China
Africa
Explore chapters and articles related to this topic
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.
Animal Models for Investigations of Biomaterial Debris
Published in Yuehuei H. An, Richard J. Friedman, Animal Models in Orthopaedic Research, 2020
Martin Lind, Yong Song, Stuart B. Goodman
Manual testing demonstrated that the control implants were well-fixed after the 12 week observation period whereas the implants with motion or particles were all manually loose. Histologically, membrane tissue around control implants consisted of very few macrophages. For motion implants a thick membrane was found but with only a moderate number of macrophages. Around the gap implants, a thick membrane was found with high numbers of macrophages in all particle stimulated groups. However, PE particles appeared the stimulate macrophage accumulation less than CoCr alloy and Ti alloy particles. Biochemical analyses of conditioned medium from cultured membrane tissue revealed high levels of collagenase activity and PGE2 release in metal particle groups and lesser activity in the polyethylene particles group. Gelatinase activity was mainly elevated in the group with motion implants. IL-1 activity was highest in CoCr alloy and PE particle groups.
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.
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
An inflammatory triangle in Sarcoidosis: PPAR-γ, immune microenvironment, and inflammation
Published in Expert Opinion on Biological Therapy, 2021
Parnia Jabbari, Mona Sadeghalvad, Nima Rezaei
Hsieh MH et al., demonstrated that PPAR-γ agonists inhibit MMPs expression in macrophages during the inflammation process [78]. It has been shown that PPAR-γ ligands inhibit the transcription of gelatinase B (MMP-9) and scavenger receptor A genes in response to phorbol ester stimulation. The result of inhibited MMP-9 gene transcription by PPAR-γ agonists was represented by the reduced gelatinolytic activity in human monocyte-derived macrophages. Activator protein 1 (AP-1) and Erythroblast Transformation Specific (ETS) as two transcription factors are involved in the activation of gelatinase B. It has been shown that PPAR-γ could exert its anti-inflammatory functions by inhibiting these transcription factors [79]. A hypothesis is raised here that maybe the binding activity of ETS and AP-1 to MMP-9 promoter could be related to the decreased expression of PPAR-γ, as a negative regulator of inflammation in sarcoidosis.
Novel matrix metalloproteinase inhibitors: an updated patent review (2014 - 2020)
Published in Expert Opinion on Therapeutic Patents, 2021
Elena Lenci, Lucrezia Cosottini, Andrea Trabocchi
Concerning which MMPs have been recently taken into account, research toward MMP-13 inhibitors is active, as this collagenase is of special interest in pathological inflammatory conditions and no MMP-13 inhibitors have received FDA approval, yet, due to lack of selectivity and poor bioavailability. Also, the two gelatinases, MMP-2 and MMP-9, are still most studied due to their well-established role in cancer pathologies, being key players in the angiogenic switch and cell invasiveness. Actually, interest to gelatinases is related to the link between their dysregulation and a number of neurological and psychiatric diseases, and suitable inhibitors that are capable of crossing the blood-brain barrier have been patented, accordingly. Finally, phosphinic-based MMP-12 inhibitors have been claimed as antiviral agents, specifically acting on extracellular MMP-12 due to their membrane-impermeability provided by the presence of negative charges at physiological pH.