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Neuromuscular Physiology
Published in Michael H. Stone, Timothy J. Suchomel, W. Guy Hornsby, John P. Wagle, Aaron J. Cunanan, Strength and Conditioning in Sports, 2023
Michael H. Stone, Timothy J. Suchomel, W. Guy Hornsby, John P. Wagle, Aaron J. Cunanan
Globular actin (G-actin) is polymerized and forms F-actin. Two F-actins wrap around each other in an alpha-helix to form an actin myofilament. The regulatory proteins troponin and tropomyosin (forming regulatory units) are embedded in regular intervals in the actin myofilament.
Clinical Applications of Gene Therapy for Immuno-Deficiencies
Published in Yashwant Pathak, Gene Delivery, 2022
Khushboo Faldu, Sakshi Gurbani, Jigna Shah
WAS, X-linked inheritable PID presents itself as autoimmunity, recurrent infections, tendency to develop lymphoid cancer, macrothrombocytopenia, and severe eczema. WAS gene mutation hinders WAS protein (WASp) which is essential for actin polymerization. Actin is crucial for entire hematopoietic lineages, as it plays an important role in formation of immunological synapse, cell migration, and cytotoxicity [46]. AlloHSCT has provided conservative benefits in WAS, with benefits deteriorating for patients aged more than five years [27]. γRV vectors led to the development of leukemogenesis [47]. A SIN-LV vector utilizing a fragment of endogenous WAS gene promoter, together with fludarabine and busulfan conditioning, is showing promise in clinical trials with patients not requiring Ig-replacement therapy [48]. Yet the platelet counts were below normal, maybe attributed to WASp expression in platelet precursors [49, 50].
Ethnomedicinal and Pharmacological Importance of Glycyrrhiza glabra L
Published in Mahendra Rai, Shandesh Bhattarai, Chistiane M. Feitosa, Wild Plants, 2020
Ashish K. Bhattarai, Sanjaya M. Dixit
GA induces actin disruption and has tumor cell-selective toxic properties, and its selectivity is superior to those of all the clinically available antitumor agents tested in this study. The cytotoxic activity of GA and the tested antitumor agents showed a better correlation with the partition coefficient (log P) values rather than the polar surface area (PSA) values. For selective toxicity against tumor cells, GA was most effective at 10 μM (Yamaguchi et al. 2010).
Novel ligands and modulators of triggering receptor expressed on myeloid cells receptor family: 2015-2020 updates
Published in Expert Opinion on Therapeutic Patents, 2021
Harbinder Singh, Vikrant Rai, Sunil K. Nooti, Devendra K. Agrawal
Actin is a family of multi-functional globular proteins present in all eukaryotic cells which has been found to participate in various cellular processes, including muscle contraction, cell division and cytokinesis, cell motility, cell signaling, etc. It was observed that actin could activate the inflammatory response by interacting through TREM-1 [56]. There was a controversy on the presence of actin on the cell surface since actin is a cellular cytoskeleton protein. Besides its presence in the cytoplasm, its distribution was also detected on the surface of platelets in the resting state [57]. Therefore, platelets provide surface actin for TREM-1 recognition to activate signaling. In 2017, Fu et al. found that recombinant actin can directly interact with the recombinant TREM-1 extracellular domain and enhance inflammatory response when injected in wild-type mice but not in TREM-1−/- mice. This amplification of inflammatory response could be inhibited by peptide LP17. It was confirmed that the extracellular actin is co-localized with TREM-1 in the lung tissues of septic mice [56].
TiO2 nanotubes regulate histone acetylation through F-actin to induce the osteogenic differentiation of BMSCs
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2021
Yanchang Liu, Zhicheng Tong, Chen Wang, Runzhi Xia, Huiwu Li, Haoran Yu, Juehua Jing, Wendan Cheng
Cytoskeleton is a kind of cell scaffold in cytoplasm. It maintains cell shape, provides mechanical strength, directs movement, regulates chromosome segregation during mitosis and meiosis, and intracellular organelle transport [10,11]. Actin microfilament is the main structure of cytoskeleton. Actin exists in cells in the form of globular/monomer actin (G-actin) or fibrous actin (F-actin), in which the F-actin is the main part of the cytoskeleton, which can quickly aggregate and depolymerize and is directly related to the adhesion, extension and migration of cells. F-actin provides mechanical support for cells, influences the tension in the cytoskeleton, and provides pathways through the cytoplasm to help signal transduction [12,13]. F-actin has been shown to induce lipid differentiation in cultured BMSCs [14]. The role of actin dynamics in the differentiation of chondrocytes from BMSCs has also been supported by numerous experiments. F-actin interfering compounds, such as Cytochalasin D, can induce cartilage differentiation [15]. Previous studies have found that F-actin in the cytoskeleton is very sensitive to external mechanical and physical signal stimulation. On the metal surface, the aggregation of F-actin is more obvious, forming a stronger cytoskeleton. On the surface of the hydrogel, the polymerization of F-actin is weakened. And the change of cytoskeleton is accompanied by the change of cell morphology and the expression of differentiation-related markers [16]. Therefore, F-actin itself can be used as a bridge for mechanical signals to regulate cell biological behaviour.
Regulation of differentiation of MEG01 to megakaryocytes and platelet-like particles by Valproic acid through Notch3 mediated actin polymerization
Published in Platelets, 2019
Ankita Dhenge, Rutuja Kuhikar, Vaijayanti Kale, Lalita Limaye
Levels of polymerized (F-actin) and depolymerized (G-actin) forms of actin were measured. Equal numbers (0.5X106) of untreated and VPA-treated cells were lysed in actin stabilizing buffer (0.1 M PIPES [piperazine-N,N0-bis{2-ethane-sulfonic acid}], 30% glycerol, 5% DMSO, 1mM MgSO4,1mM EGTA, 1% Triton X-100,1mM ATP and 40 mg/mL protease inhibitor cocktail). The cells were dislodged by scraping, and entire extract was centrifuged at 4°C for 75 min at 16000g. The supernatant containing G-actin was separated, and the pellet containing F-actin was solubilized with actin depolymerization buffer (0.1 M PIPES pH = 6.9, 1mM MgSO4, 10mM CaCl2, 5μM Cytochalasin D). The supernatant and the pellets were resuspended separately in protein lysis buffer and analyzed by western blotting with β-actin antibody.