Database : MEDLINE
Search on : Collagenases [Words]
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[PMID]: 29267658
[Au] Autor:Ferrúa CP; Centeno EGZ; Rosa LCD; Amaral CCD; Severo RF; Sarkis-Onofre R; Nascimento GG; Cordenonzi G; Bast RK; Demarco FF; Nedel F
[Ad] Address:Universidade Católica de Pelotas - UCPel, Program in Health and Behavior, Pelotas, RS, Brazil.
[Ti] Title:How has dental pulp stem cells isolation been conducted? A scoping review.
[So] Source:Braz Oral Res;31:e87, 2017 Dec 18.
[Is] ISSN:1807-3107
[Cp] Country of publication:Brazil
[La] Language:eng
[Ab] Abstract:The objective of this study was to realize a scoping review the literature in order to identify the profile of DPSCs isolation and analyze the possible risk factors that could change the native behavior of these cells. An initial search was conducted using the following MeSH terms: "(dental pulp stem cell [MeSH])"; "(dental pulp [MeSH])" AND "(stem cell [MeSH])"; "("dental pulp stem cell" [MeSH]")". The electronic search was done without date restriction up to and including April 2014, in PubMed, Scopus, Scielo and ISI Web of Knowledge databases. Studies were submitted to inclusion and exclusion criteria and 222 articles were included. Data showed that over the past 15 years many studies have been conducted using DPSCs. However this is the first systematic review regarding the isolation of stem cell, and more specifically of dental pulp stem cells. The isolation of dental pulp stem cells showed great variability, hampering the development of standard protocols to achieve in vitro dental pulp stem cells with similar characteristics. This scoping review combined, for the first time, the methodologies used for dental pulp stem isolation, highlighting the most frequently used.
[Mh] MeSH terms primary: Dental Pulp/cytology
Stem Cells/cytology
[Mh] MeSH terms secundary: Cell Culture Techniques
Collagenases
Culture Media
Humans
Publication Bias
Risk Factors
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Culture Media); EC 3.4.24.- (Collagenases)
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[Js] Journal subset:D; IM
[Da] Date of entry for processing:171222
[St] Status:MEDLINE

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[PMID]: 29485268
[Au] Autor:Kany AM; Sikandar A; Haupenthal J; Yahiaoui S; Maurer CK; Proschak E; Köhnke J; Hartmann RW
[Ad] Address:Department of Drug Design and Optimization , Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) , Campus E8.1 , 66123 , Saarbrücken , Germany.
[Ti] Title:Binding Mode Characterization and Early in Vivo Evaluation of Fragment-Like Thiols as Inhibitors of the Virulence Factor LasB from Pseudomonas aeruginosa.
[So] Source:ACS Infect Dis;, 2018 Mar 06.
[Is] ISSN:2373-8227
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The increasing emergence of antibiotic resistance necessitates the development of anti-infectives with novel modes of action. Targeting bacterial virulence is considered a promising approach to develop novel antibiotics with reduced selection pressure. The extracellular collagenase elastase (LasB) plays a pivotal role in the infection process of Pseudomonas aeruginosa and therefore represents an attractive antivirulence target. Mercaptoacetamide-based thiols have been reported to inhibit LasB as well as collagenases from clostridia and bacillus species. The present work provides an insight into the structure-activity relationship (SAR) of these fragment-like LasB inhibitors, demonstrating an inverse activity profile compared to similar inhibitors of clostridial collagenase H (ColH). An X-ray cocrystal structure is presented, revealing distinct binding of two compounds to the active site of LasB, which unexpectedly maintains an open conformation. We further demonstrate in vivo efficacy in a Galleria mellonella infection model and high selectivity of the LasB inhibitors toward human matrix metalloproteinases (MMPs).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher
[do] DOI:10.1021/acsinfecdis.8b00010

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[PMID]: 29366749
[Au] Autor:Gonzalez EA; Martins GR; Tavares AMV; Viegas M; Poletto E; Giugliani R; Matte U; Baldo G
[Ad] Address:Gene Therapy Center, Hospital de Clínicas de Porto Alegre, Porto Alegre, Brazil; Post-Graduation Program in Genetics and Molecular Biology, UFRGS, Porto Alegre, Brazil.
[Ti] Title:Cathepsin B inhibition attenuates cardiovascular pathology in mucopolysaccharidosis I mice.
[So] Source:Life Sci;196:102-109, 2018 Mar 01.
[Is] ISSN:1879-0631
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Mucopolysaccharidosis type I (MPS I) is a lysosomal storage disorder with multisystemic features, including heart enlargement, heart valve dysfunction, and aortic stiffness and dilatation. Previous studies have shown that MPS I mice overexpress cathepsin B (CtsB) in multiple tissues, including those from the cardiovascular system. Here, we hypothesized that inhibition of CtsB could ameliorate cardiac function parameters, as well as aorta and valve abnormalities found in MPS I. First, we found that total elastase activity in an MPS I aorta is elevated. Following that, we demonstrated that CtsB leaks from the lysosome in MPS I human fibroblasts, possibly acting as a degradative agent of extracellular matrix components from the aorta, cardiac muscle, and heart valves. We then used a CtsB inhibitor in vivo in the MPS I mouse model. After 4 months of treatment, partial inhibition of CtsB activity in treated mice reduced aortic dilatation, as well as heart valve thickening, and led to improvements in cardiac function parameters, although none of these were completely normalized. Based on these results, we conclude that lysosomal alterations in this disease promote leakage of CtsB to outside the organelle, where this protein can have multiple pathological roles. CtsB inhibition improved cardiovascular parameters in MPS I mice and can have a potential benefit in this disease.
[Mh] MeSH terms primary: Cardiovascular System/pathology
Cathepsin B/antagonists & inhibitors
Cysteine Proteinase Inhibitors/therapeutic use
Dipeptides/therapeutic use
Mucopolysaccharidosis I/diagnostic imaging
Mucopolysaccharidosis I/drug therapy
[Mh] MeSH terms secundary: Animals
Aorta/pathology
Aorta/physiopathology
Cardiovascular System/diagnostic imaging
Cathepsin B/metabolism
Collagenases/metabolism
Female
Fibroblasts/metabolism
Heart Function Tests
Heart Valve Diseases/diagnostic imaging
Heart Valve Diseases/drug therapy
Heart Valve Diseases/pathology
Humans
Lysosomes/metabolism
Male
Mice
Mice, Inbred C57BL
Mucopolysaccharidosis I/pathology
Pancreatic Elastase/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Cysteine Proteinase Inhibitors); 0 (Dipeptides); 134448-10-5 (N-(3-propylcarbamoyloxirane-2-carbonyl)-isoleucyl-proline); EC 3.4.21.36 (Pancreatic Elastase); EC 3.4.22.1 (Cathepsin B); EC 3.4.24.- (Collagenases)
[Em] Entry month:1802
[Cu] Class update date: 180226
[Lr] Last revision date:180226
[Js] Journal subset:IM
[Da] Date of entry for processing:180126
[St] Status:MEDLINE

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[PMID]: 29460078
[Au] Autor:Madzuki IN; Lau SF; Che Ahmad Tantowi NA; Mohd Ishak NI; Mohamed S
[Ad] Address:UPM-MAKNA Laboratory of Cancer Research, Institute of Bioscience, Universiti Putra Malaysia UPM, 43400, Serdang, Malaysia.
[Ti] Title:Labisia pumila prevented osteoarthritis cartilage degeneration by attenuating joint inflammation and collagen breakdown in postmenopausal rat model.
[So] Source:Inflammopharmacology;, 2018 Feb 19.
[Is] ISSN:1568-5608
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:The tropical herb Labisia pumila is traditionally used in facilitating childbirth and post-partum care. The effects of L. pumila leaf extract (LP) in explant cartilage culture and on postmenopausal osteoarthritis (OA) rat model were assessed. The LP (10, 25 and 50 µg/ml) or diclofenac (10 µg/ml) was added to the cartilage explants containing bovine IL-1ß (20 ng/ml), to evaluate their direct effects on cartilage degradation. In the preclinical study, rats were grouped (n = 8) into: non-treated OA; OA + diclofenac (5 mg/kg); OA + LP extract (150 and 300 mg/kg); and healthy control. To induce OA, monosodium iodoacetate was injected into the ovariectomised female rats' intra-articular knee joints and evaluated for OA severity after 8 weeks via physical (radiological, macroscopic and histological observations), biochemical, ELISA and mRNA expression analysis (for inflammation and cartilage degradation biomarkers). The LP reduced the nitric oxide and proteoglycan release from the cartilage explants under IL-1ß induction. The radiological, macroscopic, microscopic and histological images showed the OA rats treated with LP and diclofenac had significantly reduced osteophytes and cartilage erosions compared to non-treated OA rats. The extract significantly up-regulated the anti-inflammatory interleukin-10, collagen type II and down-regulated pro-inflammatory PTGS2 (prostaglandin-endoperoxide synthase 2) mRNA expressions compared to non-treated control. The LP treatment significantly reduced serum collagenases (MMP-1 and MMP-3) and collagen type II degradation biomarker (CTX-II) levels in OA rats. The LP containing myricetin and gallic acid suppressed inflammation, collagenases and cartilage degradation, and helped cartilage matrix synthesis, to prevent OA at the dose equivalent to 30-60 mg/kg daily for humans.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180220
[Lr] Last revision date:180220
[St] Status:Publisher
[do] DOI:10.1007/s10787-018-0452-6

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[PMID]: 29444248
[Au] Autor:Takita T; Qian J; Geng H; He Z; Nemoto S; Mori M; Tanaka K; Hattori S; Kojima K; Yasukawa K
[Ad] Address:Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
[Ti] Title:Comparative studies on the activities of collagenases from Grimontia hollisae and Clostridium hystoliticum in the hydrolysis of synthetic substrates.
[So] Source:J Biochem;, 2018 Feb 10.
[Is] ISSN:1756-2651
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The collagenase produced by a gram-negative bacterium Grimontia hollisae strain 1706B (Ghcol) degrades collagen more efficiently than that produced by a gram-positive bacterium Clostridium histolyticum (Chcol), which is currently the most widely used collagenase in industry (Teramura et al. (2011) J. Bacteriol.193, 3049‒3056). Here, we compared the Ghcol and Chcol activities using two synthetic substrates. In the hydrolysis of (7-methoxycoumarin-4-yl)acetyl-L-Lys-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophen-yl)-L-2,3-diaminopropioyl]-L-Ala-L-Arg-NH2, Ghcol exhibited 350-fold higher activity than Chcol in the absence of CaCl2 and NaCl. The Ghcol activity markedly decreased with increasing concentrations of buffer, CaCl2, or NaCl, while the Chcol activity did not, suggesting that the Ghcol activity was sensitive to solvent components. In the hydrolysis of N-[3-(2-furyl)acryloyl]-L-Leu-Gly-L-Pro-Ala, Ghcol exhibited 16-fold higher activity than Chcol in the absence of CaCl2, and NaCl, and both enzyme activities did not decrease with increasing concentrations of buffer, CaCl2 or NaCl. pH dependences of activity revealed that the ionizable group responsible for acidic pKe may be Glu for Ghcol and Chcol, while that for alkaline pKe may be His for Ghcol and Tyr for Chcol. These striking differences suggest that the catalytic mechanism of Ghcol might be considerably different from that of clostridial collagenases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180214
[Lr] Last revision date:180214
[St] Status:Publisher
[do] DOI:10.1093/jb/mvy009

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[PMID]: 29281816
[Au] Autor:Madsen DH; Jürgensen HJ; Siersbæk MS; Kuczek DE; Grey Cloud L; Liu S; Behrendt N; Grøntved L; Weigert R; Bugge TH
[Ad] Address:Proteases and Tissue Remodeling Section , Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA; Center for Cancer Immune Therapy, Department of Haematology, Copenhagen University Hospital, 2730 Herlev, Denma
[Ti] Title:Tumor-Associated Macrophages Derived from Circulating Inflammatory Monocytes Degrade Collagen through Cellular Uptake.
[So] Source:Cell Rep;21(13):3662-3671, 2017 Dec 26.
[Is] ISSN:2211-1247
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Physiologic turnover of interstitial collagen is mediated by a sequential pathway in which collagen is fragmented by pericellular collagenases, endocytosed by collagen receptors, and routed to lysosomes for degradation by cathepsins. Here, we use intravital microscopy to investigate if malignant tumors, which are characterized by high rates of extracellular matrix turnover, utilize a similar collagen degradation pathway. Tumors of epithelial, mesenchymal, or neural crest origin all display vigorous endocytic collagen degradation. The cells engaged in this process are identified as tumor-associated macrophage (TAM)-like cells that degrade collagen in a mannose receptor-dependent manner. Accordingly, mannose-receptor-deficient mice display increased intratumoral collagen. Whole-transcriptome profiling uncovers a distinct extracellular matrix-catabolic signature of these collagen-degrading TAMs. Lineage-ablation studies reveal that collagen-degrading TAMs originate from circulating CCR2+ monocytes. This study identifies a function of TAMs in altering the tumor microenvironment through endocytic collagen turnover and establishes macrophages as centrally engaged in tumor-associated collagen degradation.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180210
[Lr] Last revision date:180210
[St] Status:In-Data-Review

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[PMID]: 29374192
[Au] Autor:Das A; Datta S; Roche E; Chaffee S; Jose E; Shi L; Grover K; Khanna S; Sen CK; Roy S
[Ad] Address:Department of Surgery, Center for Regenerative Medicine and Cell Based Therapies and Comprehensive Wound Center, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
[Ti] Title:Novel mechanisms of Collagenase Santyl Ointment (CSO) in wound macrophage polarization and resolution of wound inflammation.
[So] Source:Sci Rep;8(1):1696, 2018 Jan 26.
[Is] ISSN:2045-2322
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Collagenases are useful in enzymatic wound debridement. Clostridial collagenase, marketed as Collagenase Santyl Ointment (CSO), is FDA approved for such use. Building on the scientific premise that collagenases as well as collagen degradation products may regulate immune cell function, we sought to investigate the potential role of CSO in wound inflammation. We tested the hypothesis that in addition to enacting debridement, CSO contributes to the resolution of persistent wound inflammation. Wound macrophages were isolated from PVA sponges loaded with CSO or petrolatum and implanted in mice. Significant increase in pro-reparative and decrease in pro-inflammatory polarization was noted in macrophages of acute as well as diabetic wounds. Wound macrophages from CSO-treated group displayed increased production of anti-inflammatory cytokines IL-10 and TGF-ß, and decreased levels of pro-inflammatory cytokines TNF-α and IL-1ß. The active ingredient of CSO, CS-API, induced the expression of mÏ• /M(IL-4) polarization markers ex vivo. CS-API treatment attenuated transactivation of NF-κB and significantly induced STAT6 phosphorylation. A significant role of a novel PGE2-EP4 pathway in CS-API induced STAT6 activation and the mÏ• /M(IL-4) polarization was identified. Taken together, findings of this work reposition CSO as a potential agent that may be effective in resolving wound inflammation, including diabetic wounds.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180209
[Lr] Last revision date:180209
[St] Status:In-Data-Review
[do] DOI:10.1038/s41598-018-19879-w

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[PMID]: 27771138
[Au] Autor:Hiraishi N; Maruno T; Tochio N; Sono R; Otsuki M; Takatsuka T; Tagami J; Kobayashi Y
[Ad] Address:Cariology and Operative Dentistry, Department of Oral Health Sciences, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan. Electronic address: hiraope@tmd.ac.jp.
[Ti] Title:Hesperidin interaction to collagen detected by physico-chemical techniques.
[So] Source:Dent Mater;33(1):33-42, 2017 01.
[Is] ISSN:1879-0097
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVE: Dentin collagen can be modified by some plant-derived flavonoids to improve properties of dentin organic matrix. Hesperidin (HPN), a hesperetin-7-O-rutinoside flavonoid, has a potential of dentin modification for being based on evidence that a treatment with HPN may resist collagenase degradation and arrest demineralization of human dentin. In this study, biophysical and molecular-level information on the interaction of HPN and collagen was investigated. METHODS: HPN is extracted from citrus fruits. Sample collagenous solution was prepared using atelocollagen (ATCL) as a triple-helical peptide model. We have performed circular dichroism spectroscopic analysis, sedimentation velocity measurement by ultracentrifuge and saturation transfer difference measurement (STD) by NMR on HPN-collagen in solution state. RESULTS: The circular dichroism and sedimentation velocity measurement showed the evidence for the molecular interaction between ATCL and HPN, while HPN did not induce any conformational change of ATCL. The STD-NMR study further confirmed this interaction and suggested that HPN interacted with ATCL through its aromatic part, not through its disaccharide moiety. SIGNIFICANCE: These findings indicated that HPN is weakly bound to ATCL not causing structural modification of collagen. This interaction may contribute to the preservation of collagen by protecting from collagenase degradation.
[Mh] MeSH terms primary: Collagen/metabolism
Dentin/metabolism
Hesperidin/pharmacology
[Mh] MeSH terms secundary: Collagenases/metabolism
Humans
Magnetic Resonance Spectroscopy
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:9007-34-5 (Collagen); E750O06Y6O (Hesperidin); EC 3.4.24.- (Collagenases)
[Em] Entry month:1801
[Cu] Class update date: 180201
[Lr] Last revision date:180201
[Js] Journal subset:D
[Da] Date of entry for processing:161025
[St] Status:MEDLINE

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[PMID]: 29310800
[Au] Autor:Wang X; Khalil RA
[Ad] Address:Vascular Surgery Research Laboratories, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, United States.
[Ti] Title:Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease.
[So] Source:Adv Pharmacol;81:241-330, 2018.
[Is] ISSN:1557-8925
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade various proteins in the extracellular matrix (ECM). Typically, MMPs have a propeptide sequence, a catalytic metalloproteinase domain with catalytic zinc, a hinge region or linker peptide, and a hemopexin domain. MMPs are commonly classified on the basis of their substrates and the organization of their structural domains into collagenases, gelatinases, stromelysins, matrilysins, membrane-type (MT)-MMPs, and other MMPs. MMPs are secreted by many cells including fibroblasts, vascular smooth muscle (VSM), and leukocytes. MMPs are regulated at the level of mRNA expression and by activation through removal of the propeptide domain from their latent zymogen form. MMPs are often secreted in an inactive proMMP form, which is cleaved to the active form by various proteinases including other MMPs. MMPs degrade various protein substrates in ECM including collagen and elastin. MMPs could also influence endothelial cell function as well as VSM cell migration, proliferation, Ca signaling, and contraction. MMPs play a role in vascular tissue remodeling during various biological processes such as angiogenesis, embryogenesis, morphogenesis, and wound repair. Alterations in specific MMPs could influence arterial remodeling and lead to various pathological disorders such as hypertension, preeclampsia, atherosclerosis, aneurysm formation, as well as excessive venous dilation and lower extremity venous disease. MMPs are often regulated by endogenous tissue inhibitors of metalloproteinases (TIMPs), and the MMP/TIMP ratio often determines the extent of ECM protein degradation and tissue remodeling. MMPs may serve as biomarkers and potential therapeutic targets for certain vascular disorders.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180114
[Lr] Last revision date:180114
[St] Status:In-Data-Review

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[PMID]: 29317799
[Au] Autor:Wong K; Trudel G; Laneuville O
[Ad] Address:Bone and Joint Research Laboratory, The Ottawa Hospital Rehabilitation Centre, Ottawa, Ontario.
[Ti] Title:Intra-articular collagenase injection increases range of motion in a rat knee flexion contracture model.
[So] Source:Drug Des Devel Ther;12:15-24, 2018.
[Is] ISSN:1177-8881
[Cp] Country of publication:New Zealand
[La] Language:eng
[Ab] Abstract:Objectives: A knee joint contracture, a loss in passive range of motion (ROM), can be caused by prolonged immobility. In a rat knee immobilization flexion contracture model, the posterior capsule was shown to contribute to an irreversible limitation in ROM, and collagen pathways were identified as differentially expressed over the development of a contracture. Collagenases purified from are currently prescribed to treat Dupuytren's and Peyronie's contractures due to their ability to degrade collagen. The potential application of collagenases to target collagen in the posterior capsule was tested in this model. Materials and methods: Rats had one hind leg immobilized, developing a knee flexion contracture. After 4 weeks, the immobilization device was removed, and the rats received one 50 µL intra-articular injection of 0.6 mg/mL purified collagenase. Control rats were injected with only the buffer. After 2 weeks of spontaneous remobilization following the injections, ROM was measured with a rat knee arthrometer, and histological sections were immunostained with antibodies against rat collagen types I and III. Results/conclusion: Compared with buffer-injected control knees, collagenase-treated knees showed increased ROM in extension by 8.0°±3.8° ( -value <0.05). Immunohistochemical analysis revealed an increase in collagen type III staining ( <0.01) in the posterior capsule of collagenase-treated knees indicating an effect on the extracellular matrix due to the collagenase. Collagen I staining was unchanged ( >0.05). The current study provides experimental evidence for the pharmacological treatment of knee flexion contractures with intra-articular collagenase injection, improving the knee ROM.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180112
[Lr] Last revision date:180112
[St] Status:In-Process
[do] DOI:10.2147/DDDT.S144602


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