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Hyaluronidase and Gelatinase (MMP-2, MMP-9) Inhibitor Plants
Published in Megh R. Goyal, Durgesh Nandini Chauhan, Assessment of Medicinal Plants for Human Health, 2020
C. Donmez, G. D. Durbilmez, H. El-Seedi, U. Koca-Caliskan
Although both have substantial effects, level of HA and gelatin in the skin decreases due to aging, improper diet, stress, and various external factors, such as sunlight, wind, irritation, injury, and cigarette smoke. The degradation of HA and gelatin is undesirable in terms of maintaining vitality and flexibility of the skin. “Replacement therapy”, “increasing the synthesis of the related enzymes”, and “inhibiting their disintegration” on the skin are some of the solutions to keep the level of the enzymes at desirable levels. “Hyaluronidase” is an enzyme that catalyzes the degradation of HA. “Gelatinase A and B” (also known as “matrix metalloproteinase (MMP)-2 and MMP-9”) are members of the matrix metalloproteinase enzyme family to catalyze the degradation of gelatin.
Methods of Evaluation in Orthopaedic Animal Research
Published in Yuehuei H. An, Richard J. Friedman, Animal Models in Orthopaedic Research, 2020
Numerous biochemical tests are available for quantification of biochemical components in bone, cartilage, ligament, tendon, and other tissues. For articular cartilage, DNA content can be evaluated with several different methods,145-147 the hydroxyproline content (a measure of collagen) with a colorimetric148,149 or 3H-hydroxyproline method,150 the ratios of type I and II collagen with SDS-polyacrylamide gel method,151 PGs or GAG content with a hexosamine method,152 electrophoresis,153 immunoblotting,153 or 1,9-dimethylmethylene blue method,149,154 PGs synthesis with RIA,149,155,156 CMP synthesis with a immunoblotting method,50 and fibronectin content with ELISA.58 Biochemical methods are also used to evaluate gelatinase activity149,157,158 and tissue inhibitor of metalloproteinase (TIMP).149,159 Immunochemical methods in cartilage research were summarized by Hardingham.160
Effects of TNF-α on Endothelial Control of Hemostasis
Published in Pia Glas-Greenwalt, Fibrinolysis in Disease Molecular and Hemovascular Aspects of Fibrinolysis, 2019
The TNF-α-induced secretion of u-PA by endothelial cells in vitro is vectorial.121 With endothelial cells cultured on porous filters it has been demonstrated that almost all u-PA is secreted to the basolateral side of the cell. On the other hand, the production of t-PA and PAI-1 occurs almost equally towards the luminal and the basolateral sides of the cells. The increased production of u-PA is accompanied by an increased degradation of extracellular matrix proteins.123 The pericellular action of u-PA is spatially controlled by a specific cellular receptor.27,83,133 Parallel with the induction of u-PA, TNF-α increases the expression of the matrix metalloproteinases stromelysin, type I collagenase, and gelatinase-B by endothelial cells.134 It is of interest to note that gelatinase activities are also secreted predominantly to the basolateral side of endothelial cells.135 This favors the idea that u-PA, probably together with plasmin and matrix metalloproteinases, has a function in proteolytic events regulating the interaction of the cell with its basal membrane. The simultaneous induction of u-PA and PAI-1 by TNF-α may therefore point to an additional function of PAI-1: to protect the extracellular matrix against excessive u-PA action.
Neurotherapeutic efficacy of loaded sulforaphane on iron oxide nanoparticles against cuprizone-induced neurotoxicity: role of MMP-9 and S100β
Published in Toxicology Mechanisms and Methods, 2023
Ghadha Ibrahim Fouad, Mostafa Mabrouk, Sara A. M. El-Sayed, Maha Z. Rizk, Hanan H. Beherei
Neuroinflammation is another well-known feature in MS patients (Kemanetzoglou and Andreadou 2017). In our study, CUP intoxication resulted in significant upregulation in the genetic expression of both MMP-9 and S100β. CUP-induced oxidative stress might be implicated indirectly in MS pathogenesis by stimulating the expression and activation of matrix metalloproteinases (MMPs) by interfering with the mechanism of ‘cystein switch’, which is essential for MMP activation (Nelson and Melendez 2004). CUP-associated oxidative stress and inflammation stimulate MMP-9 (gelatinase-B) expression, which could directly degrade the components of the extracellular matrix and disrupt the BBB (Haorah et al. 2008). The BBB integrity and permeability are regulated by MMP-9 expression; on the other hand, the BBB disruption is a key pathological hallmark in MS (Li et al. 2013; Ashok et al. 2016; Greene et al. 2019).
Serum activity of matrix metalloproteinase-2 and -9 is increased in chronic post-stroke individuals: a cross-sectional exploratory study
Published in Topics in Stroke Rehabilitation, 2022
Luisa Fernanda García-Salazar, Jean Alex Matos Ribeiro, Jonathan Emanuel Cunha, Stela Marcia Mattiello, Thiago Luiz Russo
Matrix Metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that promote the degradation and synthesis of extracellular matrix (ECM) proteins. Among one of the categories of this type of enzymes are gelatinase matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9).1 In blood circulation, high concentrations of these gelatinases, are associated with an inflammatory process such as that observed after stroke.2,3 Activation of MMP-2 begins during hypoxia and participates in the disruption of the ECM proteins in the basal lamina and degrades the tight junction proteins.1,4 On the other hand, inducible MMP-9 enzymes, which are normally kept inactive, become active due to the action of free radicals and other enzymes, and induce the opening of the blood-brain barrier (BBB). This gelatinase degrades the neurovascular matrix, promoting neuroinflammation and vasogenic edema, including the activation of several other pro-inflammatory cytokines and chemokines such as interleukin (IL)-1 and tumor necrosis factor alpha (TNF-α).1,4
A topical formulation containing quercetin-loaded microcapsules protects against oxidative and inflammatory skin alterations triggered by UVB irradiation: enhancement of activity by microencapsulation
Published in Journal of Drug Targeting, 2021
David L. Vale, Renata M. Martinez, Daniela C. Medeiros, Camila da Rocha, Natália Sfeir, Renata F. V. Lopez, Fabiana T. M. C. Vicentini, Waldiceu A. Verri, Sandra R. Georgetti, Marcela M. Baracat, Rúbia Casagrande
SDS-PAGE (sodium dodecyl sulphate polyacrylamide gel electrophoresis) substrate-embedded enzymography was used to detect enzymes with gelatinase activity. Assays were carried out as previously described 30,37]. The dorsal skin of hairless mice (1:4, w/w dilution) was homogenised (Ultra Turrax® - T18 basic, IKA) in 0.05 M Tris–HCl buffer (pH 7.4) containing 0.01 M CaCl2 and 1% protease inhibitor cocktail. Whole homogenates were centrifuged twice at 12000xg for 10 min at 4 °C. The Lowry method was used to measure protein levels in skin homogenates [43]. Aliquots of 50 µL of samples were mixed with 10 µL of 0.1 M Tris-HCl (pH 7.4) containing 20% glycerol, 4% SDS and 0.005% xylene cyanol. For electrophoresis, 25 µL of the mixture was used were taken for electrophoresis in a gel containing 10% acrylamide and 0.025% gelatine. After electrophoresis, the gels were incubated for 1 h with 2.5% Triton X-100 under constant shaking, incubated overnight in 0.05 M Tris-HCl (pH 7.4), 0.01 M CaCl2 and 0.02% sodium azide at 37 °C, and stained the following day with brilliant blue R. After destaining in 20% acetic acid, zone of enzyme activity was analysed by comparing the groups in the ImageJ software package (NIH, Bethesda, MD, USA).