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The S100A7/8/9 Proteins: Novel Biomarker and Therapeutic Targets for Solid Tumor Stroma
Published in Surinder K. Batra, Moorthy P. Ponnusamy, Gene Regulation and Therapeutics for Cancer, 2021
Sanjay Mishra, Dinesh Ahirwar, Mohd W. Nasser, Ramesh K. Ganju
The deregulated expression of S100A7 has been reported in several tumors of epithelial origins but little is known about its expression in melanocyte-derived tumors of neuroectodermal origin. Petersson et al. have analyzed the differential expression of S100 proteins by using SAGE Genie informatics [28]. In this study, they have not found any significant changes in differential expression of S100A4, S100A7, S100A8, S100A9 and S100A11 in melanocytes and melanocytic lesions. But, one study reported by another group has identified the increased level of S100A7 in the urine of patients with melanoma (77%, 24 out of 31) as compared to healthy subjects (41%, seven out of 17) and patients with different types of cancer (53%, 39 out of 73) [29]. But, till date no study has been reported about its role in metastasis and angiogenesis in melanoma.
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.
Serum S100A6, S100A8, S100A9 and S100A11 proteins in colorectal neoplasia: results of a single centre prospective study
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2020
Paula Moravkova, Darina Kohoutova, Jaroslava Vavrova, Jan Bures
S100A11, also known as calgizzarin or S100C, was first discovered by DeVries et al. in 1989 [31]. Overexpression of calgizzarin has been observed in colorectal cancer tissue in multiple studies [14,19,32,33]. In comparison with other S100 proteins, predominant nuclear localisation of S100A11 has been postulated in normal tissues [34,35]. Interestingly, Cross at al. showed translocation of S100A11 from the nucleus into the cytoplasm in tumours, which is presumed to lead to decreased nuclear concentrations of p21 and p13 (negative regulators of cell growth), thus leading to an increased cell proliferation [36]. We assume, that the movement of S100A11 from the nucleus to the cytoplasm could also lead to a significantly decreased gene transcription and subsequent decreased release of S100A11 protein into the extracellular area, which would explain why our results showed lower levels of serum S100A11 in those with colorectal neoplasia.
S100B protein: general characteristics and pathophysiological implications in the Central Nervous System
Published in International Journal of Neuroscience, 2022
Ana Cristina Arrais, Lívia Helena M. F. Melo, Bianca Norrara, Marina Abuquerque B. Almeida, Kalina Fernandes Freire, Acydalia Madruga M. F. Melo, Lucidio Clebeson de Oliveira, Francisca Overlânia Vieira Lima, Rovena Clara G. J. Engelberth, Jeferson de Souza Cavalcante, Dayane Pessoa de Araújo, Fausto Pierdoná Guzen, Marco Aurelio M. Freire, José Rodolfo L. P. Cavalcanti
S100 proteins are present in all cells of chondrogenic origin, whether normal, arthritic or neoplastic. The expression of S100A1 is associated with the differentiation status of human articular chondrocytes, a fact observed in vitro (26). These members are dysregulated in some types of neoplasia and other diseases, such as gastric cancer, which presents high expression of S100A2, S100A4, S100A8, S100A10 and S100A11, as well as S100A14, which appeared as a useful classification marker and prognosis for this same type of pathology. S100A4, S100A8 and S100A11 are altered in other types of tumors, such as colorectal, pancreas and prostate, where S100A6, S100A9 and S100P also present altered expression (27).
Plasma insulin-like growth factor binding protein 1 in pulmonary arterial hypertension
Published in Scandinavian Cardiovascular Journal, 2021
Habib Bouzina, Roger Hesselstrand, Göran Rådegran
In the present PAH population, plasma S100A11 was found to be higher than in controls. S100A11 is an EF-hand calcium-binding protein, that is overexpressed in tumours including ccRCC [32]. This protein has been suggested to have a role in the protection of invasive cancer cells [33]. In human pulmonary artery smooth muscle cells, S100A11 has been shown to be important for cellular migration elicited by hypoxia-induced mitogenic factor [34].