Activation of human neutrophils by a synthetic anti‐microbial peptide, KLKLLLLLKLK‐NH2, via cell surface calreticulin
We previously reported that a synthetic anti‐bacterial peptide, KLKLLLLLKLK‐NH2 (L5), showed significant chemotherapeutic activity in methicillin‐resistant Staphylococcus aureus‐infected mice, and its ability to activate human neutrophils was related to its chemotherapeutic activity. In this study,...
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| Veröffentlicht in: | European journal of biochemistry 1999-12, Vol.266 (3), p.878-885 |
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| container_title | European journal of biochemistry |
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| creator | Cho, Jang‐Hyun Homma, Ko‐ichi Kanegasaki, Shiro Natori, Shunji |
| description | We previously reported that a synthetic anti‐bacterial peptide, KLKLLLLLKLK‐NH2 (L5), showed significant chemotherapeutic activity in methicillin‐resistant Staphylococcus aureus‐infected mice, and its ability to activate human neutrophils was related to its chemotherapeutic activity. In this study, we found that activation of neutrophils by L5 was inhibited by pertussis toxin, suggesting that GTP‐binding protein (G‐protein) participates in this process. We isolated an L5‐binding protein, which turned out to be human calreticulin, with a molecular mass of 60 kDa from neutrophil membranes. From experiments using an anti‐calreticulin antibody, we proposed that calreticulin is partly localized on the surface of neutrophils, and L5‐bound calreticulin transmits a signal into cells via G‐protein to activate neutrophils to generate superoxide anion. |
| doi_str_mv | 10.1046/j.1432-1327.1999.00920.x |
| format | Article |
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In this study, we found that activation of neutrophils by L5 was inhibited by pertussis toxin, suggesting that GTP‐binding protein (G‐protein) participates in this process. We isolated an L5‐binding protein, which turned out to be human calreticulin, with a molecular mass of 60 kDa from neutrophil membranes. 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In this study, we found that activation of neutrophils by L5 was inhibited by pertussis toxin, suggesting that GTP‐binding protein (G‐protein) participates in this process. We isolated an L5‐binding protein, which turned out to be human calreticulin, with a molecular mass of 60 kDa from neutrophil membranes. From experiments using an anti‐calreticulin antibody, we proposed that calreticulin is partly localized on the surface of neutrophils, and L5‐bound calreticulin transmits a signal into cells via G‐protein to activate neutrophils to generate superoxide anion.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Infective Agents - chemistry</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Calcium-Binding Proteins - genetics</subject><subject>Calcium-Binding Proteins - isolation & purification</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calreticulin</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>G‐protein</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>methicillin‐resistant Staphylococcus aureus</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>neutrophils</subject><subject>Neutrophils - drug effects</subject><subject>Neutrophils - immunology</subject><subject>Neutrophils - metabolism</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - pharmacology</subject><subject>Ribonucleoproteins - genetics</subject><subject>Ribonucleoproteins - isolation & purification</subject><subject>Ribonucleoproteins - metabolism</subject><subject>Structure-Activity Relationship</subject><subject>superoxide anion</subject><subject>Superoxides - metabolism</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkU1OwzAQhS0EoqVwBeQVqyb4P82CRalailrBAlhbjuOorvJHnJRmxxE4IychoUViNjPS-zSaeQ8AiJGPERO3Wx8zSjxMSeDjMAx9hEKC_P0JGB4EROkpGCKEmUdCLgbgwrktQkiEIjgHA4z4hNIJHoJ2qmu7U7UtclgkcNNkKoe5aeqqKDc2dTBqoYKuzeuNqa2GKq_t9-dXZnVVRFalsDRlbWMzhqv1at1X1zvgaUnGcGcV1CZNoWuqRGkDtUqrfk2T2vwSnCUqdebq2EfgbTF_nS299fPD42y69rak-8njKiYxZwmPtOARJ5HinBoRBQFiTOgQa8YQNgEhOlGKsUTrgOIJMVTEVEWGjsDNYW9ZFe-NcbXMrOuvUrkpGidFSDuLOOvA6yPYRJmJZVnZTFWt_DOrA-4OwIdNTftPl30ocit772UfiuxDkb-hyL1czO9fuon-AP9Wglg</recordid><startdate>199912</startdate><enddate>199912</enddate><creator>Cho, Jang‐Hyun</creator><creator>Homma, Ko‐ichi</creator><creator>Kanegasaki, Shiro</creator><creator>Natori, Shunji</creator><general>Blackwell Science Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>199912</creationdate><title>Activation of human neutrophils by a synthetic anti‐microbial peptide, KLKLLLLLKLK‐NH2, via cell surface calreticulin</title><author>Cho, Jang‐Hyun ; Homma, Ko‐ichi ; Kanegasaki, Shiro ; Natori, Shunji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j2920-5ad2d54f5bc65b52ba553e6b770446c91c4401e722cfaa44fcc73182e36d3abe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anti-Infective Agents - chemistry</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Calcium-Binding Proteins - genetics</topic><topic>Calcium-Binding Proteins - isolation & purification</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Calreticulin</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>G‐protein</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>methicillin‐resistant Staphylococcus aureus</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>neutrophils</topic><topic>Neutrophils - drug effects</topic><topic>Neutrophils - immunology</topic><topic>Neutrophils - metabolism</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - pharmacology</topic><topic>Ribonucleoproteins - genetics</topic><topic>Ribonucleoproteins - isolation & purification</topic><topic>Ribonucleoproteins - metabolism</topic><topic>Structure-Activity Relationship</topic><topic>superoxide anion</topic><topic>Superoxides - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cho, Jang‐Hyun</creatorcontrib><creatorcontrib>Homma, Ko‐ichi</creatorcontrib><creatorcontrib>Kanegasaki, Shiro</creatorcontrib><creatorcontrib>Natori, Shunji</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cho, Jang‐Hyun</au><au>Homma, Ko‐ichi</au><au>Kanegasaki, Shiro</au><au>Natori, Shunji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of human neutrophils by a synthetic anti‐microbial peptide, KLKLLLLLKLK‐NH2, via cell surface calreticulin</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1999-12</date><risdate>1999</risdate><volume>266</volume><issue>3</issue><spage>878</spage><epage>885</epage><pages>878-885</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>We previously reported that a synthetic anti‐bacterial peptide, KLKLLLLLKLK‐NH2 (L5), showed significant chemotherapeutic activity in methicillin‐resistant Staphylococcus aureus‐infected mice, and its ability to activate human neutrophils was related to its chemotherapeutic activity. In this study, we found that activation of neutrophils by L5 was inhibited by pertussis toxin, suggesting that GTP‐binding protein (G‐protein) participates in this process. We isolated an L5‐binding protein, which turned out to be human calreticulin, with a molecular mass of 60 kDa from neutrophil membranes. From experiments using an anti‐calreticulin antibody, we proposed that calreticulin is partly localized on the surface of neutrophils, and L5‐bound calreticulin transmits a signal into cells via G‐protein to activate neutrophils to generate superoxide anion.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10583381</pmid><doi>10.1046/j.1432-1327.1999.00920.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1999-12, Vol.266 (3), p.878-885 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Anti-Infective Agents - chemistry Anti-Infective Agents - pharmacology Calcium-Binding Proteins - genetics Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Calreticulin Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell Membrane - drug effects Cell Membrane - metabolism G‐protein Humans In Vitro Techniques Membrane Proteins - genetics Membrane Proteins - isolation & purification Membrane Proteins - metabolism methicillin‐resistant Staphylococcus aureus Mice Molecular Sequence Data neutrophils Neutrophils - drug effects Neutrophils - immunology Neutrophils - metabolism Oligopeptides - chemistry Oligopeptides - pharmacology Ribonucleoproteins - genetics Ribonucleoproteins - isolation & purification Ribonucleoproteins - metabolism Structure-Activity Relationship superoxide anion Superoxides - metabolism |
| title | Activation of human neutrophils by a synthetic anti‐microbial peptide, KLKLLLLLKLK‐NH2, via cell surface calreticulin |
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