PEP-1-GRX-1 Modulates Matrix Metalloproteinase-13 and Nitric Oxide Expression of Human Articular Chondrocytes.
Identifieur interne : 000333 ( Main/Exploration ); précédent : 000332; suivant : 000334PEP-1-GRX-1 Modulates Matrix Metalloproteinase-13 and Nitric Oxide Expression of Human Articular Chondrocytes.
Auteurs : Hyun Sook Hwang ; In Young Park ; Hyun Ah Kim ; Soo Young ChoiSource :
- Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology [ 1421-9778 ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Carragénane (toxicité), Cartilage articulaire (cytologie), Cartilage articulaire (effets des médicaments et des substances chimiques), Cartilage articulaire (métabolisme), Cellules cultivées (MeSH), Facteur de transcription NF-kappa B (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Humains (MeSH), Immunohistochimie (MeSH), Interleukine-1 bêta (pharmacologie), Lipopolysaccharides (toxicité), Matrix Metalloproteinase 13 (génétique), Matrix Metalloproteinase 13 (métabolisme), Mercaptamine (analogues et dérivés), Mercaptamine (métabolisme), Mitogen-Activated Protein Kinases (métabolisme), Modèles animaux de maladie humaine (MeSH), Monoxyde d'azote (métabolisme), Mâle (MeSH), Oedème (anatomopathologie), Oedème (induit chimiquement), Oedème (métabolisme), Peptides (génétique), Peptides (métabolisme), Protéines de fusion recombinantes (biosynthèse), Protéines de fusion recombinantes (isolement et purification), Protéines de fusion recombinantes (pharmacologie), Régulation négative (effets des médicaments et des substances chimiques), Souris (MeSH), Souris de lignée C57BL (MeSH), Transduction du signal (effets des médicaments et des substances chimiques).
- MESH :
- analogues et dérivés : Mercaptamine.
- anatomopathologie : Oedème.
- biosynthèse : Protéines de fusion recombinantes.
- cytologie : Cartilage articulaire.
- effets des médicaments et des substances chimiques : Cartilage articulaire, Régulation négative, Transduction du signal.
- génétique : Glutarédoxines, Matrix Metalloproteinase 13, Peptides.
- induit chimiquement : Oedème.
- isolement et purification : Protéines de fusion recombinantes.
- métabolisme : Cartilage articulaire, Facteur de transcription NF-kappa B, Glutarédoxines, Matrix Metalloproteinase 13, Mercaptamine, Mitogen-Activated Protein Kinases, Monoxyde d'azote, Oedème, Peptides.
- pharmacologie : Interleukine-1 bêta, Protéines de fusion recombinantes.
- toxicité : Carragénane, Lipopolysaccharides.
- Animaux, Cellules cultivées, Humains, Immunohistochimie, Modèles animaux de maladie humaine, Mâle, Souris, Souris de lignée C57BL.
English descriptors
- KwdEn :
- Animals (MeSH), Carrageenan (toxicity), Cartilage, Articular (cytology), Cartilage, Articular (drug effects), Cartilage, Articular (metabolism), Cells, Cultured (MeSH), Cysteamine (analogs & derivatives), Cysteamine (metabolism), Disease Models, Animal (MeSH), Down-Regulation (drug effects), Edema (chemically induced), Edema (metabolism), Edema (pathology), Glutaredoxins (genetics), Glutaredoxins (metabolism), Humans (MeSH), Immunohistochemistry (MeSH), Interleukin-1beta (pharmacology), Lipopolysaccharides (toxicity), Male (MeSH), Matrix Metalloproteinase 13 (genetics), Matrix Metalloproteinase 13 (metabolism), Mice (MeSH), Mice, Inbred C57BL (MeSH), Mitogen-Activated Protein Kinases (metabolism), NF-kappa B (metabolism), Nitric Oxide (metabolism), Peptides (genetics), Peptides (metabolism), Recombinant Fusion Proteins (biosynthesis), Recombinant Fusion Proteins (isolation & purification), Recombinant Fusion Proteins (pharmacology), Signal Transduction (drug effects).
- MESH :
- chemical , analogs & derivatives : Cysteamine.
- chemical , biosynthesis : Recombinant Fusion Proteins.
- chemical , genetics : Glutaredoxins, Matrix Metalloproteinase 13, Peptides.
- chemical , isolation & purification : Recombinant Fusion Proteins.
- chemical , metabolism : Cysteamine, Glutaredoxins, Matrix Metalloproteinase 13, Mitogen-Activated Protein Kinases, NF-kappa B, Nitric Oxide, Peptides.
- chemical , pharmacology : Interleukin-1beta, Recombinant Fusion Proteins.
- chemical , toxicity : Carrageenan, Lipopolysaccharides.
- chemically induced : Edema.
- cytology : Cartilage, Articular.
- drug effects : Cartilage, Articular, Down-Regulation, Signal Transduction.
- metabolism : Cartilage, Articular, Edema.
- pathology : Edema.
- Animals, Cells, Cultured, Disease Models, Animal, Humans, Immunohistochemistry, Male, Mice, Mice, Inbred C57BL.
Abstract
BACKGROUND
The protein transduction domain (PTD) enables therapeutic proteins to directly penetrate the membranes of cells and tissues, and has been increasingly utilized. Glutaredoxin-1 (GRX-1) is an endogenous antioxidant enzyme involved in the cellular redox homeostasis system. In this study, we investigated whether PEP-1-GRX-1, a fusion protein of GRX-1 and PEP-1 peptide, a PTD, could suppress catabolic responses in primary human articular chondrocytes and a mouse carrageenan-induced paw edema model.
METHODS
Human articular chondrocytes were isolated enzymatically from articular cartilage and cultured in a monolayer. The transduction efficiency of PEP-1-GRX-1 into articular chondrocytes was measured by western blot and immunohistochemistry. The effects of PEP-1-GRX-1 on matrix metalloproteinases (MMPs) and catabolic factor expression in interleukin (IL)-1β- and lipopolysaccharide (LPS)-treated chondrocytes were analyzed by real-time quantitative reverse transcription-polymerase chain reaction and western blot. The effect of PEP-1-GRX1 on the mitogen-activated protein kinase (MAPK) and nuclear factor kappa-light chain-enhancer of activated B cells (NF-κB) signaling pathway were also analyzed by western blot. Finally, the inhibitory effect of PEP-1-GRX-1 on MMP-13 production was measured in vivo in a mouse carrageenan-induced paw edema model.
RESULTS
PEP-1-GRX-1 significantly penetrated into human chondrocytes and mouse cartilage, whereas GRX-1 did not. PEP-1-GRX-1 significantly suppressed MMP-13 expression and nitric oxide (NO) production in LPS-stimulated chondrocytes, and NO production in IL-1β-stimulated chondrocytes, compared with GRX-1. In addition, PEP-1-GRX-1 decreased IL-1β- and LPS-induced activation of MAPK and NF-κB. In the mouse model of carrageenan-induced paw edema, PEP-1-GRX-1 significantly suppressed carrageenan-induced MMP-13 production as well as paw edema.
CONCLUSION
These results demonstrate that PEP-1-GRX-1 can be transduced efficiently in vitro and in vivo into human chondrocytes and mouse cartilage tissue and downregulate catabolic responses in chondrocytes by inhibiting the MAPK and NF-κB pathway. PEP-1-GRX-1 thus has the potential to reduce catabolic responses in chondrocytes and cartilage.
DOI: 10.1159/000456090
PubMed: 28214840
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Carrageenan (toxicity)</term>
<term>Cartilage, Articular (cytology)</term>
<term>Cartilage, Articular (drug effects)</term>
<term>Cartilage, Articular (metabolism)</term>
<term>Cells, Cultured (MeSH)</term>
<term>Cysteamine (analogs & derivatives)</term>
<term>Cysteamine (metabolism)</term>
<term>Disease Models, Animal (MeSH)</term>
<term>Down-Regulation (drug effects)</term>
<term>Edema (chemically induced)</term>
<term>Edema (metabolism)</term>
<term>Edema (pathology)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Immunohistochemistry (MeSH)</term>
<term>Interleukin-1beta (pharmacology)</term>
<term>Lipopolysaccharides (toxicity)</term>
<term>Male (MeSH)</term>
<term>Matrix Metalloproteinase 13 (genetics)</term>
<term>Matrix Metalloproteinase 13 (metabolism)</term>
<term>Mice (MeSH)</term>
<term>Mice, Inbred C57BL (MeSH)</term>
<term>Mitogen-Activated Protein Kinases (metabolism)</term>
<term>NF-kappa B (metabolism)</term>
<term>Nitric Oxide (metabolism)</term>
<term>Peptides (genetics)</term>
<term>Peptides (metabolism)</term>
<term>Recombinant Fusion Proteins (biosynthesis)</term>
<term>Recombinant Fusion Proteins (isolation & purification)</term>
<term>Recombinant Fusion Proteins (pharmacology)</term>
<term>Signal Transduction (drug effects)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Carragénane (toxicité)</term>
<term>Cartilage articulaire (cytologie)</term>
<term>Cartilage articulaire (effets des médicaments et des substances chimiques)</term>
<term>Cartilage articulaire (métabolisme)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Facteur de transcription NF-kappa B (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Immunohistochimie (MeSH)</term>
<term>Interleukine-1 bêta (pharmacologie)</term>
<term>Lipopolysaccharides (toxicité)</term>
<term>Matrix Metalloproteinase 13 (génétique)</term>
<term>Matrix Metalloproteinase 13 (métabolisme)</term>
<term>Mercaptamine (analogues et dérivés)</term>
<term>Mercaptamine (métabolisme)</term>
<term>Mitogen-Activated Protein Kinases (métabolisme)</term>
<term>Modèles animaux de maladie humaine (MeSH)</term>
<term>Monoxyde d'azote (métabolisme)</term>
<term>Mâle (MeSH)</term>
<term>Oedème (anatomopathologie)</term>
<term>Oedème (induit chimiquement)</term>
<term>Oedème (métabolisme)</term>
<term>Peptides (génétique)</term>
<term>Peptides (métabolisme)</term>
<term>Protéines de fusion recombinantes (biosynthèse)</term>
<term>Protéines de fusion recombinantes (isolement et purification)</term>
<term>Protéines de fusion recombinantes (pharmacologie)</term>
<term>Régulation négative (effets des médicaments et des substances chimiques)</term>
<term>Souris (MeSH)</term>
<term>Souris de lignée C57BL (MeSH)</term>
<term>Transduction du signal (effets des médicaments et des substances chimiques)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Cysteamine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
<term>Matrix Metalloproteinase 13</term>
<term>Peptides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteamine</term>
<term>Glutaredoxins</term>
<term>Matrix Metalloproteinase 13</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>NF-kappa B</term>
<term>Nitric Oxide</term>
<term>Peptides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Interleukin-1beta</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Carrageenan</term>
<term>Lipopolysaccharides</term>
</keywords>
<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Mercaptamine</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Oedème</term>
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<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="chemically induced" xml:lang="en"><term>Edema</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cartilage articulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Cartilage, Articular</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cartilage, Articular</term>
<term>Down-Regulation</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cartilage articulaire</term>
<term>Régulation négative</term>
<term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term>
<term>Matrix Metalloproteinase 13</term>
<term>Peptides</term>
</keywords>
<keywords scheme="MESH" qualifier="induit chimiquement" xml:lang="fr"><term>Oedème</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cartilage, Articular</term>
<term>Edema</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cartilage articulaire</term>
<term>Facteur de transcription NF-kappa B</term>
<term>Glutarédoxines</term>
<term>Matrix Metalloproteinase 13</term>
<term>Mercaptamine</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Monoxyde d'azote</term>
<term>Oedème</term>
<term>Peptides</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Edema</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Interleukine-1 bêta</term>
<term>Protéines de fusion recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Carragénane</term>
<term>Lipopolysaccharides</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cells, Cultured</term>
<term>Disease Models, Animal</term>
<term>Humans</term>
<term>Immunohistochemistry</term>
<term>Male</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules cultivées</term>
<term>Humains</term>
<term>Immunohistochimie</term>
<term>Modèles animaux de maladie humaine</term>
<term>Mâle</term>
<term>Souris</term>
<term>Souris de lignée C57BL</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>The protein transduction domain (PTD) enables therapeutic proteins to directly penetrate the membranes of cells and tissues, and has been increasingly utilized. Glutaredoxin-1 (GRX-1) is an endogenous antioxidant enzyme involved in the cellular redox homeostasis system. In this study, we investigated whether PEP-1-GRX-1, a fusion protein of GRX-1 and PEP-1 peptide, a PTD, could suppress catabolic responses in primary human articular chondrocytes and a mouse carrageenan-induced paw edema model.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>METHODS</b>
</p>
<p>Human articular chondrocytes were isolated enzymatically from articular cartilage and cultured in a monolayer. The transduction efficiency of PEP-1-GRX-1 into articular chondrocytes was measured by western blot and immunohistochemistry. The effects of PEP-1-GRX-1 on matrix metalloproteinases (MMPs) and catabolic factor expression in interleukin (IL)-1β- and lipopolysaccharide (LPS)-treated chondrocytes were analyzed by real-time quantitative reverse transcription-polymerase chain reaction and western blot. The effect of PEP-1-GRX1 on the mitogen-activated protein kinase (MAPK) and nuclear factor kappa-light chain-enhancer of activated B cells (NF-κB) signaling pathway were also analyzed by western blot. Finally, the inhibitory effect of PEP-1-GRX-1 on MMP-13 production was measured in vivo in a mouse carrageenan-induced paw edema model.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>PEP-1-GRX-1 significantly penetrated into human chondrocytes and mouse cartilage, whereas GRX-1 did not. PEP-1-GRX-1 significantly suppressed MMP-13 expression and nitric oxide (NO) production in LPS-stimulated chondrocytes, and NO production in IL-1β-stimulated chondrocytes, compared with GRX-1. In addition, PEP-1-GRX-1 decreased IL-1β- and LPS-induced activation of MAPK and NF-κB. In the mouse model of carrageenan-induced paw edema, PEP-1-GRX-1 significantly suppressed carrageenan-induced MMP-13 production as well as paw edema.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSION</b>
</p>
<p>These results demonstrate that PEP-1-GRX-1 can be transduced efficiently in vitro and in vivo into human chondrocytes and mouse cartilage tissue and downregulate catabolic responses in chondrocytes by inhibiting the MAPK and NF-κB pathway. PEP-1-GRX-1 thus has the potential to reduce catabolic responses in chondrocytes and cartilage.</p>
</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28214840</PMID>
<DateCompleted><Year>2017</Year>
<Month>06</Month>
<Day>06</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>02</Month>
<Day>12</Day>
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<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1421-9778</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>41</Volume>
<Issue>1</Issue>
<PubDate><Year>2017</Year>
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<Title>Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology</Title>
<ISOAbbreviation>Cell Physiol Biochem</ISOAbbreviation>
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<ArticleTitle>PEP-1-GRX-1 Modulates Matrix Metalloproteinase-13 and Nitric Oxide Expression of Human Articular Chondrocytes.</ArticleTitle>
<Pagination><MedlinePgn>252-264</MedlinePgn>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The protein transduction domain (PTD) enables therapeutic proteins to directly penetrate the membranes of cells and tissues, and has been increasingly utilized. Glutaredoxin-1 (GRX-1) is an endogenous antioxidant enzyme involved in the cellular redox homeostasis system. In this study, we investigated whether PEP-1-GRX-1, a fusion protein of GRX-1 and PEP-1 peptide, a PTD, could suppress catabolic responses in primary human articular chondrocytes and a mouse carrageenan-induced paw edema model.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">Human articular chondrocytes were isolated enzymatically from articular cartilage and cultured in a monolayer. The transduction efficiency of PEP-1-GRX-1 into articular chondrocytes was measured by western blot and immunohistochemistry. The effects of PEP-1-GRX-1 on matrix metalloproteinases (MMPs) and catabolic factor expression in interleukin (IL)-1β- and lipopolysaccharide (LPS)-treated chondrocytes were analyzed by real-time quantitative reverse transcription-polymerase chain reaction and western blot. The effect of PEP-1-GRX1 on the mitogen-activated protein kinase (MAPK) and nuclear factor kappa-light chain-enhancer of activated B cells (NF-κB) signaling pathway were also analyzed by western blot. Finally, the inhibitory effect of PEP-1-GRX-1 on MMP-13 production was measured in vivo in a mouse carrageenan-induced paw edema model.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">PEP-1-GRX-1 significantly penetrated into human chondrocytes and mouse cartilage, whereas GRX-1 did not. PEP-1-GRX-1 significantly suppressed MMP-13 expression and nitric oxide (NO) production in LPS-stimulated chondrocytes, and NO production in IL-1β-stimulated chondrocytes, compared with GRX-1. In addition, PEP-1-GRX-1 decreased IL-1β- and LPS-induced activation of MAPK and NF-κB. In the mouse model of carrageenan-induced paw edema, PEP-1-GRX-1 significantly suppressed carrageenan-induced MMP-13 production as well as paw edema.</AbstractText>
<AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">These results demonstrate that PEP-1-GRX-1 can be transduced efficiently in vitro and in vivo into human chondrocytes and mouse cartilage tissue and downregulate catabolic responses in chondrocytes by inhibiting the MAPK and NF-κB pathway. PEP-1-GRX-1 thus has the potential to reduce catabolic responses in chondrocytes and cartilage.</AbstractText>
<CopyrightInformation>© 2017 The Author(s). Published by S. Karger AG, Basel.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hwang</LastName>
<ForeName>Hyun Sook</ForeName>
<Initials>HS</Initials>
</Author>
<Author ValidYN="Y"><LastName>Park</LastName>
<ForeName>In Young</ForeName>
<Initials>IY</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Hyun Ah</ForeName>
<Initials>HA</Initials>
</Author>
<Author ValidYN="Y"><LastName>Choi</LastName>
<ForeName>Soo Young</ForeName>
<Initials>SY</Initials>
</Author>
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<Language>eng</Language>
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<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>01</Month>
<Day>23</Day>
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<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>Cell Physiol Biochem</MedlineTA>
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<ISSNLinking>1015-8987</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D053583">Interleukin-1beta</NameOfSubstance>
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<NameOfSubstance UI="D008070">Lipopolysaccharides</NameOfSubstance>
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<NameOfSubstance UI="D016328">NF-kappa B</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C503924">Pep-1 peptide</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010455">Peptides</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber>
<NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>5UX2SD1KE2</RegistryNumber>
<NameOfSubstance UI="D003543">Cysteamine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9000-07-1</RegistryNumber>
<NameOfSubstance UI="D002351">Carrageenan</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber>
<NameOfSubstance UI="D020928">Mitogen-Activated Protein Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber>
<NameOfSubstance UI="D053509">Matrix Metalloproteinase 13</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002351" MajorTopicYN="N">Carrageenan</DescriptorName>
<QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002358" MajorTopicYN="N">Cartilage, Articular</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003543" MajorTopicYN="N">Cysteamine</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015536" MajorTopicYN="N">Down-Regulation</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004487" MajorTopicYN="N">Edema</DescriptorName>
<QualifierName UI="Q000139" MajorTopicYN="N">chemically induced</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053583" MajorTopicYN="N">Interleukin-1beta</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008070" MajorTopicYN="N">Lipopolysaccharides</DescriptorName>
<QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053509" MajorTopicYN="N">Matrix Metalloproteinase 13</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020928" MajorTopicYN="N">Mitogen-Activated Protein Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016328" MajorTopicYN="N">NF-kappa B</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Chondrocyte</Keyword>
<Keyword MajorTopicYN="N">Glutaredoxin-1</Keyword>
<Keyword MajorTopicYN="N">Matrix metalloproteinase</Keyword>
<Keyword MajorTopicYN="N">Osteoarthritis.</Keyword>
<Keyword MajorTopicYN="N">Protein transduction domain</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>08</Month>
<Day>08</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>11</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2017</Year>
<Month>2</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>6</Month>
<Day>7</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2017</Year>
<Month>2</Month>
<Day>20</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">28214840</ArticleId>
<ArticleId IdType="pii">000456090</ArticleId>
<ArticleId IdType="doi">10.1159/000456090</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list></list>
<tree><noCountry><name sortKey="Choi, Soo Young" sort="Choi, Soo Young" uniqKey="Choi S" first="Soo Young" last="Choi">Soo Young Choi</name>
<name sortKey="Hwang, Hyun Sook" sort="Hwang, Hyun Sook" uniqKey="Hwang H" first="Hyun Sook" last="Hwang">Hyun Sook Hwang</name>
<name sortKey="Kim, Hyun Ah" sort="Kim, Hyun Ah" uniqKey="Kim H" first="Hyun Ah" last="Kim">Hyun Ah Kim</name>
<name sortKey="Park, In Young" sort="Park, In Young" uniqKey="Park I" first="In Young" last="Park">In Young Park</name>
</noCountry>
</tree>
</affiliations>
</record>
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