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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
The S100 proteins are a family of low-molecular-weight (9–13 kDa), ubiquitously expressed vertebrate proteins. They are called S100 because of their solubility in a 100% saturated solution with ammonium sulfate at neutral pH, as discovered by B. W. Moore in 1965. Each of them has two calcium binding EF-hand motifs in the monomer and forms antiparallel homodimers and occasionally heterodimers within themselves (e.g., S100A8/A9) and other proteins. They are not enzymes, but they are calcium-activated molecular switches similar to calmodulin or troponin C. They have pleiotropic intracellular and extracellular functions, for example, proliferation, differentiation, migration, energy metabolism, Ca2+ homeostasis, inflammation, and cell death. There are at least 25 members of S100, and some of their specific functions include scavenging of ROS and NO (i.e., S100A8/A9), cytoskeleton assembly (e.g., S100A1, S100A4, S100A6, and S100A9), membrane protein docking and trafficking (e.g., S100A10 and S100A12), transcription regulation and DNA repair (e.g., S100A4, S100A11, S100A14, and S100B), cell differentiation (e.g., S100A6, S100A8/A9, and S100B), release of cytokines and antimicrobial agents (degranulation) (e.g., S100A8/A9, S100A12, and S100A13), muscle cell contractility (e.g., S100A1), cell growth and migration (e.g., S100A4, S100A8/A9, S100B, and S100P), and apoptosis (e.g., S100A6, S100A9, and S100B). The S100 proteins, once extracellular, are saturated with calcium and do not act as a calcium sensing switch, but can now scavenge other transition metal ions, for example, Zn, Cu, and Mn, which might be part of their antimicrobial action.
Effects of Type 2 Diabetes Mellitus on Gene Expressions of Mouse Meibomian Glands
Published in Current Eye Research, 2020
Erdost Yıldız, Noushin Zibandeh, Berna Özer, Afsun Şahin
We also focused on gene ontologies for biological processes which involve in lipid metabolism, inflammatory and immune response pathway, process of cell growth, cell differentiation and apoptosis (Supplementary Table 1). Some of the related biological processes with up-regulated genes in lipid metabolism are fatty acid biosynthesis (Scd4), fatty acid oxidation (Alox12) and negative regulation of lipid biosynthesis (Serpina12). Also, we have demonstrated innate immune response (Ang1, Fcer1g, Ighg, Ighm, Igh-VJ558, Trim59), inflammatory response (Kng1, Stab1, Tnfrsf4), positive regulation of I-kappa-b kinase/NF-kappa-b signaling (Atp2c1,S100a13) and cellular response to oxidative stress (Chchd4, Prdx2) in up-regulated biological processes about immune response and inflammation; positive regulation of apoptosis (Aldh1a3, Aldh1a7, Alox12) and apoptotic process (Rmdn3, Serpina3g) in up-regulated biological processes about apoptosis.
Update on: proteome analysis in thyroid pathology – part II: overview of technical and clinical enhancement of proteomic investigation of the thyroid lesions
Published in Expert Review of Proteomics, 2018
Isabella Piga, Stefano Casano, Andrew Smith, Silvia Tettamanti, Davide Leni, Giulia Capitoli, Angela Ida Pincelli, Marcella Scardilli, Stefania Galimberti, Fulvio Magni, Fabio Pagni
Forty-one and fifty-nine proteins were found to be differentially expressed in cPTC versus benign lesion by univariate and multivariate analysis, respectively. Among them, WB analyses of cyst fluid and IHC on tissue specimens from the same patients verified the up-regulation of cytokeratin 19 (CK-19) and S100A13 in cPTC. Moreover, ELISA on non-depleted cyst fluids from cPTCs (n = 17) and benign lesions (n = 55) suggested that for CK-19 a cut-off at > 55 ng/ml resulted in 82% specificity and sensitivity whilst for S100A13 a cut-off at > 230 pg/ml gave better sensitivity (94%), but very poor specificity (35%).