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Angiogenesis and Roles of Adhesion Molecules in Psoriatic Disease
Published in Siba P. Raychaudhuri, Smriti K. Raychaudhuri, Debasis Bagchi, Psoriasis and Psoriatic Arthritis, 2017
Asmita Hazra, Saptarshi Mandal
S100A8 is also called calgranulin A or MRP8. S100A9 is also called calgranulin B or MRP14. At the time of discovery in 1987, they were actually called macrophage migration inhibitory factor (MIF)–related proteins: MRP8 and MRP14 (see Section 5.2.5.20). They preferentially form the S100A8/A9 heterodimer, which is called leukocyte protein L1 or cystic fibrosis antigen or calprotectin. These are abundantly expressed in myeloid cells, for example, neutrophils, monocytes, and early macrophages, and also to some extent in keratinocytes. In inflamed microvasculature, the S100A8/A9 complex is deposited onto the endothelium of venules associated with extravasating leukocytes. Normal tissue macrophages do not express S100A8/A9. Chronic inflammatory macrophages, for example, in RA, sarcoidosis, tuberculosis, or onchocerciasis, express both S100A8 and A9, but macrophages in acute inflammation usually express only S100A9. In neutrophils, the S100A8/A9 complex is the most abundant cytosolic protein and may represent almost 45% (30%–60%) of the soluble cytosolic protein content, and the level is 40-fold less in monocytes. This protein is also present in neutrophil granules, especially secondary granules, but the localization is blurred by the cytosolic abundance. IL10 indirectly and slowly stimulates S100A8/A9 production in a COX2-cAMP-dependent way, whereas Th2 cytokines IL4 and IL13 suppress them. Neutrophilic calprotectin, possibly largely cytosolic, is actively extruded with NETs, and this calprotectin is absolutely necessary for antifungal activity of NET in vitro.
Seronegative arthropathies
Published in Rajan Madhok, Hilary Capell, The Year in Rheumatic Disorders Volume 4, 2004
BACKGROUND. Neutrophil, macrophage and lymphocytic infiltration are characteristic of the inflamed synovium in psoriatic and seronegative disease. Factors that regulate this inflammatory response have been much more poorly characterized than in RA. S100A12 (calgranulin C; or EN-RAGE), a member of a family of proteins that share EF hand domains, is produced predominantly by granulocytes and once secreted acts as a
Discerning the promising binding sites of S100/calgranulins and their therapeutic potential in atherosclerosis
Published in Expert Opinion on Therapeutic Patents, 2021
Harbinder Singh, Vikrant Rai, Devendra K Agrawal
The S100 proteins were first reported in 1965 with the characteristic feature of their solubility in 100% saturated ammonium sulfate solution at neutral pH, thus named as ‘S100 protein’ [24]. These proteins consist of 21 members which are mainly expressed in vertebrates and perform various intracellular and extracellular functions [25]. Among all the S100 proteins, S100A8, S100A9, and S100A12 are highly associated with cardiovascular disorders [18,26–28]. These three members of the S100 protein family are commonly referred to as S100/calgranulins. S100A8 is also known as calgranulin A and myeloid-related protein 8 (MRP-8). Similarly, S100A9 is also called calgranulin B and MRP-14. Their non-covalently combined form is also known as calprotectin (MRP8/14) which is a 24 kDa heterodimer of S100A8 and S100A9 (S100A8/A9) [29,30]. Likewise, calgranulin C or EN-RAGE are the other names of S100A12.
MiR-30a Regulates S100A12-induced Retinal Microglial Activation and Inflammation by Targeting NLRP3
Published in Current Eye Research, 2019
S100/calgranulin family comprises the largest group of calcium-binding proteins.7 All of the S100 proteins are characterized by the presence of two calcium-binding EF-hand motifs with different affinities for calcium.7 In the S100/calgranulin family, S100A8, S100A9, and S100A12 have been proved to play a pivotal role in exacerbating inflammatory response cooperating with inflammatory factors. S100A12 has been demonstrated to act independently from S100A8/S100A9, which is additionally known as EN-RAGE (extracellular newly identified receptor for AGE-binding protein).7,8 S100A12 is released from activated neutrophils and macrophages, which has proinflammatory effects on immune cells, and promotes inflammatory response.7–9 Our previous study has shown that plasma levels of S100A12 are closely associated with presence and severity of DR.9 However, to the best of our knowledge, whether S100A12 can contribute to the inflammatory changes of DR and microglial activation have not been fully elucidated.
Diagnostic accuracy of one or two faecal haemoglobin and calprotectin measurements in patients with suspected colorectal cancer
Published in Scandinavian Journal of Gastroenterology, 2018
James Turvill, Samantha Mellen, Laura Jeffery, Sarah Bevan, Ada Keding, Daniel Turnock
The limited role of FC in this and indeed a lower risk population for CRC has been demonstrated previously [10,12,13]. In contrast to our results, Kok et al found a combination of tests to improve diagnostic accuracy but this study was conducted using point of care tests and non-consecutive referrals. A composite of clinical outcomes similar to OED was used. Patients were judged high risk but their median age was 60 years [23]. The benefits of the addition of a point of care FC to a point of care FIT over FIT alone are not seen in a related study [24]. Kim et al. found a combination of faecal haemoglobin and inflammatory biomarkers (calgranulin B) to improve diagnostic yield in the context of CRC screening. However, the positivity threshold of FIT was set sub-optimally at the equivalent of 17 µg Hb/g faeces [25]. Again, using a higher cut-off, Parente et al assessed FIT with pyruvate kinase isoform M2 and calprotectin, finding an improved sensitivity but poorer specificity when using these additional biomarkers [26]. We have demonstrated in this work that neither single nor double testing with FC improves the diagnostic accuracy of FIT. This is consistent with our previous findings assessing FC alone [4].