Matrix metalloproteinases in stroke

2017 ◽  
pp. 110-117
Author(s):  
А.А. Пальцын
Keyword(s):  
Matrix Metalloproteinases ◽  
Enzyme System ◽  
Enzyme Complex ◽  
Pathogenic Factors ◽  
Pathogenic Action ◽  
Activity Of Enzymes ◽  
Living Tissues ◽  
Current Reconstruction ◽  
Metalloproteinase Activity

Матриксные металлопротеиназы - ферментный комплекс, необходимый для сохранения гомеостаза. Он участник нормальной, постоянно текущей реконструкции всех живых тканей. Действие патогенных факторов нарушает слаженную работу этого комплекса. Часто нарушение выражается излишней активностью ферментов, усиливающей патогенное действие. Однако и заживление, форсированное новообразование тканевых элементов, может происходить только при повышенной, в сравнении с нормой, активности металлопротеиназ. Такая ситуация требует от медицины умения разумно вмешиваться в работу ферментной системы. В статье представлены некоторые результаты этих вмешательств. Matrix metalloproteinases - enzyme complex necessary for maintenance of the homeostasis. He is a participant of normal, constantly current reconstruction of all living tissues. Action of pathogenic factors breaks harmonious work of this complex. Often violation is expressed by the excessive activity of enzymes amplifying pathogenic action. However and healing, which is accelerated new growth of tissue elements, can happen only at raised, compared with norm, metalloproteinase activity. Such situation demands from medicine of ability participate reasonably in work of enzyme system. The article presents some of the results of these actions.

Matrix metalloproteinases, inflammation and atherosclerosis: therapeutic perspectives

2004 ◽  
Vol 42 (2) ◽  
Author(s):  
Jean-Louis Beaudeux ◽  
Philippe Giral ◽  
Eric Bruckert ◽  
Marie-José Foglietti ◽  
M. John Chapman
Keyword(s):  
Matrix Metalloproteinases ◽  
Atherosclerotic Lesion ◽  
Left Ventricular ◽  
Vascular Pathology ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Tissue Remodelling ◽  
Plaque Instability ◽  
Plaque Disruption ◽  
Extracellular Matrix Remodelling ◽  
Metalloproteinase Activity

AbstractMatrix metalloproteinases (MMPs), also called matrixins, are proteinases that participate in extracellular matrix remodelling and degradation. Under normal physiological conditions, the activities of MMPs are precisely regulated at the level of transcription, of activation of the pro-MMP precursor zymogens and of inhibition by endogenous inhibitors (tissue inhibitors of metalloproteinases; TIMPs). Alteration in the regulation of MMP activity is implicated in diseases such as cancer, fibrosis, arthritis and atherosclerosis. The pathological effects of MMPs and TIMPs in cardiovascular diseases involve vascular remodelling, atherosclerotic plaque instability and left ventricular remodelling after myocardial infarction. Since excessive tissue remodelling and increased matrix metalloproteinase activity have been demonstrated during atherosclerotic lesion progression (including plaque disruption), MMPs represent a potential target for therapeutic intervention aimed at modification of vascular pathology by restoring the physiological balance between MMPs and TIMPs. This review describes the members of the MMP and TIMP families and discusses the structure, function and regulation of MMP activity; finally, pharmacological approaches to MMP inhibition are highlighted.

Preparation and Properties of Matrix-Supported Horseradish Peroxidase

1975 ◽  
Vol 53 (8) ◽  
pp. 868-874 ◽  
Author(s):  
Greg J. Bartling ◽  
Swaraj K. Chattopadhyay ◽  
Charles W. Barker ◽  
Harry D. Brown
Keyword(s):  
Horseradish Peroxidase ◽  
Chemical Synthesis ◽  
Enzyme Immobilization ◽  
Thermal Denaturation ◽  
Enzyme System ◽  
Nucleophilic Attack ◽  
Enzyme Complex ◽  
Ph Optimum ◽  
Enzyme Coupling ◽  
Substrate Kinetics

A new method of enzyme immobilization has been described using poly(4-methacryloxybenzoic acid) as the carrier. Activation of the polymer, prior to enzyme attachment, was achieved with N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline. The enzyme coupling step proceeded through nucleophilic attack by the protein on a mixed carbonic anhydride. The degree of polymer activation was determined by analysis for quinoline, a by-product of the reaction. The polymer–enzyme complex was compared to the enzyme in solution in terms of pH optimum, substrate kinetics, and thermal denaturation. Potential uses of the polymer–enzyme system in chemical synthesis of benzoquinone derivatives are discussed.

scholarly journals Cathepsin B: an alternative protease for the generation of an aggrecan ‘metalloproteinase’ cleavage neoepitope

1998 ◽  
Vol 335 (3) ◽  
pp. 491-494 ◽  
Author(s):  
John S. MORT ◽  
Marie-Claude MAGNY ◽  
Eunice R. LEE
Keyword(s):  
Matrix Metalloproteinases ◽  
Cysteine Protease ◽  
Cathepsin B ◽  
Cartilage Proteoglycan ◽  
Metalloproteinase Activity

Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment terminating in the residues VDIPEN. We show that the combined endo- and exopeptidase activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.

scholarly journals Features of the enzyme composition of Jerusalem artichoke tubers

2019 ◽  
Vol 21 (91) ◽  
pp. 14-19
Author(s):  
I. Bilenka ◽  
N. Lazarenko ◽  
O. Zolovska ◽  
Ya. Golinskaya
Keyword(s):  
Ascorbic Acid ◽  
Polyphenol Oxidase ◽  
Raw Materials ◽  
Enzyme System ◽  
Jerusalem Artichoke ◽  
Microwave Processing ◽  
Biologically Active ◽  
Ascorbate Oxidase ◽  
Activity Of Enzymes ◽  
Active Substances

The article deals with different methods of preparing Jerusalem artichoke tubers to stabilize the color of semi-finished products and finished products. The varieties Interés and Violet de Rennes were chosen as objects of study. The purpose of this work is to study the activity of the enzyme system of Jerusalem artichoke tubers, followed by the use of raw materials as an ingredient in the preparation of culinary dishes with high nutritional and biological value. In accordance with the objective, the characteristics of the enzymatic composition of the material under study were researched. It was found that of the oxidoreductases present, the most active enzyme is polyphenol oxidase. It has been established that in the tubers of Jerusalem artichoke, the activity of polyphenol oxidase is in 1.8 times lower, peroxidase – in 1.34 times higher; ascorbate oxidase is in 2.79 times higher than that of Violet de Rennes tubers. A comparative analysis was performed on the reduction of the activity of enzymes and the preservation of the mass fraction of L-ascorbic acid in heat treatment and microwave processing. It has been established that the most successful method of treating Jerusalem artichoke tubers in order to inactivate the enzyme system and to preserve L-ascorbic acid is a microwave processing of 600 W in 1 minute. Studies have shown that with such preparation, the semi-finished product does not change color, the activity of the enzyme polyphenol oxidase decreases by 20 times, and the maintenance of the content of L-ascorbic acid is 68.4%. In further studies, it is important to study the technologies for preparing culinary dishes based on Jerusalem artichoke tubers using the results obtained to stabilize the color and preserve the biologically active substances of the raw materials.

scholarly journals Cannabidiol Decreases Metalloproteinase Activity and Normalizes Angiogenesis Factor Expression in UVB-Irradiated Keratinocytes from Psoriatic Patients

2021 ◽  
Vol 2021 ◽  
pp. 1-11
Author(s):  
Agnieszka Gęgotek ◽  
Sinemyiz Atalay ◽  
Adam Wroński ◽  
Agnieszka Markowska ◽  
Elżbieta Skrzydlewska
Keyword(s):  
Matrix Metalloproteinases ◽  
Psoriasis Vulgaris ◽  
Activity Levels ◽  
Skin Cells ◽  
Factor Expression ◽  
Basal Plasma ◽  
Angiopoietin 2 ◽  
Chemiluminescent Method ◽  
Metalloproteinase Activity

The development of psoriasis is associated with the consequences of oxidative stress and inflammation leading to metabolic changes locally, in the skin cells, and systemically, in the blood. Therefore, the aim of this study was to analyze the effect of psoriasis vulgaris (PsV) and psoriatic arthritis (PsA) on the basal plasma/keratinocyte levels of matrix metalloproteinases (MMPs), tissue inhibitors of matrix metalloproteinases (TIMPs), and angiogenesis factors, as well as to evaluate the effect of CBD on these parameters in keratinocytes isolated from psoriatic/healthy individuals with and without in vitro irradiation by UVB. A quantitative chemiluminescent method of detection based on an ELISA protocol and zymography technique was used during analysis. It was shown that activity levels of MMP-9 and TIMP-2 in PsA plasma were higher than in PsV. Changes in the proteolytic activity were accompanied by an increase in markers of angiogenesis (angiopoietin-2, HGF, VEGF, TNFα, PDGF, FGF), where in the specific case of angiopoietin-2 and TNFα, the overexpression in PsV was significantly stronger than in PsA. CBD application to keratinocytes partially restored levels of MMP-1/2/3/7 and TIMP-1/2 (in an effect which was particularly enhanced by UVB irradiation), as well as levels of the examined angiogenic factors except TNFα (levels of which were increased in psoriatic keratinocytes and decreased in healthy keratinocytes). Presented results indicate that CBD may be suggested as an antiangiogenic factor that reduces the proinflammatory action of UVB in psoriatic keratinocytes and partially has a protective effect for healthy keratinocytes.

scholarly journals Mammalian aromatases

Reproduction ◽  
2001 ◽  
pp. 685-695 ◽  
Author(s):  
A Conley ◽  
M Hinshelwood
Keyword(s):  
Cytochrome P450 ◽  
Enzyme System ◽  
Well Being ◽  
Enzyme Complex ◽  
Specific Expression ◽  
Aromatase Expression ◽  
Important Species ◽  
Tissue Specific ◽  
Essential Components ◽  
Species Specific

Aromatase is the enzyme complex that catalyses the synthesis of oestrogens from androgens, and therefore it has unique potential to influence the physiological balance between the sex steroid hormones. Both aromatase cytochrome P450 (P450arom) and NADPH-cytochrome P450 reductase (reductase), the two essential components of the enzyme complex, are highly conserved among mammals and vertebrates. Aromatase expression occurs in the gonads and brain, and is essential for reproductive development and fertility. Of interest are the complex mechanisms involving alternative promoter utilization that have evolved to control tissue-specific expression in these tissues. In addition, in a number of species, including humans, expression of aromatase has a broader tissue distribution, including placenta, adipose and bone. The relevance of oestrogen synthesis and possibly androgen metabolism in these peripheral sites of expression is now becoming clear from studies in P450arom knockout (ArKO) mice and from genetic defects recognized recently in both men and women. Important species differences in the physiological roles of aromatase expression are also likely to emerge, despite the highly conserved nature of the enzyme system. The identification of functionally distinct, tissue-specific isozymes of P450arom in at least one mammal, pigs, and several species of fish indicates that there are additional subtle, but physiologically significant, species-specific roles for aromatase. Comparative studies of mammalian and other vertebrate aromatases will expand understanding of the role played by this ancient enzyme system in the evolution of reproduction and the adaptive influence of oestrogen synthesis on general health and well being.

scholarly journals Cellulolytic enzyme system of Trichoderma koningii. Separation of components attacking native cotton

1968 ◽  
Vol 109 (2) ◽  
pp. 217-227 ◽  
Author(s):  
T. M. Wood
Keyword(s):  
Enzyme System ◽  
Soluble Sugars ◽  
Low Molecular Weight ◽  
Cellulolytic Enzyme ◽  
Enzyme Complex ◽  
Factor Activity ◽  
Trichoderma Koningii ◽  
S Factor ◽  
Separation Of Components ◽  
Swelling Factor

1. Cell-free culture filtrates from Trichoderma koningii were concentrated by precipitation with ammonium sulphate between the limits of 20% and 80% saturation. 2. Removal of a low-molecular-weight carboxymethylcellulase (CM-cellulase) component by chromatography on Sephadex G-75 had no effect on the ability of the enzyme complex to solubilize cotton. 3. Further chromatography on DEAE-Sephadex separated a component (C1) from the Cx (CM-cellulase) and β-glucosidase activities. Separately these components had little ability to produce soluble sugars from cotton, but when recombined in their original proportions this capacity was almost completely recovered. 4. The Cx component was further fractionated on SE-Sephadex into a fraction containing only CM-cellulase and a fraction showing CM-cellulase and β-glucosidase activities: the latter two components could be separated by heat treatment. 5. The C1 component had no swelling factor (S-factor) activity (Marsh, Merola & Simpson, 1953; Reese & Gilligan, 1954) on its own, but it had a synergistic effect on the S-factor activity associated with the CM-cellulase and β-glucosidase components.

scholarly journals The role of matrix metalloproteinases in the myocardial remodeling

2020 ◽  
Vol 11 (3) ◽  
pp. 22-28
Author(s):  
Vladlen V. Bazylev ◽  
Tatyana V. Kanaeva
Keyword(s):  
Heart Failure ◽  
Extracellular Matrix ◽  
Matrix Metalloproteinases ◽  
Cardiac Remodeling ◽  
Prognostic Markers ◽  
Enzyme System ◽  
Therapeutic Targets ◽  
Myocardial Remodeling ◽  
Structural Event

The main structural event in the development of heart failure is the myocardial remodeling. The extracellular matrix, that was knows as, considered an inert framework of cardiomyocytes, plays an important role in cardiac remodeling. The enzyme system, primarily responsible for the degradation of the extracellular matrix, is a matrix metalloproteinases (MMP). This review examines the evidence for the participation of MMP in the myocardial remodeling and recent studies of MMP as prognostic markers. Regulation of induction and/or activation of MMP are potential therapeutic targets.

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