Antimicrobial peptides in the stomach of Xenopus laevis
Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals. In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal previously shown to store high concentrations of ant...
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Veröffentlicht in: | The Journal of biological chemistry 1991-10, Vol.266 (29), p.19851-19857 |
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container_end_page | 19857 |
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container_issue | 29 |
container_start_page | 19851 |
container_title | The Journal of biological chemistry |
container_volume | 266 |
creator | MOORE, K. S BEVINS, C. L BRASSEUR, M. M TOMASSINI, N TURNER, K ECK, H ZASLOFF, M |
description | Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals.
In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal
previously shown to store high concentrations of antimicrobial peptides in its skin. Antimicrobial activity was detected in
extracts of X. laevis stomach tissue and nine antimicrobial peptides were then purified. A novel 24-amino acid peptide, designated
PGQ, was isolated from these extracts, and has the following amino acid sequence: GVLSNVIGYLKKLGTGALNAVLKQ. PGQ is relatively
basic and has the potential to form an amphipathic alpha-helix. The other peptides isolated are members of the magainin family
of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor
fragments. None of these peptides had been previously identified in tissues other than the skin. The purification of the peptides
from stomach extracts and subsequent protein sequence analysis reveals that the peptides have undergone the same processing
as their dermal counterparts, and that they are stored in their processed forms. Northern blot analysis indicates that the
magainin family of peptides are synthesized in the stomach, and immunohistochemical studies demonstrate that magainin is stored
in a novel granular multinucleated cell in the gastric mucosa of Xenopus. This study demonstrates that the magainin family
of antimicrobial peptides is found in the gastrointestinal system of X. laevis and offers an opportunity to further define
the physiological role of these defense peptides. |
doi_str_mv | 10.1016/S0021-9258(18)55069-9 |
format | Article |
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In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal
previously shown to store high concentrations of antimicrobial peptides in its skin. Antimicrobial activity was detected in
extracts of X. laevis stomach tissue and nine antimicrobial peptides were then purified. A novel 24-amino acid peptide, designated
PGQ, was isolated from these extracts, and has the following amino acid sequence: GVLSNVIGYLKKLGTGALNAVLKQ. PGQ is relatively
basic and has the potential to form an amphipathic alpha-helix. The other peptides isolated are members of the magainin family
of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor
fragments. None of these peptides had been previously identified in tissues other than the skin. The purification of the peptides
from stomach extracts and subsequent protein sequence analysis reveals that the peptides have undergone the same processing
as their dermal counterparts, and that they are stored in their processed forms. Northern blot analysis indicates that the
magainin family of peptides are synthesized in the stomach, and immunohistochemical studies demonstrate that magainin is stored
in a novel granular multinucleated cell in the gastric mucosa of Xenopus. This study demonstrates that the magainin family
of antimicrobial peptides is found in the gastrointestinal system of X. laevis and offers an opportunity to further define
the physiological role of these defense peptides.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)55069-9</identifier><identifier>PMID: 1717472</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Anti-Infective Agents - isolation & purification ; Antibiotics (antibacterial agents, antifungal agents) ; Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents ; antimicrobial agents ; Applied microbiology ; Biological and medical sciences ; Blotting, Northern ; Chromatography, High Pressure Liquid ; defence mechanisms ; digestive tract ; Electrophoresis ; Freshwater ; Fundamental and applied biological sciences. Psychology ; immunology ; magainin ; Microbiology ; Molecular Sequence Data ; peptides ; Peptides - pharmacology ; RNA - analysis ; Skin - chemistry ; stomach ; Stomach - chemistry ; Xenopus laevis</subject><ispartof>The Journal of biological chemistry, 1991-10, Vol.266 (29), p.19851-19857</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-c412564e942383bd6b1a078463c87d289ba0d738089cade56498bf5406168e1a3</citedby><cites>FETCH-LOGICAL-c440t-c412564e942383bd6b1a078463c87d289ba0d738089cade56498bf5406168e1a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5388454$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1717472$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MOORE, K. S</creatorcontrib><creatorcontrib>BEVINS, C. L</creatorcontrib><creatorcontrib>BRASSEUR, M. M</creatorcontrib><creatorcontrib>TOMASSINI, N</creatorcontrib><creatorcontrib>TURNER, K</creatorcontrib><creatorcontrib>ECK, H</creatorcontrib><creatorcontrib>ZASLOFF, M</creatorcontrib><title>Antimicrobial peptides in the stomach of Xenopus laevis</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals.
In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal
previously shown to store high concentrations of antimicrobial peptides in its skin. Antimicrobial activity was detected in
extracts of X. laevis stomach tissue and nine antimicrobial peptides were then purified. A novel 24-amino acid peptide, designated
PGQ, was isolated from these extracts, and has the following amino acid sequence: GVLSNVIGYLKKLGTGALNAVLKQ. PGQ is relatively
basic and has the potential to form an amphipathic alpha-helix. The other peptides isolated are members of the magainin family
of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor
fragments. None of these peptides had been previously identified in tissues other than the skin. The purification of the peptides
from stomach extracts and subsequent protein sequence analysis reveals that the peptides have undergone the same processing
as their dermal counterparts, and that they are stored in their processed forms. Northern blot analysis indicates that the
magainin family of peptides are synthesized in the stomach, and immunohistochemical studies demonstrate that magainin is stored
in a novel granular multinucleated cell in the gastric mucosa of Xenopus. This study demonstrates that the magainin family
of antimicrobial peptides is found in the gastrointestinal system of X. laevis and offers an opportunity to further define
the physiological role of these defense peptides.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Infective Agents - isolation & purification</subject><subject>Antibiotics (antibacterial agents, antifungal agents)</subject><subject>Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents</subject><subject>antimicrobial agents</subject><subject>Applied microbiology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Chromatography, High Pressure Liquid</subject><subject>defence mechanisms</subject><subject>digestive tract</subject><subject>Electrophoresis</subject><subject>Freshwater</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>immunology</subject><subject>magainin</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>peptides</subject><subject>Peptides - pharmacology</subject><subject>RNA - analysis</subject><subject>Skin - chemistry</subject><subject>stomach</subject><subject>Stomach - chemistry</subject><subject>Xenopus laevis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPwzAMgCMEGmPwEyb1gBAcCnFeTY7TxEuaxAGQdovSNKVBfdF0IP493UPbER_sgz_b8ofQFPAtYBB3rxgTiBXh8hrkDedYqFgdoTFgSWPKYXmMxnvkFJ2F8ImHYApGaAQJJCwhY5TM6t5X3nZN6k0Zta7tfeZC5OuoL1wU-qYytoiaPFq6umlXISqN-_bhHJ3kpgzuYlcn6P3h_m3-FC9eHp_ns0VsGcP9kIFwwZxihEqaZiIFgxPJBLUyyYhUqcFZQiWWyprMDaiSac4ZFiCkA0Mn6Gq7t-2ar5ULva58sK4sTe2aVdAJAUqVIv-CIICAYDCAfAsOP4fQuVy3na9M96sB67VZvTGr19o0SL0xq9UwN90dWKWVyw5TW5VD_3LXN8GaMu9MbX3YY5xKyTg7YIX_KH5853TqG1u4ShMhNFEalORA_wDdyYpr</recordid><startdate>19911015</startdate><enddate>19911015</enddate><creator>MOORE, K. S</creator><creator>BEVINS, C. L</creator><creator>BRASSEUR, M. M</creator><creator>TOMASSINI, N</creator><creator>TURNER, K</creator><creator>ECK, H</creator><creator>ZASLOFF, M</creator><general>American Society for Biochemistry and Molecular Biology</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>7QL</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19911015</creationdate><title>Antimicrobial peptides in the stomach of Xenopus laevis</title><author>MOORE, K. S ; BEVINS, C. L ; BRASSEUR, M. M ; TOMASSINI, N ; TURNER, K ; ECK, H ; ZASLOFF, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-c412564e942383bd6b1a078463c87d289ba0d738089cade56498bf5406168e1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Anti-Infective Agents - isolation & purification</topic><topic>Antibiotics (antibacterial agents, antifungal agents)</topic><topic>Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents</topic><topic>antimicrobial agents</topic><topic>Applied microbiology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Chromatography, High Pressure Liquid</topic><topic>defence mechanisms</topic><topic>digestive tract</topic><topic>Electrophoresis</topic><topic>Freshwater</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>immunology</topic><topic>magainin</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>peptides</topic><topic>Peptides - pharmacology</topic><topic>RNA - analysis</topic><topic>Skin - chemistry</topic><topic>stomach</topic><topic>Stomach - chemistry</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MOORE, K. S</creatorcontrib><creatorcontrib>BEVINS, C. L</creatorcontrib><creatorcontrib>BRASSEUR, M. 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S</au><au>BEVINS, C. L</au><au>BRASSEUR, M. M</au><au>TOMASSINI, N</au><au>TURNER, K</au><au>ECK, H</au><au>ZASLOFF, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antimicrobial peptides in the stomach of Xenopus laevis</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-10-15</date><risdate>1991</risdate><volume>266</volume><issue>29</issue><spage>19851</spage><epage>19857</epage><pages>19851-19857</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Antimicrobial peptides are widely distributed in nature and appear to play a role in the host defense of plants and animals.
In this study we report the existence of antimicrobial peptides in the stomach of the vertebrate Xenopus laevis, an animal
previously shown to store high concentrations of antimicrobial peptides in its skin. Antimicrobial activity was detected in
extracts of X. laevis stomach tissue and nine antimicrobial peptides were then purified. A novel 24-amino acid peptide, designated
PGQ, was isolated from these extracts, and has the following amino acid sequence: GVLSNVIGYLKKLGTGALNAVLKQ. PGQ is relatively
basic and has the potential to form an amphipathic alpha-helix. The other peptides isolated are members of the magainin family
of antimicrobial peptides, and include magainins I and II, PGLa, xenopsin precursor fragment, and four caerulein precursor
fragments. None of these peptides had been previously identified in tissues other than the skin. The purification of the peptides
from stomach extracts and subsequent protein sequence analysis reveals that the peptides have undergone the same processing
as their dermal counterparts, and that they are stored in their processed forms. Northern blot analysis indicates that the
magainin family of peptides are synthesized in the stomach, and immunohistochemical studies demonstrate that magainin is stored
in a novel granular multinucleated cell in the gastric mucosa of Xenopus. This study demonstrates that the magainin family
of antimicrobial peptides is found in the gastrointestinal system of X. laevis and offers an opportunity to further define
the physiological role of these defense peptides.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1717472</pmid><doi>10.1016/S0021-9258(18)55069-9</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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ispartof | The Journal of biological chemistry, 1991-10, Vol.266 (29), p.19851-19857 |
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source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | Amino Acid Sequence Animals Anti-Infective Agents - isolation & purification Antibiotics (antibacterial agents, antifungal agents) Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents antimicrobial agents Applied microbiology Biological and medical sciences Blotting, Northern Chromatography, High Pressure Liquid defence mechanisms digestive tract Electrophoresis Freshwater Fundamental and applied biological sciences. Psychology immunology magainin Microbiology Molecular Sequence Data peptides Peptides - pharmacology RNA - analysis Skin - chemistry stomach Stomach - chemistry Xenopus laevis |
title | Antimicrobial peptides in the stomach of Xenopus laevis |
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