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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
S100A12 is a relatively recent member, an additional phagocyte-specific S100 protein that is also called calgranulin C, calcium binding protein in amniotic fluid 1, and the extracellular newly identified receptor for advanced glycation end product binding protein (EN-RAGE). Neutrophils and macrophages bind tightly to S100A12-stimulated endothelium, possibly due to the VCAM1 and ICAM1 increase on endothelial cells. This upregulation is due to a signaling cascade downstream of S100A12 binding to EN-RAGE and heparan proteoglycans, partly mediated by NFkB, as shown by several works from Foell and Roth (2004).
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
Identification of hub genes and potential biomarkers of neutrophilic asthma: evidence from a bioinformatics analysis
Published in Journal of Asthma, 2023
Qibin Lin, Haiyang Ni, Jieying Zhong, Zhishui Zheng, Hanxiang Nie
Presently, the S100 protein family comprises at least 20 members that are involved in diverse functions, including cellular proliferation, differentiation, apoptosis, energy metabolism, and inflammation (26). S100A12 is a member of the S100 protein family. It is also known as S100/calgranulin C and exists both within and outside of cells (27). S100A12 is expressed in many inflammatory cells and is present in the greatest abundance in neutrophils (28). The S100A12 protein undergoes conformational rearrangement and activation (27). The activated S100A12 protein can activate cell surface receptors, such as receptor for advanced glycation end products (RAGE) and Toll-like receptor-4 (TLR-4), to promote inflammation (28). Jin Hyun Kang et al. found that S100A12 acts on airway epithelial cells to induce MUC5AC production, supporting the important role of S100 protein in the pathogenesis of obstructive airway diseases dominated by neutrophils (28). In addition, S100A12 is considered to be related to oxidative stress in local airway inflammation (29). It has been proven that the S100A12 protein participates in lung diseases (27). Our study found that the sputum S100A12 level could be used to discriminate NA patients from EA patients and healthy people, suggesting that sputum S100A12 is a potential biomarker of NA. Current clinical trials related to the S100 protein family are mainly focused on nonpulmonary diseases, such as rheumatoid arthritis (27). Our research suggests that anti-S100A12 antibodies may benefit NA patients, but further studies are warranted.
S100 Proteins, Cytokines, and Chemokines as Tear Biomarkers in Children with Juvenile Idiopathic Arthritis-associated Uveitis
Published in Ocular Immunology and Inflammation, 2021
Sheila T. Angeles-Han, Virginia Miraldi Utz, Sherry Thornton, Grant Schulert, Jackeline Rodriguez-Smith, Adam Kauffman, Alyssa Sproles, Najima Mwase, Theresa Hennard, Alexei Grom, Mekibib Altaye, Gary N. Holland
S100A12 is a pro-inflammatory protein released by neutrophils, which modulates neutrophil activities, and has roles in leukocyte recruitment, cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Serum S100A8/A9 and S100A12 were also elevated in a cross-sectional study that compared children with JIA-U or chronic anterior uveitis to controls.6 Only serum S100A8/A9 differentiated uveitis by activity in that study. AqH S100A8/A9 was also elevated in JIA-U patients compared to controls, despite all cases having inactive uveitis. There was no correlation between serum and AqH levels. In a prospective study of 953 children with JIA, baseline serum S100A12 levels were associated with uveitis.14 The role of S100 proteins in uveitis pathogenesis and activity needs further investigation.
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.