Calprotectin in rheumatic diseases

Abstract

Calprotectin is an acute-phase protein produced by monocytes and neutrophils in the circulation and inflamed tissues. Calprotectin seems to be more sensitive than CRP, being able to detect minimal residual inflammation and is a candidate biomarker in inflammatory diseases. High serum levels are associated with some severe manifestations of rheumatic diseases, such as glomerulonephritis and lung fibrosis. Calprotectin levels in other fluids, such as saliva and synovial fluid, might be helpful in the diagnosis of rheumatic diseases. Of interest is also the potential role of calprotectin as a target of treatment. AbstractCalprotectin is a heterodimer formed by two proteins, S100A8 and S100A9, which are mainly produced by activated monocytes and neutrophils in the circulation and in inflamed tissues. The implication of calprotectin in the inflammatory process has already been demonstrated, but its role in the pathogenesis, diagnosis, and monitoring of rheumatic diseases has gained great attention in recent years. Calprotectin, being stable at room temperature, is a candidate biomarker for the follow-up of disease activity in many autoimmune disorders, where it can predict response to treatment or disease relapse. There is evidence that a number of immunomodulators, including TNF-a inhibitors, may reduce calprotectin expression. S100A8 and S100A9 have a potential role as a target of treatment in murine models of autoimmune disorders, since the direct or indirect blockade of these proteins results in amelioration of the disease process. In this review, we will go over the biologic functions of calprotectin which might be involved in the etiology of rheumatic disorders. We will also report evidence of its potential use as a disease biomarker.

Transcriptomic Analysis of Cellular Pathways in Healing Flexor Tendons of Plasminogen Activator Inhibitor 1 (PAI‐1/Serpine1) Null Mice

“…The heterodimer S100A8/A9, also known as calprotectin, functions primarily to promote pro‐inflammatory cytokines and chemokines . When secreted, S100A8 is a damage‐associated molecular pattern ligand for the Toll‐like receptor‐4 and the receptor for advanced glycation end‐products .…”

“…The heterodimer S100A8/A9, also known as calprotectin, functions primarily to promote pro-inflammatory cytokines and chemokines. 38 When secreted, S100A8 is a damage-associated molecular pattern ligand for the Toll-like receptor-4 and the receptor for advanced glycation end-products. 39 As such, it plays a role in the innate adaptive immune responses to injury and has been associated with fibrosis, 40 senescence, 41 and apoptosis.…”

Effects of unsaturated fatty acids (Arachidonic/Oleic Acids) on stability and structural properties of Calprotectin using molecular docking and molecular dynamics simulation approach

“…Commonly, each subunit of the protein consists of two EF-hands with helix-loop-helix structural motif related by a central hinge region. Moreover, each monomer has the ability to bind to two calcium ions and other divalent cations such as: Zn 2+ , Cu 2+ , Mn 2+ and Fe 2+ [5,6]. The human S100A8/A9 complex has the molecular weight of 11 and 13 kDa with 93 and 114 amino acids respectively [7,8].…”

Reaction of food‐specific antibodies with different tissue antigens

“…6). For instance, zonulin is involved in gut barrier dysfunction, calprotectin is involved in the pathogenesis of rheumatic diseases, alpha-myosin is involved in cardiovascular autoimmunity, and asialoganglioside plays a role in Guillain-Barr e syndrome (Lv et al, 2011;Yuki, 2012;Vaishnav et al, 2013;Ometto et al, 2017;Vojdani et al, 2017). As was shown earlier, anti-peanut antibody reacted with twenty-four out of sixty-five different tested tissue antigens.…”

“…). For instance, zonulin is involved in gut barrier dysfunction, calprotectin is involved in the pathogenesis of rheumatic diseases, alpha‐myosin is involved in cardiovascular autoimmunity, and asialoganglioside plays a role in Guillain–Barré syndrome (Lv et al , ; Yuki, ; Vaishnav et al , ; Ometto et al , ; Vojdani et al, ).…”