A novel anti‐inflammatory peptide from human lipocortin 5

1 A novel anti‐inflammatory peptide (residues 204–212) of human recombinant lipocortin 5 (hrLC5) found on the high similarity region with uteroglobin is described. 2 Peptide 204–212 dose‐dependently inhibited the contractions of rat isolated stomach strips elicited by porcine pancreatic phospholipas...

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Veröffentlicht in:British journal of pharmacology 1991-06, Vol.103 (2), p.1327-1332
Hauptverfasser: Perretti, Mauro, Becherucci, Cristina, Mugridge, Kenneth G., Solito, Egle, Silvestri, Sergio, Parente, Luca
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container_issue 2
container_start_page 1327
container_title British journal of pharmacology
container_volume 103
creator Perretti, Mauro
Becherucci, Cristina
Mugridge, Kenneth G.
Solito, Egle
Silvestri, Sergio
Parente, Luca
description 1 A novel anti‐inflammatory peptide (residues 204–212) of human recombinant lipocortin 5 (hrLC5) found on the high similarity region with uteroglobin is described. 2 Peptide 204–212 dose‐dependently inhibited the contractions of rat isolated stomach strips elicited by porcine pancreatic phospholipase A2 (PLA2). Contractions caused by arachidonic acid (AA), prostaglandin E2 (PGE2) and 5‐hydroxytryptamine were not affected. No direct enzyme inhibition was observed in a radiochemical assay. 3 PGE2 release by both human fibroblasts and rat macrophages was reduced by peptide 204–212 in a dose‐dependent manner. 4 The development of carrageenin‐induced oedema in rats was significantly inhibited by the local administration of peptide 204–212. 5 The pattern and potency of the biological effects of peptide 204–212 are similar to those of antiflammin 2, a lipocortin 1‐derived peptide. 6 It is suggested that peptide 204–212 may represent the active site responsible for the anti‐inflammatory properties of lipocortin 5.
doi_str_mv 10.1111/j.1476-5381.1991.tb09788.x
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Contractions caused by arachidonic acid (AA), prostaglandin E2 (PGE2) and 5‐hydroxytryptamine were not affected. No direct enzyme inhibition was observed in a radiochemical assay. 3 PGE2 release by both human fibroblasts and rat macrophages was reduced by peptide 204–212 in a dose‐dependent manner. 4 The development of carrageenin‐induced oedema in rats was significantly inhibited by the local administration of peptide 204–212. 5 The pattern and potency of the biological effects of peptide 204–212 are similar to those of antiflammin 2, a lipocortin 1‐derived peptide. 6 It is suggested that peptide 204–212 may represent the active site responsible for the anti‐inflammatory properties of lipocortin 5.</description><identifier>ISSN: 0007-1188</identifier><identifier>EISSN: 1476-5381</identifier><identifier>DOI: 10.1111/j.1476-5381.1991.tb09788.x</identifier><identifier>PMID: 1832064</identifier><identifier>CODEN: BJPCBM</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Annexin A5 ; Anti-Inflammatory Agents, Non-Steroidal ; anti‐inflammatory peptide ; arachidonic acid metabolism ; Biological and medical sciences ; Bones, joints and connective tissue. Antiinflammatory agents ; Calcium-Binding Proteins - analysis ; Calcium-Binding Proteins - pharmacology ; Carrageenan ; Dinoprostone - metabolism ; Edema - chemically induced ; Edema - physiopathology ; human lipocortin 5 ; Humans ; Inflammation ; lipocortins ; Male ; Medical sciences ; Molecular Sequence Data ; Muscle Contraction - drug effects ; Muscle, Smooth - drug effects ; Peptides - pharmacology ; Pharmacology. Drug treatments ; Phospholipases A - antagonists &amp; inhibitors ; Phospholipases A2 ; Pregnancy Proteins - analysis ; Pregnancy Proteins - pharmacology ; Rabbits ; Rats ; Rats, Inbred Strains ; Recombinant Proteins - analysis ; Recombinant Proteins - pharmacology ; Sequence Alignment ; Uteroglobin - analysis</subject><ispartof>British journal of pharmacology, 1991-06, Vol.103 (2), p.1327-1332</ispartof><rights>1991 British Pharmacological Society</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4228-23167f3391a61fe4eb1609318f6151b8cced6f0b99d511f8f9ef10e6d42630bf3</citedby><cites>FETCH-LOGICAL-c4228-23167f3391a61fe4eb1609318f6151b8cced6f0b99d511f8f9ef10e6d42630bf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1908345/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1908345/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27922,27923,53789,53791</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19696826$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1832064$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Perretti, Mauro</creatorcontrib><creatorcontrib>Becherucci, Cristina</creatorcontrib><creatorcontrib>Mugridge, Kenneth G.</creatorcontrib><creatorcontrib>Solito, Egle</creatorcontrib><creatorcontrib>Silvestri, Sergio</creatorcontrib><creatorcontrib>Parente, Luca</creatorcontrib><title>A novel anti‐inflammatory peptide from human lipocortin 5</title><title>British journal of pharmacology</title><addtitle>Br J Pharmacol</addtitle><description>1 A novel anti‐inflammatory peptide (residues 204–212) of human recombinant lipocortin 5 (hrLC5) found on the high similarity region with uteroglobin is described. 2 Peptide 204–212 dose‐dependently inhibited the contractions of rat isolated stomach strips elicited by porcine pancreatic phospholipase A2 (PLA2). Contractions caused by arachidonic acid (AA), prostaglandin E2 (PGE2) and 5‐hydroxytryptamine were not affected. No direct enzyme inhibition was observed in a radiochemical assay. 3 PGE2 release by both human fibroblasts and rat macrophages was reduced by peptide 204–212 in a dose‐dependent manner. 4 The development of carrageenin‐induced oedema in rats was significantly inhibited by the local administration of peptide 204–212. 5 The pattern and potency of the biological effects of peptide 204–212 are similar to those of antiflammin 2, a lipocortin 1‐derived peptide. 6 It is suggested that peptide 204–212 may represent the active site responsible for the anti‐inflammatory properties of lipocortin 5.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Annexin A5</subject><subject>Anti-Inflammatory Agents, Non-Steroidal</subject><subject>anti‐inflammatory peptide</subject><subject>arachidonic acid metabolism</subject><subject>Biological and medical sciences</subject><subject>Bones, joints and connective tissue. Antiinflammatory agents</subject><subject>Calcium-Binding Proteins - analysis</subject><subject>Calcium-Binding Proteins - pharmacology</subject><subject>Carrageenan</subject><subject>Dinoprostone - metabolism</subject><subject>Edema - chemically induced</subject><subject>Edema - physiopathology</subject><subject>human lipocortin 5</subject><subject>Humans</subject><subject>Inflammation</subject><subject>lipocortins</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle, Smooth - drug effects</subject><subject>Peptides - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Phospholipases A - antagonists &amp; inhibitors</subject><subject>Phospholipases A2</subject><subject>Pregnancy Proteins - analysis</subject><subject>Pregnancy Proteins - pharmacology</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Recombinant Proteins - analysis</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Sequence Alignment</subject><subject>Uteroglobin - analysis</subject><issn>0007-1188</issn><issn>1476-5381</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMFO3DAURS1URAfKJ1SKKrW7pH5x4titRAUIChISXbRry3Hs4pFjp3YGmB2f0G_kS5poRlCWvI2fdO-7vjoIfQBcwDSflwVUDc1rwqAAzqEYW8wbxor7HbR4kt6gBca4yQEYe4v2U1piPIlNvYf2gJES02qBvh5nPtxql0k_2seHv9YbJ_tejiGus0EPo-10ZmLos5tVL33m7BBUiKP1Wf0O7Rrpkj7cvgfo1_nZz9OL_Or6--Xp8VWuqrJkeUmANoYQDpKC0ZVugWJOgBkKNbRMKd1Rg1vOuxrAMMO1AaxpV5WU4NaQA3S0yR1Wba87pf0YpRNDtL2MaxGkFS8Vb2_E73ArgGNGqnoK-LQNiOHPSqdR9DYp7Zz0OqySaErclA2jk_HLxqhiSClq8_QJYDGjF0sx8xUzXzGjF1v04n46fv9_zefTDetJ_7jVZVLSmSi9sunZximnrJxLfNv47qzT61c0ECc_LuaN_AOO4KK0</recordid><startdate>199106</startdate><enddate>199106</enddate><creator>Perretti, Mauro</creator><creator>Becherucci, Cristina</creator><creator>Mugridge, Kenneth G.</creator><creator>Solito, Egle</creator><creator>Silvestri, Sergio</creator><creator>Parente, Luca</creator><general>Blackwell Publishing Ltd</general><general>Nature Publishing</general><scope>IQODW</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199106</creationdate><title>A novel anti‐inflammatory peptide from human lipocortin 5</title><author>Perretti, Mauro ; Becherucci, Cristina ; Mugridge, Kenneth G. ; Solito, Egle ; Silvestri, Sergio ; Parente, Luca</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4228-23167f3391a61fe4eb1609318f6151b8cced6f0b99d511f8f9ef10e6d42630bf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Annexin A5</topic><topic>Anti-Inflammatory Agents, Non-Steroidal</topic><topic>anti‐inflammatory peptide</topic><topic>arachidonic acid metabolism</topic><topic>Biological and medical sciences</topic><topic>Bones, joints and connective tissue. Antiinflammatory agents</topic><topic>Calcium-Binding Proteins - analysis</topic><topic>Calcium-Binding Proteins - pharmacology</topic><topic>Carrageenan</topic><topic>Dinoprostone - metabolism</topic><topic>Edema - chemically induced</topic><topic>Edema - physiopathology</topic><topic>human lipocortin 5</topic><topic>Humans</topic><topic>Inflammation</topic><topic>lipocortins</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle, Smooth - drug effects</topic><topic>Peptides - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Phospholipases A - antagonists &amp; inhibitors</topic><topic>Phospholipases A2</topic><topic>Pregnancy Proteins - analysis</topic><topic>Pregnancy Proteins - pharmacology</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Recombinant Proteins - analysis</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Sequence Alignment</topic><topic>Uteroglobin - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Perretti, Mauro</creatorcontrib><creatorcontrib>Becherucci, Cristina</creatorcontrib><creatorcontrib>Mugridge, Kenneth G.</creatorcontrib><creatorcontrib>Solito, Egle</creatorcontrib><creatorcontrib>Silvestri, Sergio</creatorcontrib><creatorcontrib>Parente, Luca</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>British journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perretti, Mauro</au><au>Becherucci, Cristina</au><au>Mugridge, Kenneth G.</au><au>Solito, Egle</au><au>Silvestri, Sergio</au><au>Parente, Luca</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel anti‐inflammatory peptide from human lipocortin 5</atitle><jtitle>British journal of pharmacology</jtitle><addtitle>Br J Pharmacol</addtitle><date>1991-06</date><risdate>1991</risdate><volume>103</volume><issue>2</issue><spage>1327</spage><epage>1332</epage><pages>1327-1332</pages><issn>0007-1188</issn><eissn>1476-5381</eissn><coden>BJPCBM</coden><abstract>1 A novel anti‐inflammatory peptide (residues 204–212) of human recombinant lipocortin 5 (hrLC5) found on the high similarity region with uteroglobin is described. 2 Peptide 204–212 dose‐dependently inhibited the contractions of rat isolated stomach strips elicited by porcine pancreatic phospholipase A2 (PLA2). Contractions caused by arachidonic acid (AA), prostaglandin E2 (PGE2) and 5‐hydroxytryptamine were not affected. No direct enzyme inhibition was observed in a radiochemical assay. 3 PGE2 release by both human fibroblasts and rat macrophages was reduced by peptide 204–212 in a dose‐dependent manner. 4 The development of carrageenin‐induced oedema in rats was significantly inhibited by the local administration of peptide 204–212. 5 The pattern and potency of the biological effects of peptide 204–212 are similar to those of antiflammin 2, a lipocortin 1‐derived peptide. 6 It is suggested that peptide 204–212 may represent the active site responsible for the anti‐inflammatory properties of lipocortin 5.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1832064</pmid><doi>10.1111/j.1476-5381.1991.tb09788.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
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subjects Amino Acid Sequence
Animals
Annexin A5
Anti-Inflammatory Agents, Non-Steroidal
anti‐inflammatory peptide
arachidonic acid metabolism
Biological and medical sciences
Bones, joints and connective tissue. Antiinflammatory agents
Calcium-Binding Proteins - analysis
Calcium-Binding Proteins - pharmacology
Carrageenan
Dinoprostone - metabolism
Edema - chemically induced
Edema - physiopathology
human lipocortin 5
Humans
Inflammation
lipocortins
Male
Medical sciences
Molecular Sequence Data
Muscle Contraction - drug effects
Muscle, Smooth - drug effects
Peptides - pharmacology
Pharmacology. Drug treatments
Phospholipases A - antagonists & inhibitors
Phospholipases A2
Pregnancy Proteins - analysis
Pregnancy Proteins - pharmacology
Rabbits
Rats
Rats, Inbred Strains
Recombinant Proteins - analysis
Recombinant Proteins - pharmacology
Sequence Alignment
Uteroglobin - analysis
title A novel anti‐inflammatory peptide from human lipocortin 5
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