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Mucosal B cells and their function
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Jo Spencer, Edward N. Janoff, Per Brandtzaeg
Mucosal epithelia are protected by secretory immunoglobulin A (SIgA) and, to a lesser extent, secretory IgM (SIgM) antibodies produced by plasma cells and/or plasmablasts in the lamina propria. These tissue plasmablasts and plasma cells are identified in humans by expression of CD38, CD27, lower levels of CD19, and the absence of the B-cell marker CD20 and constitute the body's largest population of antibody-secreting cells. CD138 (syndecan-1) is reliably expressed on plasma cells, but epithelial cells also express CD138. Although IgA is the major isotype produced at mucosal surfaces, its production varies among different regions variations of the intestinal tract. Mucosal plasma cells produce mainly dimeric IgA and some larger polymers of IgA (collectively called polymeric IgA, pIgA).
Pathogenesis
Published in Aparna Palit, Arun C. Inamadar, Systemic Sclerosis, 2019
The process of angiogenesis is mainly regulated by VEGF. It stimulates the migration and proliferation of ECs, increases vascular permeability, and induces tube formation. In SSc, VEGF is strongly expressed in skin and its serum level is also significantly increased. The latter bears significant correlation with fingertip ulceration in patients with SSc. Even though the VEGF levels are increased in SSc, the time kinetics of its expression plays a critical role in angiogenesis. The new vessels become untenable if upregulation of VEGF is transient. A prolonged overexpression results in uncontrolled fusion of new vessels resembling disturbed capillary network.10 Higher levels of syndecan-1 that binds to VEGF and presents them to respective receptors on endothelial cells has been demonstrated in SSc. Higher levels of syndecan-1 correlate with SSc vasculopathy, such as telangiectasia and PAH.11
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
Works of Rong Shao’s group (e.g., Francescone et al. 2011) have shown that YKL40 plays a role in the upregulation of VEGF expression and enhances angiogenesis synergistically with VEGF. YKL40 has been shown to induce interaction of syndecan 1 and integrin αvβ3 in endothelial cells of αvβ5 in tumor cells through binding heparan sulfate chains of syndecan 1 on the cell surface and downstream activation of focal adhesion kinase (FAK) and ERK1 and 2, thus inducing VEGF-mediated further angiogenic cascade. The action of YKL40 on vascular smooth muscle action is supposed to restrict vascular leakage, and stabilizes vascular networks. Vascular sprouting and stability mediated by smooth muscle–like cells are dependent on signaling activation induced by YKL40, including N-cadherin with β-catenin and smooth muscle α actin in cytoskeleton. The adhesion and permeability of human microvascular endothelial cells (HMVECs) modulated by YKL40 depend on the interaction of VE-cadherin with β-catenin and actin. Neutralizing anti-YKL40 antibodies (e.g., clone “mAY” for mice) have been shown to inhibit migration and tube 12 formation induced by YKL40 in a dose-dependent fashion, and also inhibited the VEGFR2 (Flk1/KDR) induction and mitogen-activated protein kinase (MAPK) ERK1 and 2 activation downstream of YKL40. Thus, targeting YKL40 is an important potential antiangiogenic target.
Syndecan 1 may slow the progression of subclinical atherosclerosis in patients with ankylosing spondylitis
Published in Clinical and Experimental Hypertension, 2023
Pinar Diydem Yilmaz, Cengiz Kadiyoran, Mevlut Hakan Goktepe, Yasemin Akkubak, Abdullah Icli, Adem Kucuk
Syndecan 1 (S1) is a protein-structured member of the syndecan proteoglycan family encoded by the S1 gene (15). A transmembrane domain of S1 contains heparan sulfate and chondroitin sulfate, which interact with extracellular matrix proteins through the heparan sulfate receptor and are involved in cell proliferation and migration (16). At low S1 levels, increased intercellular adhesion molecule-1 (ICAM-1) and increased leukocyte uptake by heparan sulfate result in enhanced inflammation (17). Increased S1 levels are protective against inflammation (18). S1 expression was found in the synovial sampling of patients with rheumatoid arthritis and psoriatic arthritis (19). This condition suggests that S1 may play a role in the pathophysiology of arthritis, such as migration and recruitment of leukocytes and angiogenesis in the chronically inflamed synovium. In the absence of S1 expressed from M2 macrophages, leukocyte infiltration due to impaired migration and increased adhesion occurs, and the atherosclerotic process accelerates (20).
Epithelial damage in the cystic fibrosis lung: the role of host and microbial factors
Published in Expert Review of Respiratory Medicine, 2022
Arlene M. A. Glasgow, Catherine M. Greene
MMP-7 (or matrilysin) regulates the neutrophil chemotactic gradient during lung injury via cleavage of syndecan-1 from the epithelial cell surface, which releases CXCL1 [122]. It is also critical to the repair response, as MMP-7 inhibition impairs post-injury re-epithelialisation [123]. MMP-7 mediated syndecan-1 shedding facilitates cell migration and wound closure through its effects on alpha(2)beta(1) integrin activation [124]. MMP-10 (or stromelysin) appears to control inflammation during pathogenic colonization of bacteria via modulation of macrophage phenotype [125]. MMP-7 and MMP-10 are increased in the CF airway epithelium and alveolar macrophages, respectively [123,125]. Whilst it is clear that many MMPs contribute to the co-ordination of initiation and termination of the host immune response as well as roles in injury repair, more studies are needed to pinpoint whether persistently high levels of MMP activity in chronic lung diseases such as CF have a net destructive or beneficial effect.
Increased salivary syndecan-1 level is associated with salivary gland function and inflammation in patients with Sjögren’s syndrome
Published in Scandinavian Journal of Rheumatology, 2022
NY Lee, NR Kim, JW Kang, G Kim, M-S Han, JA Jang, D Ahn, JH Jeong, M-H Han, EJ Nam
Syndecan-1 (SDC-1) is a transmembrane heparin sulphate proteoglycan consisting of glycosaminoglycan chains including heparin sulphate and chondroitin sulphate, and core protein (4, 5). SDC-1 is predominantly expressed on epithelial and plasma cells (4, 5) and induced by growth factors (6, 7). SDC-1 functions primarily as a co-receptor by binding to and regulating numerous heparin sulphate-binding molecules, including growth factors, cytokines, chemokines, matrix molecules, and enzymes such as metzincin proteases, thereby affecting cell proliferation, adhesion, and motility (4, 5, 8). SDC-1 also exists in a soluble form through ectodomain shedding mediated by sheddases, such as matrix metalloproteinase (MMP)-2, MMP-3, MMP-7, MMP-9, and MMP-14 (4, 9, 10). SDC-1 ectodomain shedding constitutes an important regulatory mechanism because it rapidly changes surface receptor dynamics and generates soluble ectodomains that can behave as paracrine or autocrine effectors, or competitive inhibitors (4, 10). The shedding mechanism may be induced by inflammatory mediators, including cytokines, chemokines, growth factors, and cell stress (4, 5). Therefore, an inflammatory milieu with increased expression of such mediators along with MMPs (11–19) may induce SDC-1 shedding and alter SDC-1 expression on SGECs in the glands of patients with SS.