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 |
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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 |
format | Article |
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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><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 & 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&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 & 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 & 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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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
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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