STATs in Cell Mobility and Polarity during Morphogenetic Movement

2003 ◽  
pp. 595-607 ◽  
Author(s):  
Susumu Yamashita ◽  
Toshio Hirano
Keyword(s):  
Morphogenetic Movement ◽  
Cell Mobility

Beam Management in mmWave 5G NR: an Intra-Cell Mobility Study

2021 ◽  
Author(s):  
Filipa Fernandes ◽  
Christian Rom ◽  
Johannes Harrebek ◽  
Gilberto Berardinelli
Keyword(s):  
Cell Mobility ◽  
Mobility Study

scholarly journals Ubl4A is required for insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching

2015 ◽  
Vol 112 (31) ◽  
pp. 9644-9649 ◽  
Author(s):  
Yu Zhao ◽  
Yuting Lin ◽  
Honghong Zhang ◽  
Adriana Mañas ◽  
Wenwen Tang ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Glycogen Synthesis ◽  
Membrane Translocation ◽  
Insulin Stimulation ◽  
Serine Threonine Kinase ◽  
Newborn Mice ◽  
Threonine Kinase ◽  
Cell Mobility ◽  
Close Proximity ◽  
Extracellular Stimuli

The serine-threonine kinase Akt is a key regulator of cell proliferation and survival, glucose metabolism, cell mobility, and tumorigenesis. Activation of Akt by extracellular stimuli such as insulin centers on the interaction of Akt with PIP3 on the plasma membrane, where it is subsequently phosphorylated and activated by upstream protein kinases. However, it is not known how Akt is recruited to the plasma membrane upon stimulation. Here we report that ubiquitin-like protein 4A (Ubl4A) plays a crucial role in insulin-induced Akt plasma membrane translocation. Ubl4A knockout newborn mice have defective Akt-dependent glycogen synthesis and increased neonatal mortality. Loss of Ubl4A results in the impairment of insulin-induced Akt translocation to the plasma membrane and activation. Akt binds actin-filaments and colocalizes with actin-related protein 2 and 3 (Arp2/3) complex in the membrane ruffles and lamellipodia. Ubl4A directly interacts with Arp2/3 to accelerate actin branching and networking, allowing Akt to be in close proximity to the plasma membrane for activation upon insulin stimulation. Our finding reveals a new mechanism by which Akt is recruited to the plasma membrane for activation, thereby providing a missing link in Akt signaling.

scholarly journals Urokinase-Type Plasminogen Activator System in Norm and in Life-Threatening Processes (Review)

2018 ◽  
Vol 14 (6) ◽  
pp. 61-79 ◽  
Author(s):  
Elena V. Kugaevskaya ◽  
Tatiana A. Gureeva ◽  
Olga S. Timoshenko ◽  
Nina I. Solovyeva
Keyword(s):  
Cell Mobility ◽  
Plasminogen Activator System ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Upa System ◽  
System Components ◽  
Life Threatening ◽  
Threatening Processes ◽  
Activator System ◽  
Pai 1

The multifunctional urokinase-type plasminogen activator system (uPA-system) includes serine proteinase — uPA or urokinase, its receptor (uPAR) and two inhibitors (PAI-1 and PAI-2). The review discusses the structural features and involvement of the system components in the development of life-threatening processes including carcinogenesis, inflammation, neurogenesis and fibrinolysis, in regulation of which the destruction of extracellular matrix (ECM), cell mobility and signaling inside and outside the cell play a decisive role. uPA triggers the processes by activating the plasminogen and its convertion into plasmin involved in the activation of matrix metalloproteinases (MMPs) in addition to the regulation of fibrinolysis. MMPs can hydrolyze all the major ECM components and therefore play a key role in invasion, metastasis, and cell mobility. MMPs activates a cassette of biologically active regulatory molecules and release them from ECM. uPAR, PAI-1 and PAI-2 are responsible for regulation of the uPA activity. In addition, being a signaling receptor, uPAR along with MMPs lead to the stimulation of a number of signaling pathways that are associated with the regulation of proliferation, apoptosis, adhesion, growth and migration of cells contributing to tumor progression, inflammation, chemotaxis, and angiogenesis. Effective participation of the uPA system components in ECM destruction and regulation of intracellular and extracellular signaling pathways demonstrates that the system significantly contributes to the regulation of various physiological and pathological processes.

scholarly journals Viscoelasticity and cell jamming state transition

2021 ◽  
Author(s):  
Ivana Pajic-Lijakovic ◽  
Milan Milivojevic
Keyword(s):  
Residual Stress ◽  
Wound Healing ◽  
Cell Migration ◽  
State Transition ◽  
State Transitions ◽  
Collective Cell Migration ◽  
Biological Processes ◽  
Cell Mobility ◽  
Controversial Topic ◽  
The Impact

Although collective cell migration (CCM) is a highly coordinated migratory mode, perturbations in the form of jamming state transitions and vice versa often occur even in 2D. These perturbations are involved in various biological processes, such as embryogenesis, wound healing and cancer invasion. CCM induces accumulation of cell residual stress which has a feedback impact to cell packing density. Density-mediated change of cell mobility influences the state of viscoelasticity of multicellular systems and on that base the jamming state transition. Although a good comprehension of how cells collectively migrate by following molecular rules has been generated, the impact of cellular rearrangements on cell viscoelasticity remains less understood. Thus, considering the density driven evolution of viscoelasticity caused by reduction of cell mobility could result in a powerful tool in order to address the contribution of cell jamming state transition in CCM and help to understand this important but still controversial topic. In addition, five viscoelastic states gained within three regimes: (1) convective regime, (2) conductive regime, and (3) damped-conductive regime was discussed based on the modeling consideration with special emphasis of jamming and unjamming states.

scholarly journals Crosstalk Between Abnormal TSHR Signaling Activation and PTEN/PI3K in the Dedifferentiation of Thyroid Cancer Cells

2021 ◽  
Vol 11 ◽  
Author(s):  
Fang Feng ◽  
Huiqin Han ◽  
Shuqi Wu ◽  
Hui Wang
Keyword(s):  
Thyroid Cancer ◽  
Cancer Cells ◽  
Mtor Signaling ◽  
Iodide Uptake ◽  
Thyroid Cells ◽  
Cell Mobility ◽  
Signaling Activation ◽  
Thyroid Cancer Cells ◽  
Serum Tsh

Iodide uptake and the metabolism of thyroid cells are regulated by thyrotropin (TSH)-TSH receptor (TSHR) signaling. Thus, it is necessary to elevate serum TSH levels by T4 withdraw or rTSH administration to facilitate radioiodide (131I) therapy for differentiated thyroid cancer (DTC). However, non-iodide-avid metastases of DTC which is dedifferentiated do not respond to stimulation by high levels of TSH, suggesting abnormal TSH-TSHR signal transduction in cancer cells. In addition, PI3K/AKT/mTOR signaling activation has been shown to be associated with the dedifferentiated phenotype of thyroid cancer, but the mechanism remains elusive. Therefore, in this study, we aimed to explore the role of abnormal TSH-TSHR signaling activation in regulating iodide uptake and cell mobility in thyroid cancer and its relationship with PI3K/AKT/mTOR signaling. We found that in thyroid cancer cells, TSH binds TSHR coupled to the Gα12/13 protein and then activates RhoA through interacting with leukemia associated RhoA guanine exchange factor (LARG). This results in a promigration tumorigenic phenotype independent of canonical TSHR-GαS signaling that regulates the expression of molecules involved in iodine uptake and metabolism. We observed that signaling pathways downstream of Gα12/13 signaling were increased, while that of Gαs signaling was decreased in thyroid cancer cells undergoing dedifferentiation compared to control cells following stimulation with different levels of TSH. PI3K/AKT/mTOR signaling activation enhanced Gα12/13 signaling through increasing LARG levels but also inhibited the expression of molecules downstream of Gαs signaling, including thyroid-specific molecules, and iodide uptake. In summary, our results demonstrate the noncanonical activation of TSH-TSHR signaling and its role in increasing the cell mobility and dedifferentiation of thyroid cancer through crosstalk with PI3K/AKT/mTOR signaling.

Fusobacterium nucleatum Promotes Gastric Cancer Aggressiveness through Upregulation of Cell Mobility and Interferon Genes

2020 ◽  
Author(s):  
Yung-Yu Hsieh ◽  
Shui-Yi Tung ◽  
Hung-Yu Pan ◽  
Te-Sheng Chang ◽  
Kuo-Liang Wei ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Fusobacterium Nucleatum ◽  
High Multiplicity ◽  
Cancer Tissue ◽  
Multiplicity Of Infection ◽  
Continuous Increase ◽  
Cell Mobility ◽  
Cancer Aggressiveness ◽  
Tissue Specimens

Abstract Background Fusobacterium nucleatum was previously found to become a dominant species in the gastric cancer-associated microbiota of patients from Taiwan. However, the prevalence of Fusobacterium nucleatum infection in gastric cancer has not been examined in a larger patient cohort. In addition, whether Fusobacterium nucleatum elicits a cellular response in gastric cancer remains unknown.Methods A study cohort of resected gastric cancer tissue specimens was examined using nested PCR to detect Fusobacterium nucleatum. In vitro coculture of Fusobacterium nucleatum was carried out to identify the alteration in the expression profile of patient-derived gastric cancer cell line.Results approximately one-third of gastric cancer tissues are positive for Fusobacterium nucleatum. Statistical analysis showed that the risk for Fusobacterium nucleatum infection is increased in late-stage cancer tissue specimens and incurs poorer survival in Helicobacter pylori-positive patients. In vitro coculture experiment shows a drastic interferon response activated only by a high multiplicity of infection, and the response peaks within 24 hours and subsides after 72 hours of incubation. Another set of response genes is the continuous increase of actins and their regulators with prolonged time of incubation, activated by both low and high multiplicity of infection.Conclusions Our data indicates that Fusobacterium nucleatum incites an inflammatory response from the cancer cells and promotes cell mobility, likely

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