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[PMID]:29272917
[Au] Autor:Liping S; Qiuming L; Jian F; Xiao L; Yongliang Z
[Ad] Endereço:Yunnan Institute of Food Safety, Kunming University of Science and Technology , 727 South Jingming Road, Kunming, Yunnan 650500, People's Republic of China.
[Ti] Título:Purification and Characterization of Peptides Inhibiting MMP-1 Activity with C Terminate of Gly-Leu from Simulated Gastrointestinal Digestion Hydrolysates of Tilapia (Oreochromis niloticus) Skin Gelatin.
[So] Source:J Agric Food Chem;66(3):593-601, 2018 Jan 24.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tilapia skin gelatin hydrolysates (TSGHs) were prepared by simulated gastrointestinal digestion and separated by gel filtration and semi-preparative reversed-phase high-performance liquid chromatography. The anti-photoaging effects were evaluated using an ultraviolet radiation B (UVB)-induced mouse embryonic fibroblast (MEF) photoaging model in vitro. Three fractions from TSGHs with high inhibitory intercellular matrix metalloproteinase-1 (MMP-1) activities and reactive oxygen species (ROS) production were obtained. Three key peptides, GYTGL, LGATGL, and VLGL, were identified, and their C terminate was Gly-Leu. Three peptides were synthesized and exhibited a significant inhibition of intercellular MMP-1 activity and ROS production. Furthermore, three peptides inhibiting MMP-1 activities were evaluated through their docking of S ' and S ' active pockets of MMP-1. Hydrogen bonds and C terminate Gly-Leu played important roles. Finally, the protective effects of three peptides on intercellular collagen in UVB-induced MEFs were compared. Our results indicated that tilapia gelatin peptides exhibited potential activities to prevent and regulate photoaging.
[Mh] Termos MeSH primário: Gelatina/química
Inibidores de Metaloproteinases de Matriz/química
Peptídeos/química
Pele/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Antioxidantes/química
Antioxidantes/isolamento & purificação
Antioxidantes/farmacologia
Colágeno/metabolismo
Digestão
Fibroblastos/efeitos dos fármacos
Fibroblastos/enzimologia
Fibroblastos/metabolismo
Fibroblastos/efeitos da radiação
Proteínas de Peixes/química
Proteínas de Peixes/isolamento & purificação
Proteínas de Peixes/farmacologia
Trato Gastrointestinal/metabolismo
Gelatina/isolamento & purificação
Gelatina/farmacologia
Metaloproteinase 1 da Matriz/química
Metaloproteinase 1 da Matriz/metabolismo
Inibidores de Metaloproteinases de Matriz/isolamento & purificação
Camundongos
Modelos Biológicos
Simulação de Acoplamento Molecular
Peptídeos/isolamento & purificação
Peptídeos/farmacologia
Espécies Reativas de Oxigênio/metabolismo
Pele/metabolismo
Tilápia
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Fish Proteins); 0 (Matrix Metalloproteinase Inhibitors); 0 (Peptides); 0 (Reactive Oxygen Species); 9000-70-8 (Gelatin); 9007-34-5 (Collagen); EC 3.4.24.7 (Matrix Metalloproteinase 1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04196


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[PMID]:29034777
[Au] Autor:Wang S; Liu C; Liu X; He Y; Shen D; Luo Q; Dong Y; Dong H; Pang Z
[Ad] Endereço:Department of General Surgery, The Second Affiliated Hospital of Zhengzhou University, Zhengzhou, China.
[Ti] Título:Effects of matrix metalloproteinase inhibitor doxycycline and CD147 antagonist peptide-9 on gallbladder carcinoma cell lines.
[So] Source:Tumour Biol;39(10):1010428317718192, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gallbladder carcinoma is the most common and aggressive malignancy of the biliary tree and highly expresses CD147, which is closely related to disease prognosis in a variety of human cancers. Doxycycline exhibited anti-tumor properties in many cancer cells. CD147 antagonist peptide-9 is a polypeptide and can specifically bind to CD147. The effect of these two drugs on gallbladder cancer cells has not been studied. The aim of this study is to investigate the effect of doxycycline and antagonist peptide-9 on gallbladder carcinoma cells and the possible mechanism of inhibition on cancer cell of doxycycline. To investigate the effects of doxycycline and antagonist peptide-9 on gallbladder carcinoma cells (GBC-SD and SGC-996), cell proliferation, CD147 expression, and early-stage apoptosis rate were measured after treated with doxycycline. Matrix metalloproteinase-2 and matrix metalloproteinase-9 activities were measured after treated with different concentrations of doxycycline, antagonist peptide-9, and their combination. The results demonstrated that doxycycline inhibited cell proliferation, reduced CD147 expression level, and induced an early-stage apoptosis response in GBC-SD and SGC-996 cells. The matrix metalloproteinase-2 and matrix metalloproteinase-9 activities were inhibited by antagonist peptide-9 and doxycycline, and the inhibitory effects were enhanced by combined drugs in gallbladder carcinoma cell lines. Taken together, doxycycline showed inhibitory effects on gallbladder carcinoma cell lines and reduced the expression of CD147, and this may be the mechanism by which doxycycline inhibits cancer cells. This study provides new information and tries to implement the design of adjuvant therapy method for gallbladder carcinoma.
[Mh] Termos MeSH primário: Basigina/metabolismo
Doxiciclina/farmacologia
Neoplasias da Vesícula Biliar/tratamento farmacológico
Inibidores de Metaloproteinases de Matriz/farmacologia
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Neoplasias da Vesícula Biliar/metabolismo
Seres Humanos
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Matrix Metalloproteinase Inhibitors); 0 (Peptides); 136894-56-9 (Basigin); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.35 (Matrix Metalloproteinase 9); N12000U13O (Doxycycline)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317718192


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[PMID]:28958936
[Au] Autor:Kim J; Jeong YH; Lee EJ; Park JS; Seo H; Kim HS
[Ad] Endereço:Department of Molecular & Life Sciences, College of Science & Technology, Hanyang University, Ansan, South Korea.
[Ti] Título:Suppression of neuroinflammation by matrix metalloproteinase-8 inhibitor in aged normal and LRRK2 G2019S Parkinson's disease model mice challenged with lipopolysaccharide.
[So] Source:Biochem Biophys Res Commun;493(2):879-886, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microglial priming is caused by aging and neurodegenerative diseases, and is characterized by an exaggerated microglial inflammatory response to secondary and sub-threshold challenges. In the present study, we examined the effects of the matrix metalloproteinase-8 (MMP-8) inhibitor (M8I) on the brain of aged normal and leucine-rich repeat kinase 2 (LRRK2) G2019S Parkinson's disease (PD) model mice systemically stimulated with lipopolysaccharide (LPS). The results indicated that Iba-1 positive microglia and GFAP-positive astrocytes, which were increased by LPS, significantly decreased by M8I in aged normal and PD model mice. M8I also decreased the expression of pro-inflammatory markers in the hippocampus and midbrain of aged normal and PD model mice challenged with LPS, while it also improved the motor coordination of aged normal mice after LPS challenge in rotor rod test and the general crossing locomotor activities of LPS-treated LRRK2G2019S PD mice after LPS challenge in open field test. To assess the effects of M8I in an in vitro priming model, BV2 microglia were pretreated with macrophage colony-stimulating factor (CSF)-1 or interleukin (IL)-34, and subsequently stimulated with LPS or polyinosinic-polycytidylic acid (poly[I:C]). M8I inhibited the LPS- or poly(I:C)-induced production of the tumor necrosis factor-α and nitric oxide, alone or in combination with CSF-1 or IL-34. Collectively, the data suggested that M8I has a therapeutic potential in treating neurodegenerative diseases that are aggravated by systemic inflammation.
[Mh] Termos MeSH primário: Anti-Inflamatórios/uso terapêutico
Inflamação/tratamento farmacológico
Lipopolissacarídeos/imunologia
Metaloproteinase 8 da Matriz/imunologia
Inibidores de Metaloproteinases de Matriz/uso terapêutico
Microglia/efeitos dos fármacos
Doença de Parkinson/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Inflamação/genética
Inflamação/imunologia
Inflamação/patologia
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/genética
Locomoção/efeitos dos fármacos
Camundongos
Camundongos Transgênicos
Microglia/imunologia
Microglia/patologia
NF-kappa B/imunologia
Óxido Nítrico/imunologia
Doença de Parkinson/genética
Doença de Parkinson/imunologia
Doença de Parkinson/patologia
Mutação Puntual
Fator de Necrose Tumoral alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Lipopolysaccharides); 0 (Matrix Metalloproteinase Inhibitors); 0 (NF-kappa B); 0 (Tumor Necrosis Factor-alpha); 31C4KY9ESH (Nitric Oxide); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 3.4.24.34 (Matrix Metalloproteinase 8)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE


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[PMID]:28860188
[Au] Autor:Scannevin RH; Alexander R; Haarlander TM; Burke SL; Singer M; Huo C; Zhang YM; Maguire D; Spurlino J; Deckman I; Carroll KI; Lewandowski F; Devine E; Dzordzorme K; Tounge B; Milligan C; Bayoumy S; Williams R; Schalk-Hihi C; Leonard K; Jackson P; Todd M; Kuo LC; Rhodes KJ
[Ad] Endereço:From Janssen Research and Development, LLC, Spring House, Pennsylvania 19477 rscannevin@yumanity.com.
[Ti] Título:Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation.
[So] Source:J Biol Chem;292(43):17963-17974, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aberrant activation of matrix metalloproteinases (MMPs) is a common feature of pathological cascades observed in diverse disorders, such as cancer, fibrosis, immune dysregulation, and neurodegenerative diseases. MMP-9, in particular, is highly dynamically regulated in several pathological processes. Development of MMP inhibitors has therefore been an attractive strategy for therapeutic intervention. However, a long history of failed clinical trials has demonstrated that broad-spectrum MMP inhibitors have limited clinical utility, which has spurred the development of inhibitors selective for individual MMPs. Attaining selectivity has been technically challenging because of sequence and structural conservation across the various MMPs. Here, through a biochemical and structural screening paradigm, we have identified JNJ0966, a highly selective compound that inhibited activation of MMP-9 zymogen and subsequent generation of catalytically active enzyme. JNJ0966 had no effect on MMP-1, MMP-2, MMP-3, MMP-9, or MMP-14 catalytic activity and did not inhibit activation of the highly related MMP-2 zymogen. The molecular basis for this activity was characterized as an interaction of JNJ0966 with a structural pocket in proximity to the MMP-9 zymogen cleavage site near Arg-106, which is distinct from the catalytic domain. JNJ0966 was efficacious in reducing disease severity in a mouse experimental autoimmune encephalomyelitis model, demonstrating the viability of this therapeutic approach. This discovery reveals an unprecedented pharmacological approach to MMP inhibition, providing an opportunity to improve selectivity of future clinical drug candidates. Targeting zymogen activation in this manner may also allow for pharmaceutical exploration of other enzymes previously viewed as intractable drug targets.
[Mh] Termos MeSH primário: Precursores Enzimáticos/antagonistas & inibidores
Precursores Enzimáticos/química
Metaloproteinase 9 da Matriz/química
Inibidores de Metaloproteinases de Matriz/química
[Mh] Termos MeSH secundário: Regulação Alostérica
Animais
Células COS
Domínio Catalítico
Cercopithecus aethiops
Precursores Enzimáticos/genética
Precursores Enzimáticos/metabolismo
Seres Humanos
Metaloproteinase 9 da Matriz/genética
Metaloproteinase 9 da Matriz/metabolismo
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Precursors); 0 (Matrix Metalloproteinase Inhibitors); EC 3.4.24.- (pro-matrix metalloproteinase 9); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.806075


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[PMID]:28826677
[Au] Autor:Caria CREP; Gotardo ÉMF; Santos PS; Acedo SC; de Morais TR; Ribeiro ML; Gambero A
[Ad] Endereço:Clinical Pharmacology and Gastroenterology Unit, São Francisco University Medical School, Bragança Paulista, SP 12916-900, Brazil. Electronic address: cintiarabello@yahoo.com.br.
[Ti] Título:Extracellular matrix remodeling and matrix metalloproteinase inhibition in visceral adipose during weight cycling in mice.
[So] Source:Exp Cell Res;359(2):431-440, 2017 Oct 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extracellular matrix (ECM) remodeling is necessary for a health adipose tissue (AT) expansion and also has a role during weight loss. We investigate the ECM alteration during weight cycling (WC) in mice and the role of matrix metalloproteinases (MMPs) was assessed using GM6001, an MMP inhibitor, during weight loss (WL). Obesity was induced in mice by a high-fat diet. Obese mice were subject to caloric restriction for WL followed by reintroduction to high-fat diet for weight regain (WR), resulting in a WC protocol. In addition, mice were treated with GM6001 during WL period and the effects were observed after WR. Activity and expression of MMPs was intense during WL. MMP inhibition during WL results in inflammation and collagen content reduction. MMP inhibition during WL period interferes with the period of subsequent expansion of AT resulting in improvements in local inflammation and systemic metabolic alterations induced by obesity. Our results suggest that MMPs inhibition could be an interesting target to improve adipose tissue inflammation during WL and to support weight cyclers.
[Mh] Termos MeSH primário: Dipeptídeos/farmacologia
Matriz Extracelular/metabolismo
Gordura Intra-Abdominal/metabolismo
Inibidores de Metaloproteinases de Matriz/farmacologia
Obesidade/enzimologia
[Mh] Termos MeSH secundário: Animais
Restrição Calórica
Colágeno/genética
Colágeno/metabolismo
Dieta Hiperlipídica/efeitos adversos
Metabolismo Energético
Matriz Extracelular/efeitos dos fármacos
Expressão Gênica
Inflamação/prevenção & controle
Gordura Intra-Abdominal/efeitos dos fármacos
Metabolismo dos Lipídeos/efeitos dos fármacos
Masculino
Metaloproteinase 12 da Matriz/genética
Metaloproteinase 12 da Matriz/metabolismo
Metaloproteinase 2 da Matriz/genética
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 3 da Matriz/genética
Metaloproteinase 3 da Matriz/metabolismo
Metaloproteinase 8 da Matriz/genética
Metaloproteinase 8 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/genética
Metaloproteinase 9 da Matriz/metabolismo
Camundongos
Obesidade/etiologia
Obesidade/genética
Obesidade/patologia
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Ganho de Peso/efeitos dos fármacos
Perda de Peso/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Matrix Metalloproteinase Inhibitors); 0 (N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide); 0 (Protein Isoforms); 9007-34-5 (Collagen); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.17 (Mmp3 protein, mouse); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.24 (Mmp2 protein, mouse); EC 3.4.24.34 (MMP8 protein, mouse); EC 3.4.24.34 (Matrix Metalloproteinase 8); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.4.24.35 (Mmp9 protein, mouse); EC 3.4.24.65 (Matrix Metalloproteinase 12); EC 3.4.24.65 (matrix metallopeptidase 12, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE


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[PMID]:28756264
[Au] Autor:Huang RZ; Liang GB; Huang XC; Zhang B; Zhou MM; Liao ZX; Wang HS
[Ad] Endereço:Pharmaceutical Research Center and School of Chemistry and Chemical Engineering, Southeast University, Nanjing 211189, China.
[Ti] Título:Discovery of dehydroabietic acid sulfonamide based derivatives as selective matrix metalloproteinases inactivators that inhibit cell migration and proliferation.
[So] Source:Eur J Med Chem;138:979-992, 2017 Sep 29.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:A series of dehydroabietic acid (DHAA) dipeptide derivatives containing the sulfonamide moiety were designed, synthesized and evaluated for inhibition of MMPs as well as the effects of in vitro cell migration. These compounds exhibited relatively good inhibition activity against MMPs with IC values in low micromolar range. A docking study of the most active compound 8k revealed key interactions between 8k and MMP-3 in which the sulfonamide moiety and the dipeptide group were important for improving activity. It is noteworthy that further antitumor activity screening revealed that some compounds exhibited better inhibitory activity than the commercial anticancer drug 5-FU. In particular, compound 8k appeared to be the most potent compound against the HepG2 cell line, at least partly, by inhibition of the activity of MMP-3 and apoptosis induction. The treatment of HepG2 cells with compound 8k resulted in inhibition of in vitro cell migration through wound healing assay and G1 phase of cell cycle arrested. In addition, 8k-induced apoptosis was significantly facilitated in HepG2 cells. Thus, we conclude that DHAA dipeptide derivatives containing the sulfonamide moiety may be the potential MMPs inhibitors with the ability to suppress cells migration.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Diterpenos Abietanos/farmacologia
Descoberta de Drogas
Inibidores de Metaloproteinases de Matriz/farmacologia
Metaloproteinases da Matriz/metabolismo
Sulfonamidas/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos/síntese química
Antineoplásicos/química
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Diterpenos Abietanos/síntese química
Diterpenos Abietanos/química
Relação Dose-Resposta a Droga
Ensaios de Seleção de Medicamentos Antitumorais
Seres Humanos
Inibidores de Metaloproteinases de Matriz/síntese química
Inibidores de Metaloproteinases de Matriz/química
Simulação de Acoplamento Molecular
Estrutura Molecular
Relação Estrutura-Atividade
Sulfonamidas/síntese química
Sulfonamidas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Diterpenes, Abietane); 0 (Matrix Metalloproteinase Inhibitors); 0 (Sulfonamides); 0S5XP6S3AU (dehydroabietic acid); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE


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[PMID]:28739306
[Au] Autor:Wang XW; Liu JJ; Wu QN; Wu SF; Hao DJ
[Ad] Endereço:Department of Spine Surgery, Honghui Hospital, Xi'an Jiaotong University, Xi'an 710054, PR China.
[Ti] Título:The in vitro and in vivo effects of microRNA-133a on intervertebral disc destruction by targeting MMP9 in spinal tuberculosis.
[So] Source:Life Sci;188:198-205, 2017 Nov 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: We aim to investigate the role of microRNA-133a (miR-133a) in intervertebral disc destruction by targeting MMP9 in spinal tuberculosis (TB). MAIN METHODS: Rabbit models with spinal TB were established and assigned to the blank, miR-133a mimic, miR-133a inhibitor and negative control (NC) groups. Primary notochordal cells were extracted and separately transfected with miR-133a mimics, miR-133a inhibitor, miR-nonsense sequence control (NC), si-NC and si-MMP9. QRT-PCR and Western blot assay were used to detect the expression of MMP-9, Collagen I, Collagen II and Collagen-X. Gelatin Zymography was performed to detect MMP9 activity. Immunohistochemistry was used to detect the expression of Collagen I, Collagen II and Collagen-X proteins. Osteoclast morphology and the number of osteoclast cells were observed after Tartrate resistant acid phosphatase staining. KEY FINDINGS: MMP9, Collagen-X and Collagen I expression and MMP9 activity were higher while the expression of Collagen II was lower in the miR-133a mimic group than the miR-NC group. MMP9, Collagen-X Collagen I and MMP9 activities were lower and Collagen II expression was higher in the miR-133a inhibitor group than the miR-NC group. Compared with the si-NC group, the si-MMP9 group showed increased Collagen II expression but decreased expression of MMP9, Collagen-X and Collagen I and MMP9 activity. A reduced amount of osteoclast cells exhibited in the miR-133a mimic group while an increased number was seen in the miR-133a inhibitor group compared to the blank group. SIGNIFICANCE: MiR-133a could inhibit Collagen degradation by down-regulating MMP-9 expression to attenuate the destructive effects of spinal TB on intervertebral disc.
[Mh] Termos MeSH primário: Regulação para Baixo
Regulação Enzimológica da Expressão Gênica
Disco Intervertebral/metabolismo
Disco Intervertebral/patologia
Metaloproteinase 9 da Matriz/biossíntese
Metaloproteinase 9 da Matriz/genética
MicroRNAs/genética
[Mh] Termos MeSH secundário: Animais
Contagem de Células
Colágeno/biossíntese
Feminino
Disco Intervertebral/enzimologia
Masculino
Inibidores de Metaloproteinases de Matriz
MicroRNAs/agonistas
MicroRNAs/antagonistas & inibidores
Osteoclastos/patologia
Osteoclastos/fisiologia
RNA Interferente Pequeno/agonistas
RNA Interferente Pequeno/antagonistas & inibidores
RNA Interferente Pequeno/genética
Coelhos
Tuberculose da Coluna Vertebral/metabolismo
Tuberculose da Coluna Vertebral/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN133 microRNA, human); 0 (Matrix Metalloproteinase Inhibitors); 0 (MicroRNAs); 0 (RNA, Small Interfering); 9007-34-5 (Collagen); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  8 / 4741 MEDLINE  
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[PMID]:28722301
[Au] Autor:Xie XW; Wan RZ; Liu ZP
[Ad] Endereço:Institute of Medicinal Chemistry, Key Laboratory of Chemical Biology (Ministry of Education), School of Pharmaceutical Sciences, Shandong University, Jinan, 250012, P.R. China.
[Ti] Título:Recent Research Advances in Selective Matrix Metalloproteinase-13 Inhibitors as Anti-Osteoarthritis Agents.
[So] Source:ChemMedChem;12(15):1157-1168, 2017 Aug 08.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Matrix metalloproteinase-13 (MMP-13) plays a key role in the degradation of type II collagen in cartilage and bone in osteoarthritis (OA). The subtle differences between the S1' loop of MMP-13 and that of other MMPs offer a structural base for the design of selective MMP-13 inhibitors to mitigate the unperceived risk associated with inhibiting other MMP isoforms. In this review, we summarize zinc-binding and non-zinc-binding selective MMP-13 inhibitors. The zinc-binding MMP-13 inhibitors contain a small set of zinc-binding groups (ZBGs), including hydroxamic acid, pyrimidinetrione, reversed hydroxamic acid and hydantoin, carboxylic acid, 1,2,4,-triazole, and 1,2,4,-triazolone. The non-zinc-binding MMP-13 inhibitors have different structural scaffolds, including diphenyl ethers, biaryls (aryltetrazoliums, arylfurans, pyrazole-indoles), pyrimidines, and aryl/cycloalkyl-fused pyrimidines. This review provides a systematic overview of recent developments in MMP-13 inhibitors for the treatment of OA, with emphasis on their enzyme inhibitory potency, selectivity, and biological activities, and highlights the various binding modes of typical inhibitors with MMP-13.
[Mh] Termos MeSH primário: Metaloproteinase 13 da Matriz/metabolismo
Inibidores de Metaloproteinases de Matriz/farmacologia
Osteoartrite/tratamento farmacológico
[Mh] Termos MeSH secundário: Seres Humanos
Inibidores de Metaloproteinases de Matriz/síntese química
Inibidores de Metaloproteinases de Matriz/química
Inibidores de Metaloproteinases de Matriz/metabolismo
Relação Estrutura-Atividade
Zinco/química
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Matrix Metalloproteinase Inhibitors); EC 3.4.24.- (MMP13 protein, human); EC 3.4.24.- (Matrix Metalloproteinase 13); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201700349


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[PMID]:28692737
[Au] Autor:Mohamed-Ahmed AHA; Lockwood A; Li H; Bailly M; Khaw PT; Brocchini S
[Ad] Endereço:UCL School of Pharmacy, London, United Kingdom 2UCL Institute of Ophthalmology, London, United Kingdom.
[Ti] Título:An Ilomastat-CD Eye Drop Formulation to Treat Ocular Scarring.
[So] Source:Invest Ophthalmol Vis Sci;58(9):3425-3431, 2017 Jul 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: The purpose of this study was to develop a topical matrix metalloproteinase inhibitor preparation for antiscarring therapy. Methods: The broad spectrum matrix metalloproteinase inhibitor ilomastat was formulated using 2-hydroxypropyl-ß-cyclodextrin in aqueous solution. In vitro activity of ilomastat-cyclodextrin (ilomastat-CD) was examined using fibroblasts seeded in collagen. Permeation of ilomastat-CD eye drop through pig eye conjunctiva was confirmed using Franz diffusion cells. Ilomastat-CD eye drop was applied to rabbit eyes in vivo, and the distribution of ilomastat in ocular tissues and fluids was determined by liquid chromatography-mass spectroscopy. Results: The aqueous solubility of ilomastat-CD was ∼1000 µg/mL in water and 1400 µg/mL in PBS (pH 7.4), which is greater than ilomastat alone (140 and 160 µg/mL in water and PBS, respectively). The in vitro activity of ilomastat-CD to inhibit collagen contraction in the presence of human Tenon fibroblast cells was unchanged compared to uncomplexed ilomastat. Topically administered ilomastat-CD in vivo to rabbit eyes resulted in a therapeutic concentration of ilomastat being present in the sclera and conjunctiva and within the aqueous humor. Conclusions: Ilomastat-CD has the potential to be formulated as an eye drop for use as an antifibrotic, which may have implications for the prevention of scarring in many settings, for example glaucoma filtration surgery.
[Mh] Termos MeSH primário: Cicatriz/tratamento farmacológico
Indóis/farmacologia
Inibidores de Metaloproteinases de Matriz/farmacologia
[Mh] Termos MeSH secundário: Animais
Humor Aquoso/metabolismo
Disponibilidade Biológica
Células Cultivadas
Colágeno/efeitos dos fármacos
Túnica Conjuntiva/metabolismo
Córnea
Fibroblastos/efeitos dos fármacos
Seres Humanos
Ácidos Hidroxâmicos
Indóis/química
Indóis/farmacocinética
Inibidores de Metaloproteinases de Matriz/química
Inibidores de Metaloproteinases de Matriz/farmacocinética
Soluções Oftálmicas
Esclera/metabolismo
Solubilidade
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydroxamic Acids); 0 (Indoles); 0 (Matrix Metalloproteinase Inhibitors); 0 (Ophthalmic Solutions); 9007-34-5 (Collagen); I0403ML141 (ilomastat)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.16-21377


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[PMID]:28682555
[Au] Autor:Lingling J; Qianbing W
[Ad] Endereço:State Key Laboratory of Oral Diseases, National Clinical Research Center for Oral Diseases, Dept. of Prosthetics, West China Hospital of Stomatology, Sichuan University, Chengdu 610041, China.
[Ti] Título:[Progress on matrix metalloproteinase inhibitors].
[So] Source:Hua Xi Kou Qiang Yi Xue Za Zhi;35(2):208-214, 2017 Apr 01.
[Is] ISSN:1000-1182
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Continuing advances in dentin bonding technology and adhesives revolutionized bonding of resin-based composite restorations. However, hybrid layers created by contemporary dentin adhesives present imperfect durability, and degradation of collagen matrix by endogenous enzymes is a significant factor causing destruction of hybrid layers. Bond durability can be improved by using enzyme inhibitors to prevent collagen degradation and to preserve integrity of collagen matrix. This review summarizes progress on matrix metalloproteinase inhibitors (including chlorhexidine, ethylenediaminetetraacetic acid, quaternary ammonium salt, tetracycline and its derivatives, hydroxamic acid inhibitors, bisphosphonate derivative, and cross-linking agents) and suggests prospects for these compounds.
[Mh] Termos MeSH primário: Adesivos Dentinários
Inibidores de Metaloproteinases de Matriz
[Mh] Termos MeSH secundário: Ataque Ácido Dentário
Bis-Fenol A-Glicidil Metacrilato
Colágeno
Colagem Dentária
Dentina
Seres Humanos
Metaloproteinase 2 da Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dentin-Bonding Agents); 0 (Foundation composite resin); 0 (Matrix Metalloproteinase Inhibitors); 454I75YXY0 (Bisphenol A-Glycidyl Methacrylate); 9007-34-5 (Collagen); EC 3.4.24.24 (Matrix Metalloproteinase 2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.7518/hxkq.2017.02.019



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