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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.
The National PTSD Brain Bank: Honoring the Vision and Contributions of Dr. Matthew Friedman
Published in Psychiatry, 2022
Impressive early successes have been reported in studies from the NPBB. Ursano et al. (2007) reported that p11 protein, also known as S100A10, is overexpressed in prefrontal cortex area 46 in the PTSD postmortem brain, compared with age- and sex-matched controls. These findings were validated in an animal model of PTSD in which p11 expression was upregulated in the prefrontal cortex of rats exposed to inescapable shock. Of note, the authors determined whether p11 could serve as a peripheral blood biomarker for PTSD. They measured p11 gene expression in peripheral blood mononuclear cells in 13 PTSD patients and 15 healthy controls, as assessed by real-time polymerase chain reaction (PCR). They found that p11 messenger RNA (mRNA) significantly decreased in PTSD patients compared to controls. These findings provide evidence that p11 gene expression is downregulated in peripheral blood, although it is upregulated in the brain. They also provide preliminary support for p11 as a therapeutic target in PTSD, given that the glucocorticoid receptor antagonist RU486 attenuates p11 expression. These findings, while preliminary and involving small samples, provided proof of concept for the value of a PTSD brain bank for accelerating knowledge of the neurobiology of PTSD and identification of novel targets for pharmacological treatment.
Annexin A2 promotes development of retinal neovascularization through PI3K/ AKT signaling pathway
Published in Current Eye Research, 2022
Chenyue Li, Zichang Zhao, Shihong Zhao
Of note, numerous studies have reported that upregulation of ANXA2 on extracellular localization has a profound impact on invasion and migration of cells and is directly correlated with neovascularization in cancers. ANXA2 can be phosphorylated and subsequently bind to S100A10, which acts as a precondition for the localization of its translocation to the cell surface.8,9 ANXA2 complex can prominently accelerate the conversion of plasminogen (Plg) to plasmin as a cell surface receptor for Plg and tissue plasminogen activator. As a result, a cascade of matrix metalloproteinases including MMP2 and MMP9 can be activated10 and ultimately lead to the degradation of fibrin, fibronectin, laminin, and several kinds of collagen.11 Studies recapitulate that fibrin can accumulate within micro vessels of mice deficient in ANXA2, and their isolated endothelial cells are unable to support tPA-dependent plasminogen activation in vivo.12
DLC1 inhibits lung adenocarcinoma cell proliferation, migration and invasion via regulating MAPK signaling pathway
Published in Experimental Lung Research, 2021
Niu Niu, Xingjie Ma, Haitao Liu, Junjie Zhao, Chao Lu, Fan Yang, Weibo Qi
For the development of targeted therapy against LUAD, effective target genes are emerging to be vital significant. Numerous studies proved that mRNA is closely associated with the diagnosis and prognosis of LUAD and plays a regulatory role in tumor malignant progression. Koh YW et al.8 found that high expression of aldehyde dehydrogenase-1 (ALDH1) improves the prognosis of LUAD. Li B et al.9 reported that low expression of surfactant protein C (SFTPC) is associated with poor overall survival of LUAD patients, and overexpression of SFTPC can inhibit tumor cell proliferation. Recent studies show that Deleted in Liver Cancer 1 (DLC1) has received increasing attention as a metastasis suppressor gene in various cancers including lung cancer.10 DLC1 was initially identified as a deleted or down-regulated gene in primary hepatocellular carcinoma (HCC), and it exerts its tumor suppressive role mainly through the Rho-GTPase-activating protein (RhoGAP) domain.11,12 Yang X et al.13 discovered that DLC1 can inhibit in vitro migration, invasion, colony formation and anchorage-independent growth of aggressive lung cancer cells by interacting with S100A10. Besides, DLC1 expression is significantly associated with the prognosis of patients with LUAD.14 Collectively, these findings suggest that DLC1 may play a role in malignant progression of LUAD, thereby to make an effect on the prognosis of patients.