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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.
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
S100A6 protein, also known as calcyclin, is a member of S100 subfamily of EF-hand calcium-binding proteins. Tissue overexpression of S100A6 has been confirmed in gastric, pancreatic and colorectal carcinoma [9,21–23]. Recently, Feng et al. documented very important findings having carried out experiments on human colon cancer cell lines: they have proven, that S100A6 is required for the calcium-dependent translocation of ‘Calcyclin binding protein/Siah-1 interacting protein’ from the cytosol into the nucleus. Its nuclear accumulation is related to the proliferation of cancer cells [24]. To our knowledge, only five studies evaluated serum S100A6 in relation to cancer in human individuals so far. Three of them showed elevated serum S100A6 in patients with gastric cancer, urothelial carcinoma and with early stages of non-small lung cell carcinoma [25–27]. Another two studies focussed on serum S100A6 levels in patients with cholangiocarcinoma: Loosen et al. observed unaltered serum S100A6 despite proven tissue overexpression of S100A6 [28]. On contrary, Onsurahtum et al. confirmed significantly elevated serum S100A6 levels. This could be explained by presence of O. viverrini infection in association with cholangiocarcinoma in the Thailand population compared to the results in the previously studied European population [28,29].
Upregulation of S100A6 in patients with endometriosis and its role in ectopic endometrial stromal cells
Published in Gynecological Endocrinology, 2018
Yaoming Peng, Jiabin Lin, Junyan Ma, Kaiqing Lin, Kaihong Xu, Jun Lin
S100A6 is a member of the S100 family of Ca2+-binding proteins, which was first purified from Ehrlich ascites tumor cells [5]. Previous research demonstrates that S100A6 regulates many cellular and molecular functions such as proliferation, apoptosis, cell-cycle, differentiation and cytoskeletal constituents [6]. In recent years, up-regulated S100A6 has been found in several cancer types, such as breast, stomach, pancreas and colon cancer [7–8]. The expression of S100A6 is also associated with enhanced invasiveness of tumor cells and poor survival in some cancers [9–11]. A recent study demonstrated that S100A6 was highly expressed in eutopic ESCs, inhibition of S100A6 expression suppressed β-catenin expression and reduced the migratory and proliferatory ability of eutopic ESCs [12]. However, the expression of S100A6 in endometriosis tissues and the effect of S100A6 on ectopic ESCs and the underlying mechanisms is still unknown.
RAGE receptor targeted bioconjuguate lipid nanoparticles of diallyl disulfide for improved apoptotic activity in triple negative breast cancer: in vitro studies
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2018
Venkata Talluri Siddhartha, Sai Kiran S. S. Pindiprolu, Pavan Kumar Chintamaneni, Shashank Tummala, S. Nandha Kumar
Receptor for advanced glycation end-products (RAGE) is a multi-ligand cell-surface receptor belongs to immunoglobulin super family which has inbuilt affinity to interact with advanced glycation end products (AGE) [9,10]. Recently, many studies have demonstrated the role of RAGE in various cancer pathologies, where the upregulation of RAGE was reported to be oncogenic by activating various oncogenic signalling pathways [11,12]. It was reported that, interaction of RAGE with its ligands like, AGE [13], S100/Calgranulin [14], HMGB1 and the S100 family of proteins (S100A4, S100A6, S100A7, S100A9) stimulate P38 and P44/42, MAP kinase Ras-extracellular signal-regulated kinase and NF-κβ to promote tumour progression. Recently, Nasser et al (2015) reported that RAGE-S100A7 signalling axis is associated with metastasis in TNBC. In another study, it was found that there is over expression of RAGE in TNBC cells than MCF-7/SK-Br-3 luminal breast cancer cells [15–17]. We, therefore, hypothesize that RAGE-targeted delivery of cytotoxic drugs might have potential to achieve radical cure by selectively targeting TNBC and also RAGE inhibition can sensitize cancer cells to cytotoxic effects. As a proof of the concept in this study, we propose RAGE receptor targeted delivery of diallyl disulfide (DADS), an organosulfur ingredient of garlic with cytotoxic activity against breast cancer to achieve enhanced antitumour activity.