scholarly journals Tensin links energy metabolism to extracellular matrix assembly

2017 ◽  
Vol 216 (4) ◽  
pp. 867-869 ◽  
Author(s):  
Emmanuel Dornier ◽  
Jim C. Norman
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Energy Metabolism ◽  
Protein Kinase ◽  
Adenosine Monophosphate ◽  
Matrix Assembly ◽  
Cellular Processes ◽  
Metabolic Sensor ◽  
Fibrillar Adhesion ◽  
Α5β1 Integrin

The regulation of integrin function is key to fundamental cellular processes, including cell migration and extracellular matrix (ECM) assembly. In this issue, Georgiadou et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201609066) report that the metabolic sensor adenosine monophosphate–activated protein kinase influences tensin production to regulate α5β1-integrin and fibrillar adhesion assembly and thus reveal an important connection between energy metabolism and ECM assembly.

Establishment of substratum polarity in the blastocoel roof of the Xenopus embryo

Development ◽  
1999 ◽  
Vol 126 (9) ◽  
pp. 1975-1984 ◽  
Author(s):  
M. Nagel ◽  
R. Winklbauer
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Signaling Pathways ◽  
Fibril Formation ◽  
Fgf Signaling ◽  
Matrix Assembly ◽  
Mesoderm Cell ◽  
Guidance Cues ◽  
Mesoderm Formation ◽  
Fibronectin Fibrils

The fibronectin fibril matrix on the blastocoel roof of the Xenopus gastrula contains guidance cues that determine the direction of mesoderm cell migration. The underlying guidance-related polarity of the blastocoel roof is established in the late blastula under the influence of an instructive signal from the vegetal half of the embryo, in particular from the mesoderm. Formation of an oriented substratum depends on functional activin and FGF signaling pathways in the blastocoel roof. Besides being involved in tissue polarization, activin and FGF also affect fibronectin matrix assembly. Activin treatment of the blastocoel roof inhibits fibril formation, whereas FGF modulates the structure of the fibril network. The presence of intact fibronectin fibrils is permissive for directional mesoderm migration on the blastocoel roof extracellular matrix.

Role of Adenosine Monophosphate-Activated Protein Kinase on Cell Migration, Matrix Contraction, and Matrix Metalloproteinase-1 and Matrix Metalloproteinase-2 Production in Nasal Polyp–Derived Fibroblasts

2017 ◽  
Vol 31 (6) ◽  
pp. 357-363 ◽  
Author(s):  
Ti-Young Um ◽  
Seoung-Ae Lee ◽  
Joo-Hoo Park ◽  
Jae-Min Shin ◽  
Il-Ho Park ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Matrix Metalloproteinase ◽  
Nasal Polyp ◽  
Nasal Polyps ◽  
Tissue Remodeling ◽  
Adenosine Monophosphate ◽  
Compound C ◽  
Matrix Contraction

Purpose Activation of adenosine monophosphate-activated protein kinase (AMPK) by metformin, as a master regulator of metabolism, is involved in airway tissue remodeling. Here, we investigated the physical role of AMPK on cell migration, matrix contraction, and the production of matrix metalloproteinases (MMP) in nasal polyp–derived fibroblasts (NPDF). Methods Primary NPDFs from six patients with chronic rhinosinusitis and nasal polyps were isolated and cultured. To assess the effect of AMPK on fibroblast migration, we conducted scratch and migration assays in NPDF treated with metformin and/or compound C. A collagen gel contraction assay measured activity of contractile. MMP expression was measured with reverse transcription-polymerase chain reaction, Western blot, and zymography. To evaluate for specific AMPK action, we examined by AMPK small interfering RNA. Results Metformin, an activator of AMPK, significantly inhibited cell migration in NPDFs in a dose-dependent manner. Compound C, an inhibitor of AMPK, partially reversed the inhibitory effect of metformin. Metformin also significantly decreased contractile activity, with a concomitant reduction in the production of MMP-1 and MMP-2 but not of MMP-9. Specific silencing that targeted AMPK resulted in the enhancement of mobility and contractility and in the production of MMP-1 and MMP-2. Conclusion AMPK played an important role in regulating cell migration, matrix contraction, and MMP production in NPDFs, which provided data that AMPK activator might be a therapeutic target for the prevention of tissue remodeling in nasal polyps.

scholarly journals AMP-Activated Protein Kinase Regulates the Cell Surface Proteome and Integrin Membrane Traffic

2021 ◽  
Author(s):  
Antonescu Costin ◽  
Eden Ross ◽  
Rehman Ata ◽  
Thanusi Thavarajah ◽  
Sergei Medvedev ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Cell Surface ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Metabolic Sensor ◽  
Acute Changes ◽  
Surface Proteome ◽  
Amp Activated Protein Kinase ◽  
Cell Surface Proteome

The cell surface proteome controls numerous cellular functions including cell migration and adhesion, intercellular communication and nutrient uptake. Cell surface proteins are controlled by acute changes in protein abundance at the plasma membrane through regulation of endocytosis and recycling (endomembrane traffic). Many cellular signals regulate endomembrane traffic, including metabolic signaling; however, the extent to which the cell surface proteome is controlled by acute regulation of endomembrane traffic under various conditions remains incompletely understood. AMP-activated protein kinase (AMPK) is a key metabolic sensor that is activated upon reduced cellular energy availability. AMPK activation alters the endomembrane traffic of a few specific proteins, as part of an adaptive response to increase energy intake and reduce energy expenditure. How increased AMPK activity during energy stress may globally regulate the cell surface proteome is not well understood. To study how AMPK may regulate the cell surface proteome, we used cell-impermeable biotinylation to selectively purify cell surface proteins under various conditions. Using ESI-MS/MS, we found that acute (90 min) treatment with the AMPK activator A-769662 elicits broad control of the cell surface abundance of diverse proteins. In particular, A-769662 treatment depleted from the cell surface proteins with functions in cell migration and adhesion. To complement our mass spectrometry results, we used other methods to show that A-769662 treatment results in impaired cell migration. Further, A-769662 treatment reduced the cell surface abundance of β1-integrin, a key cell migration protein, and AMPK gene silencing prevented this effect. While the control of the cell surface abundance of various proteins by A-769662 treatment was broad, it was also selective, as this treatment did not change the cell surface abundance of the transferrin receptor. Hence, the cell surface proteome is subject to acute regulation by treatment with A-769662, at least some of which is mediated by the metabolic sensor AMPK.

scholarly journals Prostaglandin F2 Alpha Triggers the Disruption of Cell Adhesion with Cytokeratin and Vimentin in Bovine Luteal Theca Cells

Animals ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 1073
Author(s):  
Sang-Hee Lee ◽  
Seunghyung Lee
Keyword(s):  
Cell Migration ◽  
Cell Adhesion ◽  
Protein Kinase ◽  
Cell Structure ◽  
Control Group ◽  
Theca Cells ◽  
Cellular Processes ◽  
Prostaglandin F2 Alpha ◽  
Bovine Corpus Luteum ◽  
Cell Cell

Intermediate filaments (IFs) maintain cell–cell adhesions and are involved in diverse cellular processes such as cytokinesis, cell migration and the maintenance of cell structure. In this study, we investigated the influence of prostaglandin F2 alpha (PGF2α) on cytokeratin and vimentin IFs, Rho-associated protein kinase (ROCK), and cell-cell adhesion in bovine luteal theca cells (LTCs). The luteal cells were isolated from bovine corpus luteum (CL), and the LTCs were treated with 0, 0.01, 0.1 and 1.0 mM PGF2α. Cytokeratin, vimentin and desmoplakin proteins were disrupted and the ROCK protein was significantly increased in PGF2α-treated LTCs. In addition, cell–cell adhesion was significantly (p < 0.05) decreased in the PGF2α-induced LTCs compared to control group (0 mM PGF2α). In conclusion, PGF2α affected the adhesion of cell to cell via disruption of desmoplakin, cytokeratin and vimentin, additionally increasing ROCK in bovine LTCs. These results may provide a better understanding of the mechanism of bovine CL regression.

scholarly journals Study of the AMP-activated protein kinase role in energy metabolism changes during the postmortem aging of yak longissimus lumborum

2019 ◽  
Author(s):  
Yayuan Yang ◽  
Ling Han ◽  
Qunli Yu ◽  
Yongfang Gao ◽  
Rende Song
Keyword(s):  
Energy Metabolism ◽  
Protein Kinase ◽  
Opposite Effect ◽  
Ph Value ◽  
Physiological Mechanism ◽  
Adenosine Monophosphate ◽  
Postmortem Aging ◽  
Longissimus Lumborum ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase

AbstractTo explore the postmortem physiological mechanism of muscle, activity of adenosine monophosphate activated protein kinase (AMPK) as well as its role in energy metabolism of postmortem yaks were studied. In this experiment, we injected 5-amino-1-beta-d-furanonyl imidazole-4-formamide (AICAR), a specific activator of AMPK, and the specific AMPK inhibitor STO-609, to observe the changes in glycolysis, energy metabolism, AMPK activity and AMPK gene expression (PRKA1 and PRKA2) in postmortem yaks during maturation. The results showed that AICAR could increase the expression of the PRKKA1 and PRKAA2 genes, activate AMPK and increase its activity. The effects of AICAR include a lower concentration of ATP, an increase in AMP production, an acceleration of glycolysis, an increase in the lactic acid concentration, and a decrease in the pH value. In contrast, STO-609 had the opposite effect. Under hypoxic adaptation, the activity of the meat AMPK increased, which accelerated glycolysis and metabolism, and more effectively regulated energy production.

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