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The diagnosis and management of preterm labor with intact membranes
Published in Hung N. Winn, Frank A. Chervenak, Roberto Romero, Clinical Maternal-Fetal Medicine Online, 2021
Roberto Romero, Tinnakorn Chaiworapongsa, Francesca Gotsch, Lami Yeo, Ichchha Madan, Sonia S. Hassan
Neutrophils produce a collagenase, which is called matrix metalloproteinase 8 (MMP-8). MMP-8 has been proven to be an excellent marker for intra-amniotic infection/inflammation (234,235). Amniotic fluid MMP-8 >30ng/mL has a sensitivity of 82.4%, specificity of 78%, positive predictive value of 36%, and negative predictive value of 97.7% for the prediction of intra-amniotic infection, defined as positive amniotic fluid culture (235). A rapid test (MMP-8 PTD Check test; SK Pharma Co. LTD, Korea) has been produced (236,237), which has high sensitivity and specificity, as well as likelihood ratios for a positive and a negative result (238).
Cardiac biomarkers in acute coronary syndrome
Published in K Sarat Chandra, AJ Swamy, Acute Coronary Syndromes, 2020
Metalloproteinases (MMPs) are a class of 24 endopeptidases that are physiologic regulators of the extracellular matrix. They are an expanding group of proteolytic enzymes that participate in numerous physiological and pathological processes including embryogenesis, connective tissue turn-over, healing, and angiogenesis. Inflammatory stimuli augment the production of the interstitial collagenases MMP-1, MMP-13, and MMP-8 from several cell types found in atherosclerotic plaques. Human atherosclerotic plaque also contains elevated levels of the MMP-9 active form, an enzyme with gelatinolytic activity that can continue the catabolism of collagen cleaved by interstitial collagenases [41].
Micronutrients in Improvement of the Standard Therapy in Traumatic Brain Injury
Published in Kedar N. Prasad, Micronutrients in Health and Disease, 2019
Experimental data in animal models of severe TBI suggested that an increase in the levels of matrix metalloproteinases 3 and 9, which are considered responsible for inflammation in the blood-brain-barrier disruption, hemorrhage, and neuronal death occurred after TBI. Indeed, a clinical study on 6 patients with TBI showed that the CSF levels of MMP-9 were elevated; however, elevated levels of MMP-3 were observed in the plasma but not in the CSF.151 These data suggest that MMPs play an important role in the progression of damage after TBI. Increased levels of MMP-8 and MMP-9 were associated with increased levels of pro-inflammatory cytokines (IL-1 alpha, IL-2, and TNF-alpha) in the microdialysis samples of 8 patients with severe TBI. In contrast, the levels of MMP-7 decreased with increases in the levels of IL-1beta, Il-2 and IL-6.152
Challenges with matrix metalloproteinase inhibition and future drug discovery avenues
Published in Expert Opinion on Drug Discovery, 2021
As mentioned, MMPs can be grouped into a subgroup that is anchored to the cell surface (MMP-14, −15, −16, −17, −24, −25), and the members that are secreted to the ECM, which outnumber the membrane-bound ones. In addition, they can be classified with respect to their preferential substrate into collagenases (MMP-1, −8, −13, −18), gelatinases (MMP-2, −9), stromelysins (MMP-3, −10, −11), and others (MMP-7, −12, −19, −20, −21, −22). Together, the MMPs have the capacity to decompose all components found in the extracellular matrix, and if one member is taken out of the equation by inhibition or in a knock-out model for example, another one can step in and take over its function. Increased MMP-8 expression was observed in a MMP-13 knock-out mice model during wound healing, and elevated MMP-9 levels were found in a MMP-8 deficient wound repair model[36,37]. An explanation for this can be that each MMP in the network is able to hydrolyze various substrates, whereas specific substrates might be cleaved by different MMPs. This substrate redundancy is a major challenge for the pharmaceutical targeting of the enzyme family.
Odontoblast-like MDPC-23 cells produce pro-inflammatory IL-6 in response to lipoteichoic acid and express the antimicrobial peptide CRAMP
Published in Acta Odontologica Scandinavica, 2020
Karin Odlén, Felicia Fält, Sara Dahl, Alexandra Aidoukovitch, Dan Ericson, Bengt-Olof Nilsson, Anders Hedenbjörk-Lager
Cells were scraped off in ice-cold PBS from the culture wells using cell scrapers (Sarstedt, Newton, NC, USA) and sonicated (2 × 10 s) on ice. The cell-homogenates were centrifuged (1700 g at 4 °C for 5 min) and the supernatants collected. MMP-8 and IL-6 protein production was determined in the cell supernatants using ELISA kits (MMP-8 and IL-6 kits purchased from LifeSpan BioSciences, Seattle, WA, USA and Nordic BioSite, Täby, Sweden, respectively). Determination of MMP-8 and IL-6 concentration was performed as recommended by the manufacturers. Each sample was analyzed in duplicate, and the concentrations of MMP-8 and IL-6 normalized to total protein concentration in each sample determined by a Bio-Rad protein assay kit (Bio-Rad, Hercules, CA, USA).
Active matrix metalloproteinase-8 and interleukin-6 detect periodontal degeneration caused by radiotherapy of head and neck cancer: a pilot study
Published in Expert Review of Proteomics, 2020
Mutlu Keskin, Hanna Lähteenmäki, Nilminie Rathnayake, Ismo T. Räisänen, Taina Tervahartiala, Pirjo Pärnänen, Ahmet Murat Şenışık, Didem Karaçetin, Ayben Yentek Balkanay, Pia Heikkilä, Jaana Hagström, Jaana Rautava, Caj Haglund, Ulvi Kahraman Gursoy, Angelika Silbereisen, Nagihan Bostanci, Timo Sorsa
Our results support and further extend the previous studies that have demonstrated a significant damage to the periodontium and loss of periodontal attachment due to radiotherapy [4–8]. This deteriorating effect of radiotherapy on the periodontium is significantly reflected in elevated aMMP-8 levels measured and detectable by the aMMP-8 point-of-care mouthrinse test utilized in this study. Furthermore, we observed a moderate to strong positive correlation between the aMMP-8 and IL-6 levels measured in the mouthrinses before, during and after the HNC radiotherapy. To our knowledge, this is the first time this kind of an association between these two periodontitis biomarkers, aMMP-8 and IL-6, is reported in oral fluid in vivo. Although a correlation does not necessarily imply causality, it has been previously shown that MMP-8 activity can modulate the production of proinflammatory IL-6 and IL-8 in inflammation [24]. In this regard, it should be noted that elevated IL-6 levels may cause excessive osteoclastic activity and osteolysis [18]. Furthermore, previous studies have reported that IL-6 plays an important role mainly in the initiation and acute phase of periodontitis [17]. Thus, MMP-8 is not only a proteinase but has also inflammatory regulatory and immunomodulatory roles, as has been previously shown, as well [10]. Nevertheless, activation of MMP-8 is a complex process [10]. Further research is still needed to better understand the initiation of the periodontal pathogenesis in HNC radiotherapy and the role of different molecules and cascades in it, such as TIMP-1, the major endogenous inhibitor of MMP-8 activation, and, for example, if its downregulation occurs in effect of HNC radiotherapy.