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Interleukin-1
Published in Jason Kelley, Cytokines of the Lung, 2022
Timothy R. Aksamit, Gary W. Hunninghake
Activation of the IL-1 receptor by IL-1 leads to phosphorylation of several cellular proteins through the action of a PKC-independent serine/threonine kinase (Kaur and Saklatvala, 1988; Bird and Saklatvala, 1989). Proteins undergoing phosphorylation include the IL-1 receptor (Gallis et al., 1989), a heat-shock protein (Kaur et al., 1989), the EGF-receptor (Bird and Saklatvala, 1989), and L-plastin (Matsushima et al., 1988). Since there are no amino acid sequence similarities between the cytoplasmic domain of the human T-cell type IL-1 receptor and any other known protein kinases, it is likely that the IL-1 receptor directly or indirectly interacts with and activates another intracellular protein that is a distinct cellular kinase. Further characterization of this serine/threonine kinase remains to be defined.
Disorders in tHemostasis System and Changes in the Rheological Properties of the Blood in Ischemic Heart Disease and Diabetes Mellitus Patients
Published in E.I. Sokolov, Obesity and Diabetes Mellitus, 2020
In the appearance of pathological processes such as DIC and IHD, both qualitative and quantitative changes occur in the system of blood coagulation. First of all, the sensitivity to thrombin lowers and the process of polymerization of the fibrin monomers is disturbed. They partly form complex compounds with fibrinogen, probably with early products of the decomposition of fibrinogen by plastin. Products of paracoagulation appear — soluble fibrin-monomer complexes (SFMC). These large and medium-size molecular SFMC coagulate poorly under the influence of thrombin. This thrombin resistance of the complexes disturbs the normal transformation of fibrinogen into fibrin and may produce the phenomenon of the DIC syndrome (syndrome of disseminated intravascular coagulation).
Precision medicine in osteoporosis and bone diseases
Published in Debmalya Barh, Precision Medicine in Cancers and Non-Communicable Diseases, 2018
Fatmanur Hacievliyagil Kazanci, Fatih Kazanci, M. Ramazan Yigitoglu, Mehmet Gunduz
Juvenile osteoporosis is a group of heritable disorders that present during childhood. Decreased WNT signaling activity because of mutations in WNT1 itself and mutations in LRP5 (which encodes a coreceptor involved in Wnt/β-catenin signaling) have been reported to cause juvenile osteoporosis. Recently, mutations in the plastin 3 (PLS3) gene were identified in patients suffering from an X-linked variant of the disease (van Dijk, 2015).
Plastin 3 down-regulation augments the sensitivity of MDA-MB-231 cells to paclitaxel via the p38 MAPK signalling pathway
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Yan Ma, Wenjia Lai, Minzhi Zhao, Chunyan Yue, Fanghao Shi, Ren Li, Zhiyuan Hu
Herein, we report that another effector molecule, plastin 3 (PLS3), is involved in the regulation of PTX-induced apoptosis. PLS3 (a T-plastin, also named T-fimbrin) functions as filamentous actin (F-actin)-bundling protein to polymerize actin fibres by inhibiting depolymerization [16,17]. PLS3 plays an important role in early cancer diagnosis and therapy [18,19]. Since the 1980s, several studies have reported that PLS3 expression was associated with cellular resistance to chemotherapeutic drugs and cancer progression. Compared with the PLS3 expression level in cisplatin-sensitive human cancer cell lines (e.g. bladder, prostate, and head and neck cancer cell lines), that in their cisplatin-resistant counterparts was increased [20]. The down-regulation of PLS3 expression increased the sensitivity not only to cisplatin in bladder cancer cells but also to VP-16 in human liver cells [21]. These findings indicated that PLS3 may be a novel marker of drug resistance in cancer cells and that the relationship between its expression and drug sensitivity might be due to its involvement in apoptosis. However, the exact details behind the relevance of PLS3 expression to drug therapy and cancer progression are still unknown. In this present study, we sought to identify the role that PLS3 plays in PTX-induced apoptosis in cancer cells. To this end, we conducted PLS3 gene-silencing studies using a TNBC cell line, MDA-MB-231 and compared the responses of the gene-silenced cells under PTX and ABR exposure.
Advances in understanding the role of angiotensin-regulated proteins in kidney diseases
Published in Expert Review of Proteomics, 2019
Ana Belén Sanz, Adrian Mario Ramos, Maria Jose Soler, Maria Dolores Sanchez-Niño, Beatriz Fernandez-Fernandez, Maria Vanessa Perez-Gomez, Marta Ruiz Ortega, Gloria Alvarez-Llamas, Alberto Ortiz
In isolated proximal tubules from rats continuously infused with pressor or non-pressor doses of angiotensin II over 2 weeks, 14 phosphoproteins were altered by the pressor dose, including increased phosphorylation of the PKC isoenzymes, PKCα and PKCβII, and the glycogen synthase kinases, GSK3α and GSK3β [91]. Phosphorylation of the cAMP-response element binding protein 1 and PKCδ were decreased. By contrast, the phosphorylation of only seven proteins was altered by the non-pressor dose, which increased PKCα, PKCδ, and GSKα phosphorylation. ERK1/2 phosphorylation was increased in cultured proximal tubule cells but not in proximal tubules in vivo, implying potential cell culture-in vivo differences. Infusion of the pressor dose decreased, whereas the non-pressor dose increased NHE3 phosphorylation in proximal tubule membranes. These responses were largely AT1R-dependent and blocked by losartan [91]. More recently, the phosphoproteome of podocytes stimulated with angiotensin II was reported. Phosphorylated peptides were mainly related to actin filaments, cytoskeleton, lamellipodia, mammalian target of rapamycin, and MAPK signaling. Among others, the actin-bundling protein L-plastin (LCP1) was phosphorylated by several kinases and promoted filopodia formation [92].
Actin stabilizer TAGLN2 potentiates adoptive T cell therapy by boosting the inside-out costimulation via lymphocyte function-associated antigen-1
Published in OncoImmunology, 2018
Bu-Nam Jeon, Hye-Ran Kim, Yun Shin Chung, Bo-Ra Na, Hyunkyung Park, Chorong Hong, Yasmin Fatima, Hyeonju Oh, Chang-Hyun Kim, Chang-Duk Jun
Dynamic rearrangement of the actin cytoskeleton at the IS is absolutely necessary to sustain correct temporal and spatial control of the T-cell activation process.13,23 TCR stimulation results in actin polymerization.24 For full activation, however, T cells also require ‘outside-in’ costimulation, which leads to significant rearrangement of the actin cytoskeleton and promotes accumulation of receptors and raft membrane microdomains at the interface between T cells and APCs.10–12,25 These previous works imply that the artificial engineering of F-actin contents at the IS may mimic the signals evoked by costimulatory molecules. From this perspective, we utilized TAGLN2 as we found in a previous report that TAGLN2 increases F-actin contents through stabilization of F-actin in T cells during IS formation.17 Recently, we also found that TAGLN2 is significantly upregulated in macrophages in response to lipopolysaccharide and enhances macrophage phagocytic function,26 demonstrating that TAGLN2 plays an essential role in actin dynamics at the immunological or phagocytic synapses. In the present study, more strikingly, drastic down-regulation of TAGLN2 in T cells from severe E0771 tumor-bearing mice further emphasizes that TAGLN2 is an important actin regulator for cytotoxic T cell adhesion to tumor target cells. However, other proteins also can be considered. For instance, L-plastin, similar to TAGLN2, stabilizes actin filaments by means of its actin-bundling activity.27 In contrast, cofilin enhances actin polymerization via its actin-severing activity.28 Interestingly, we previously showed that TAGLN2 and cofilin localize to two distinguishable regions in the IS; cofilin localizes to the upper region of d-SMAC, where TAGLN2 is rather absent, and TAGLN2 localizes at the bottom of d-SMAC.17