://journals.sagepub.com/doi/10.1177/154405910508400208$$EHTML$$P50$$Gsage$$H</linktohtml><link.rule.ids>314,780,784,21819,27924,27925,43621,43622</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15668332$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Geetha, C.</creatorcontrib><creatorcontrib>Venkatesh, S.G.</creatorcontrib><creatorcontrib>Bingle, L.</creatorcontrib><creatorcontrib>Bingle, C.D.</creatorcontrib><creatorcontrib>Gorr, S.-U.</creatorcontrib><title>Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein</title><title>Journal of dental research</title><addtitle>J Dent Res</addtitle><description>Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNFα from RAW 264.7 macrophage cells. At 200 μg/mL, the peptide GK-7 exhibited inhibition similar to that achieved with 10 μg/mL of polymyxin B. PSP peptides directly inhibited the binding of LPS to LPS-binding protein. The cationic peptide Substance P had no inhibitory effect in these assays, confirming the specificity of the PSP peptides. 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genetics</subject><subject>Phosphoproteins - pharmacology</subject><subject>Protein Engineering - methods</subject><subject>RNA - analysis</subject><subject>Salivary Proteins and Peptides - chemistry</subject><subject>Salivary Proteins and Peptides - genetics</subject><subject>Salivary Proteins and Peptides - pharmacology</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, Protein</subject><subject>Tumor Necrosis Factor-alpha - drug effects</subject><issn>0022-0345</issn><issn>1544-0591</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kE1r3DAQhkVp6G7S_oEegughNzejD9vSMeRrA4EG-kFvRiuNFi22tJHsQ_59vOxCIIWeBh6eeWd4CfnK4DtjbXvJaimh1gxqUBKAg_pAlntY7elHspwZr0DIekFOS9kCMM2V-EQWrG4aJQRfkr83WMImUhMd_WP64MwYUqTJ06s4hipE35thMGPKL_QJd2NwWKjPaaCraTCRPpmcZkh_os14sGaAIX4mJ970Bb8c5xn5fXf763pVPf64f7i-eqys0O1YrQ060Mwrhb4VtrFKOJANl4104C0ACoFrZXUL2jUonOLgBEOu114gs-KMXBxydzk9T1jGbgjFYt-biGkqXdOKVtaNnsVv78RtmnKcf-s4aCmUkmKW-EGyOZWS0Xe7HAaTXzoG3b707t_S56XzY_K0HtC9rRxbnoXLg1DMBt_O_ifyFQf5iWo</recordid><startdate>200502</startdate><enddate>200502</enddate><creator>Geetha, C.</creator><creator>Venkatesh, S.G.</creator><creator>Bingle, L.</creator><creator>Bingle, C.D.</creator><creator>Gorr, S.-U.</creator><general>SAGE Publications</general><general>SAGE PUBLICATIONS, INC</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7RQ</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>U9A</scope><scope>7X8</scope></search><sort><creationdate>200502</creationdate><title>Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein</title><author>Geetha, C. ; Venkatesh, S.G. ; Bingle, L. ; Bingle, C.D. ; Gorr, S.-U.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-baed091f88ef73c6c83d0462464d0fc00e33eb8c9709d6e3d820d31e29bf3e1c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Analysis of Variance</topic><topic>Anti-Bacterial Agents - 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Academic</collection><jtitle>Journal of dental research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Geetha, C.</au><au>Venkatesh, S.G.</au><au>Bingle, L.</au><au>Bingle, C.D.</au><au>Gorr, S.-U.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein</atitle><jtitle>Journal of dental research</jtitle><addtitle>J Dent Res</addtitle><date>2005-02</date><risdate>2005</risdate><volume>84</volume><issue>2</issue><spage>149</spage><epage>153</epage><pages>149-153</pages><issn>0022-0345</issn><eissn>1544-0591</eissn><coden>JDREAF</coden><abstract>Parotid secretory protein (PSP) and palate-lung-nasal epithelium clone (PLUNC) are novel secretory proteins that are expressed in the oral cavity and upper airways. Both proteins are related to bactericidal/permeability increasing protein (BPI). Cationic peptides derived from BPI exhibit anti-inflammatory activity. To test if PSP (C20orf70 gene product) also contains anti-inflammatory peptides, we designed 3 cationic peptides based on the predicted structure of PSP and known active regions of BPI. Each peptide inhibited the lipopolysaccharide (LPS)-stimulated secretion of TNFα from RAW 264.7 macrophage cells. At 200 μg/mL, the peptide GK-7 exhibited inhibition similar to that achieved with 10 μg/mL of polymyxin B. PSP peptides directly inhibited the binding of LPS to LPS-binding protein. The cationic peptide Substance P had no inhibitory effect in these assays, confirming the specificity of the PSP peptides. These findings suggest that PSP peptides can serve as templates for the design of novel anti-inflammatory peptides.</abstract><cop>United States</cop><pub>SAGE Publications</pub><pmid>15668332</pmid><doi>10.1177/154405910508400208</doi><tpages>5</tpages></addata></record> |
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| subjects | Amino Acid Sequence Analysis of Variance Anti-Bacterial Agents - chemistry Antimicrobial Cationic Peptides - chemical synthesis Antimicrobial Cationic Peptides - pharmacology Blood Proteins - chemistry Blood Proteins - genetics Cell Line Cloning, Molecular Dentistry Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - pharmacology Humans Macrophages - cytology Macrophages - drug effects Membrane Proteins - chemistry Membrane Proteins - genetics Molecular Sequence Data Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - pharmacology Protein Engineering - methods RNA - analysis Salivary Proteins and Peptides - chemistry Salivary Proteins and Peptides - genetics Salivary Proteins and Peptides - pharmacology Sequence Alignment Sequence Analysis, Protein Tumor Necrosis Factor-alpha - drug effects |
| title | Design and Validation of Anti-inflammatory Peptides from Human Parotid Secretory Protein |
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