Hyaluronidase and Gelatinase (MMP-2, MMP-9) Inhibitor Plants
Megh R. Goyal, Durgesh Nandini Chauhan in Assessment of Medicinal Plants for Human Health, 2020
Gelatinase is a proteolytic enzyme that catalyzes the breakdown of gelatin. Gelatinase includes MMPs that are found in human, vertebrate, and nonvertebrate.66 MMPs, belonging to the “Metzincins” superfamily, are calcium-dependent. These include MMP-2 (gelatinase-A) and MMP-9 (gelatinase-B). Their basic activity is to hydrolyze the gelatin to amino acid. Further, it reduces the extracellular matrix components (ECM) like elastin, fibronectin, and collagens (types IV, V, VII, and X) in helical domains.35 While activated MMP-2 may connect to integrin αvβ3 on the uppermost layer of angiogenic endothelial cells and spreading cancer cells, MMP-9 binds to type IV collagen α2 chains on the surface of various cell types especially in skin cancers.7,51 Moreover, angiogenesis and tumor cell invasion are supported via the localizations of MMPs to the cell surfaces. In malignant cancers, MMPs are activated and their levels are increased. Therefore, inhibition of these enzymes is required for treatments of many cancers.66 MMPs are involved in numerous biological and physiological processes, such as embryonic development, inflammatory response, tissue morphogenesis, wound repairing, bone remodeling, autoimmunity, and cell growth.45,50,52
Serratia
Dongyou Liu in Handbook of Foodborne Diseases, 2018
Serratia also has a unique ability to produce extracellular enzymes, specifically protease, DNase, lipase, and gelatinase2; thus, it can degrade chitin, a substance that is a main component of fungal cell walls.45 Such chitinolytic enzymes could have possible industrial and agricultural uses such as the introduction of these genes for chitin-degrading enzymes into crops and fermentative bacteria.46 Some Serratia species have the reproducible capability to break down casein via proteases that disrupt the peptide bonds (CO-NH) producing a clearing on milk agar plates. Hydrolysis of casein is not a common trait and thus is useful in the differentiation of Serratia from other strains of Enterobacteriaceae and Pseudomonadaceae.47 Similarly, gelatinase breaks down gelatin, an incomplete protein that lacks tryptophan. Gelatin hydrolysis transforms the protein to individual amino acids and causes it to liquefy in cold conditions under 25°C, when it would otherwise be solid.48 As a facultative anaerobe, Serratia uses fermentation as the means of gathering energy and produces enzymes such as superoxide dismutase, catalase, and peroxides that protect it from reactive oxygen species, allowing it to live in oxygenated environments.
Differentiation of Ameloblasts and Its Regulation by Epithelial-Mesenchymal Interactions
Colin Robinson, Jennifer Kirkham, Roger Shore in Dental Enamel, 2017
The degradation of the basement membrane may, however, be important for the mediation of inductive signals between the odontoblasts and preameloblasts. Apart from the possibility of the formation of actual cell-to-cell contacts, this also allows the preameloblast cell surface to come in contact with the predentine matrix, which contains a variety of potential regulatory components including both structural and soluble molecules. The mesenchyme appears to have an active role in regulating the breakdown of the basement membrane. Gelatinase A (72-kDa type IV collagenase) is a proteolytic enzyme that is known to cleave basement membrane collagen and its expression in odontoblasts correlates with basement membrane degradation.58 The enzyme is not expressed by the dental epithelium but is present in the dental mesenchyme throughout tooth morphogenesis. Upregulation is evident in the odontoblasts prior to basement membrane removal and thereafter the expression is downregulated (Figure 12).
Progesterone suppresses the lipopolysaccharide-induced pro-inflammatory response in primary mononuclear cells isolated from human placental blood
Published in Immunological Investigations, 2018
E. Preciado-Martínez, G. García-Ruíz, P. Flores-Espinosa, L. Bermejo-Martínez, A. Espejel-Nuñez, G. Estrada-Gutiérrez, G. Razo-Aguilera, M. Granados-Cepeda, A. C. Helguera-Repetto, C. Irles, V. Zaga-Clavellina
Clinical and experimental data propose that several cytokines, such as IL-1β, TNF-α, and IL-6, are able to induce an increase in MMP-9 production. This enzyme with gelatinase properties plays an important role in the degradation of the extracellular matrix and structural loss of human fetal membranes (Gomez-Lopez et al., 2013). MMP-9 participates in the physiological labor process, but it is also involved in tissue damage associated with infection; higher levels of this enzyme in amniotic fluid have been related to intra-amniotic infectious processes (Harirah et al., 2002; Locksmith et al., 1999). In the current work, PLBMCs stimulated with LPS induced a modest increase in total MMP-9 (active and pro-enzyme), present in the cell lysates. This increment might be in part explained by the cell response to the endotoxin and simultaneously to the inductor effect of IL-1β, TNF-α, and IL-6. These findings agree with the previous results observed in fetal membranes (Garcia-Lopez et al., 2007; Pineda-Torres et al., 2014) and in explants from human term placenta [27]. In this context, there is evidence that reveals IL-10 as a key factor in the process of placentation and trophoblastic invasion, which have been related to higher levels of MMP-9 and lower levels of IL-10 (Stearns et al., 1995). Our model of P4 and LPS co-stimulation failed to decrease in a significant manner MMP-9 expression; however, there is evidence that P4 can inhibit MMP-1 and MMP-3 expression in decidua term cells; both enzymes are involved in the process of PROM in physiological and pathological conditions (Oner et al., 2008).
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
Enhanced efficacy of curcumin with phosphatidylserine-decorated nanoparticles in the treatment of hepatic fibrosis
Published in Drug Delivery, 2018
Ji Wang, Wen Pan, Ying Wang, Wan Lei, Bin Feng, Caigan Du, Xiao-juan Wang
Gelatinase activity of MMP-2 was determined by gelatin zymography. In brief, liver samples were homogenized with NP40 (1:30 mass ratio) on ice. The homogenate was centrifuged at 13,000 g for 10 min, and then the BCA method was used to determine protein content in the supernatant. Dilute samples at 1:1 with 2 × SDS-PAGE non-reducing buffer. Equal amounts of protein were loaded into 9% SDS-PAGE containing 10% gelatin to separate proteins. After electrophoresis at 40 mA, gels were washed three times with 2.5% Triton X-100 for 30 min and then incubated in a solution containing 50 mM Tris and 10 mM CaCl2, pH 7.5 at 37 °C for 18 h, and then were stained with 0.25% Coomassie blue for 15 min, followed by being decolored with a solution containing 7% acetic acid and 5% methanol. The intensity of bands was quantified by densitometry analysis using Gel-Pro Analyzer (Media Cybernetics, Inc., MD).
Related Knowledge Centers
- Enzyme
- Gelatin
- Hydrolase
- Matrix Metalloproteinase
- Extracellular Matrix
- Gelatinase A
- Mmp2
- Gelatinase B
- Mmp9
- Enzyme Commission Number