Anti-Inflammatory Activity of β-thymosin Peptide Derived from Pacific Oyster (Crassostrea gigas) on NO and PGE₂ Production by Down-Regulating NF-κB in LPS-Induced RAW264.7 Macrophage Cells.
Identifieur interne : 000584 ( Main/Exploration ); précédent : 000583; suivant : 000585Anti-Inflammatory Activity of β-thymosin Peptide Derived from Pacific Oyster (Crassostrea gigas) on NO and PGE₂ Production by Down-Regulating NF-κB in LPS-Induced RAW264.7 Macrophage Cells.
Auteurs : Dukhyun Hwang [Corée du Sud] ; Min-Jae Kang [Corée du Sud] ; Mi Jeong Jo [Corée du Sud] ; Yong Bae Seo [Corée du Sud] ; Nam Gyu Park [Corée du Sud] ; Gun-Do Kim [Corée du Sud]Source :
- Marine drugs [ 1660-3397 ] ; 2019.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Anti-inflammatoires (pharmacologie), Cellules RAW 264.7 (MeSH), Cellules cultivées (MeSH), Crassostrea (composition chimique), Cyclooxygenase 2 (métabolisme), Dinoprostone (biosynthèse), Dinoprostone (métabolisme), Facteur de nécrose tumorale alpha (métabolisme), Facteur de transcription NF-kappa B (métabolisme), Humains (MeSH), Interleukine-1 bêta (métabolisme), Interleukine-6 (métabolisme), Kératinocytes (effets des médicaments et des substances chimiques), Lipopolysaccharides (pharmacologie), Macrophages (effets des médicaments et des substances chimiques), Macrophages (métabolisme), Monoxyde d'azote (biosynthèse), Monoxyde d'azote (métabolisme), Nitric oxide synthase type II (métabolisme), Souris (MeSH), Survie cellulaire (MeSH), Thymosine (isolement et purification), Thymosine (pharmacologie), Transduction du signal (effets des médicaments et des substances chimiques).
- MESH :
- biosynthèse : Dinoprostone, Monoxyde d'azote.
- composition chimique : Crassostrea.
- effets des médicaments et des substances chimiques : Kératinocytes, Macrophages, Transduction du signal.
- isolement et purification : Thymosine.
- métabolisme : Cyclooxygenase 2, Dinoprostone, Facteur de nécrose tumorale alpha, Facteur de transcription NF-kappa B, Interleukine-1 bêta, Interleukine-6, Macrophages, Monoxyde d'azote, Nitric oxide synthase type II.
- pharmacologie : Anti-inflammatoires, Lipopolysaccharides, Thymosine.
- Alignement de séquences, Animaux, Cellules RAW 264.7, Cellules cultivées, Humains, Souris, Survie cellulaire.
English descriptors
- KwdEn :
- Animals (MeSH), Anti-Inflammatory Agents (pharmacology), Cell Survival (MeSH), Cells, Cultured (MeSH), Crassostrea (chemistry), Cyclooxygenase 2 (metabolism), Dinoprostone (biosynthesis), Dinoprostone (metabolism), Humans (MeSH), Interleukin-1beta (metabolism), Interleukin-6 (metabolism), Keratinocytes (drug effects), Lipopolysaccharides (pharmacology), Macrophages (drug effects), Macrophages (metabolism), Mice (MeSH), NF-kappa B (metabolism), Nitric Oxide (biosynthesis), Nitric Oxide (metabolism), Nitric Oxide Synthase Type II (metabolism), RAW 264.7 Cells (MeSH), Sequence Alignment (MeSH), Signal Transduction (drug effects), Thymosin (isolation & purification), Thymosin (pharmacology), Tumor Necrosis Factor-alpha (metabolism).
- MESH :
- chemical , biosynthesis : Dinoprostone, Nitric Oxide.
- chemical , isolation & purification : Thymosin.
- chemical , metabolism : Cyclooxygenase 2, Dinoprostone, Interleukin-1beta, Interleukin-6, NF-kappa B, Nitric Oxide, Nitric Oxide Synthase Type II, Tumor Necrosis Factor-alpha.
- chemical , pharmacology : Anti-Inflammatory Agents, Lipopolysaccharides, Thymosin.
- chemistry : Crassostrea.
- drug effects : Keratinocytes, Macrophages, Signal Transduction.
- metabolism : Macrophages.
- Animals, Cell Survival, Cells, Cultured, Humans, Mice, RAW 264.7 Cells, Sequence Alignment.
Abstract
β-thymosin is known for having 43 amino acids, being water-soluble, having a light molecular weight and ubiquitous polypeptide. The biological activities of β-thymosin are diverse and include the promotion of wound healing, reduction of inflammation, differentiation of T cells and inhibition of apoptosis. Our previous studies showed that oyster β-thymosin originated from the mantle of the Pacific oyster, Crassostrea gigas and had antimicrobial activity. In this study, we investigated the anti-inflammatory effects of oyster β-thymosin in lipopolysaccharide (LPS)-induced RAW264.7 macrophage cells using human β-thymosin as a control. Oyster β-thymosin inhibited the nitric oxide (NO) production as much as human β-thymosin in LPS-induced RAW264.7 cells. It also showed that oyster β-thymosin suppressed the expression of prostaglandin E₂ (PGE₂), inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2). Moreover, oyster β-thymosin reduced inflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β) and interleukin-6 (IL-6). Oyster β-thymosin also suppressed the nuclear translocation of phosphorylated nuclear factor-κB (NF-κB) and degradation of inhibitory κB (IκB) in LPS-induced RAW264.7 cells. These results suggest that oyster β-thymosin, which is derived from the mantle of the Pacific oyster, has as much anti-inflammatory effects as human β-thymosin. Additionally, oyster β-thymosin suppressed NO production, PGE₂ production and inflammatory cytokines expression via NF-κB in LPS-induced RAW264.7 cells.
DOI: 10.3390/md17020129
PubMed: 30795639
PubMed Central: PMC6409780
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<author><name sortKey="Hwang, Dukhyun" sort="Hwang, Dukhyun" uniqKey="Hwang D" first="Dukhyun" last="Hwang">Dukhyun Hwang</name>
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<author><name sortKey="Hwang, Dukhyun" sort="Hwang, Dukhyun" uniqKey="Hwang D" first="Dukhyun" last="Hwang">Dukhyun Hwang</name>
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<author><name sortKey="Kang, Min Jae" sort="Kang, Min Jae" uniqKey="Kang M" first="Min-Jae" last="Kang">Min-Jae Kang</name>
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<author><name sortKey="Kim, Gun Do" sort="Kim, Gun Do" uniqKey="Kim G" first="Gun-Do" last="Kim">Gun-Do Kim</name>
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<series><title level="j">Marine drugs</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Anti-Inflammatory Agents (pharmacology)</term>
<term>Cell Survival (MeSH)</term>
<term>Cells, Cultured (MeSH)</term>
<term>Crassostrea (chemistry)</term>
<term>Cyclooxygenase 2 (metabolism)</term>
<term>Dinoprostone (biosynthesis)</term>
<term>Dinoprostone (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Interleukin-1beta (metabolism)</term>
<term>Interleukin-6 (metabolism)</term>
<term>Keratinocytes (drug effects)</term>
<term>Lipopolysaccharides (pharmacology)</term>
<term>Macrophages (drug effects)</term>
<term>Macrophages (metabolism)</term>
<term>Mice (MeSH)</term>
<term>NF-kappa B (metabolism)</term>
<term>Nitric Oxide (biosynthesis)</term>
<term>Nitric Oxide (metabolism)</term>
<term>Nitric Oxide Synthase Type II (metabolism)</term>
<term>RAW 264.7 Cells (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Signal Transduction (drug effects)</term>
<term>Thymosin (isolation & purification)</term>
<term>Thymosin (pharmacology)</term>
<term>Tumor Necrosis Factor-alpha (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Anti-inflammatoires (pharmacologie)</term>
<term>Cellules RAW 264.7 (MeSH)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Crassostrea (composition chimique)</term>
<term>Cyclooxygenase 2 (métabolisme)</term>
<term>Dinoprostone (biosynthèse)</term>
<term>Dinoprostone (métabolisme)</term>
<term>Facteur de nécrose tumorale alpha (métabolisme)</term>
<term>Facteur de transcription NF-kappa B (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Interleukine-1 bêta (métabolisme)</term>
<term>Interleukine-6 (métabolisme)</term>
<term>Kératinocytes (effets des médicaments et des substances chimiques)</term>
<term>Lipopolysaccharides (pharmacologie)</term>
<term>Macrophages (effets des médicaments et des substances chimiques)</term>
<term>Macrophages (métabolisme)</term>
<term>Monoxyde d'azote (biosynthèse)</term>
<term>Monoxyde d'azote (métabolisme)</term>
<term>Nitric oxide synthase type II (métabolisme)</term>
<term>Souris (MeSH)</term>
<term>Survie cellulaire (MeSH)</term>
<term>Thymosine (isolement et purification)</term>
<term>Thymosine (pharmacologie)</term>
<term>Transduction du signal (effets des médicaments et des substances chimiques)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Dinoprostone</term>
<term>Nitric Oxide</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Thymosin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cyclooxygenase 2</term>
<term>Dinoprostone</term>
<term>Interleukin-1beta</term>
<term>Interleukin-6</term>
<term>NF-kappa B</term>
<term>Nitric Oxide</term>
<term>Nitric Oxide Synthase Type II</term>
<term>Tumor Necrosis Factor-alpha</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Inflammatory Agents</term>
<term>Lipopolysaccharides</term>
<term>Thymosin</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Dinoprostone</term>
<term>Monoxyde d'azote</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Crassostrea</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Crassostrea</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Keratinocytes</term>
<term>Macrophages</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Kératinocytes</term>
<term>Macrophages</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Thymosine</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Macrophages</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cyclooxygenase 2</term>
<term>Dinoprostone</term>
<term>Facteur de nécrose tumorale alpha</term>
<term>Facteur de transcription NF-kappa B</term>
<term>Interleukine-1 bêta</term>
<term>Interleukine-6</term>
<term>Macrophages</term>
<term>Monoxyde d'azote</term>
<term>Nitric oxide synthase type II</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Anti-inflammatoires</term>
<term>Lipopolysaccharides</term>
<term>Thymosine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Survival</term>
<term>Cells, Cultured</term>
<term>Humans</term>
<term>Mice</term>
<term>RAW 264.7 Cells</term>
<term>Sequence Alignment</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term>
<term>Animaux</term>
<term>Cellules RAW 264.7</term>
<term>Cellules cultivées</term>
<term>Humains</term>
<term>Souris</term>
<term>Survie cellulaire</term>
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<front><div type="abstract" xml:lang="en">β-thymosin is known for having 43 amino acids, being water-soluble, having a light molecular weight and ubiquitous polypeptide. The biological activities of β-thymosin are diverse and include the promotion of wound healing, reduction of inflammation, differentiation of T cells and inhibition of apoptosis. Our previous studies showed that oyster β-thymosin originated from the mantle of the Pacific oyster, <i>Crassostrea gigas</i>
and had antimicrobial activity. In this study, we investigated the anti-inflammatory effects of oyster β-thymosin in lipopolysaccharide (LPS)-induced RAW264.7 macrophage cells using human β-thymosin as a control. Oyster β-thymosin inhibited the nitric oxide (NO) production as much as human β-thymosin in LPS-induced RAW264.7 cells. It also showed that oyster β-thymosin suppressed the expression of prostaglandin E₂ (PGE₂), inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2). Moreover, oyster β-thymosin reduced inflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β) and interleukin-6 (IL-6). Oyster β-thymosin also suppressed the nuclear translocation of phosphorylated nuclear factor-κB (NF-κB) and degradation of inhibitory κB (IκB) in LPS-induced RAW264.7 cells. These results suggest that oyster β-thymosin, which is derived from the mantle of the Pacific oyster, has as much anti-inflammatory effects as human β-thymosin. Additionally, oyster β-thymosin suppressed NO production, PGE₂ production and inflammatory cytokines expression via NF-κB in LPS-induced RAW264.7 cells.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30795639</PMID>
<DateCompleted><Year>2019</Year>
<Month>07</Month>
<Day>22</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>02</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1660-3397</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>17</Volume>
<Issue>2</Issue>
<PubDate><Year>2019</Year>
<Month>Feb</Month>
<Day>21</Day>
</PubDate>
</JournalIssue>
<Title>Marine drugs</Title>
<ISOAbbreviation>Mar Drugs</ISOAbbreviation>
</Journal>
<ArticleTitle>Anti-Inflammatory Activity of β-thymosin Peptide Derived from Pacific Oyster (<i>Crassostrea gigas</i>
) on NO and PGE₂ Production by Down-Regulating NF-κB in LPS-Induced RAW264.7 Macrophage Cells.</ArticleTitle>
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<ELocationID EIdType="doi" ValidYN="Y">10.3390/md17020129</ELocationID>
<Abstract><AbstractText>β-thymosin is known for having 43 amino acids, being water-soluble, having a light molecular weight and ubiquitous polypeptide. The biological activities of β-thymosin are diverse and include the promotion of wound healing, reduction of inflammation, differentiation of T cells and inhibition of apoptosis. Our previous studies showed that oyster β-thymosin originated from the mantle of the Pacific oyster, <i>Crassostrea gigas</i>
and had antimicrobial activity. In this study, we investigated the anti-inflammatory effects of oyster β-thymosin in lipopolysaccharide (LPS)-induced RAW264.7 macrophage cells using human β-thymosin as a control. Oyster β-thymosin inhibited the nitric oxide (NO) production as much as human β-thymosin in LPS-induced RAW264.7 cells. It also showed that oyster β-thymosin suppressed the expression of prostaglandin E₂ (PGE₂), inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2). Moreover, oyster β-thymosin reduced inflammatory cytokines such as tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β) and interleukin-6 (IL-6). Oyster β-thymosin also suppressed the nuclear translocation of phosphorylated nuclear factor-κB (NF-κB) and degradation of inhibitory κB (IκB) in LPS-induced RAW264.7 cells. These results suggest that oyster β-thymosin, which is derived from the mantle of the Pacific oyster, has as much anti-inflammatory effects as human β-thymosin. Additionally, oyster β-thymosin suppressed NO production, PGE₂ production and inflammatory cytokines expression via NF-κB in LPS-induced RAW264.7 cells.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hwang</LastName>
<ForeName>Dukhyun</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, College of Natural Sciences, Pukyong National University, Busan 48513, Korea. amitie725@naver.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kang</LastName>
<ForeName>Min-Jae</ForeName>
<Initials>MJ</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, College of Natural Sciences, Pukyong National University, Busan 48513, Korea. rkdalsrbmc@naver.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jo</LastName>
<ForeName>Mi Jeong</ForeName>
<Initials>MJ</Initials>
<Identifier Source="ORCID">0000-0001-7289-6203</Identifier>
<AffiliationInfo><Affiliation>Department of Microbiology, College of Natural Sciences, Pukyong National University, Busan 48513, Korea. miss5274@naver.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Seo</LastName>
<ForeName>Yong Bae</ForeName>
<Initials>YB</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, College of Natural Sciences, Pukyong National University, Busan 48513, Korea. haehoo76@pknu.ac.kr.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Park</LastName>
<ForeName>Nam Gyu</ForeName>
<Initials>NG</Initials>
<AffiliationInfo><Affiliation>Department of Biotechnology, College of Fishery Sciences, Pukyong National University, Busan 48513, Korea. ngpark@pknu.ac.kr.</Affiliation>
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<affiliations><list><country><li>Corée du Sud</li>
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<name sortKey="Jo, Mi Jeong" sort="Jo, Mi Jeong" uniqKey="Jo M" first="Mi Jeong" last="Jo">Mi Jeong Jo</name>
<name sortKey="Kang, Min Jae" sort="Kang, Min Jae" uniqKey="Kang M" first="Min-Jae" last="Kang">Min-Jae Kang</name>
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<name sortKey="Park, Nam Gyu" sort="Park, Nam Gyu" uniqKey="Park N" first="Nam Gyu" last="Park">Nam Gyu Park</name>
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