scholarly journals Modulation of Glucose Takeup by Glucose Transport on the Isolated OHCs

2018 ◽  
Vol 2018 ◽  
pp. 1-7
Author(s):  
Xiao-ting Cheng ◽  
Feng-bo Yang ◽  
Qing-qing Jiang ◽  
Rong Zhang ◽  
Shi-ming Yang ◽  
...  

Glucose is a fundamental source of energy for mammalian cells; however, whether glucose is taken up through the lateral walls of cochlear outer hair cells (OHCs) is unknown. The OHC lateral wall is complex, composed of a plasma membrane, cortical lattice, and subsurface cisternae. This study assessed the uptake of glucose by OHCs using live-cell microscopy and examined the distribution of glucose transporter isoforms by immunohistochemistry. We found that glucose transporter-4 was mostly expressed on the lateral wall of OHCs. Glucose crossed the lateral walls of OHCs via glucose transporters-4 mainly, and this process could be modulated. These results suggest that the lateral walls are involved in modulating energy transport into OHCs.

2020 ◽  
Vol 117 (51) ◽  
pp. 32443-32452
Author(s):  
Ryan J. Schulze ◽  
Eugene W. Krueger ◽  
Shaun G. Weller ◽  
Katherine M. Johnson ◽  
Carol A. Casey ◽  
...  

Hepatocytes metabolize energy-rich cytoplasmic lipid droplets (LDs) in the lysosome-directed process of autophagy. An organelle-selective form of this process (macrolipophagy) results in the engulfment of LDs within double-membrane delimited structures (autophagosomes) before lysosomal fusion. Whether this is an exclusive autophagic mechanism used by hepatocytes to catabolize LDs is unclear. It is also unknown whether lysosomes alone might be sufficient to mediate LD turnover in the absence of an autophagosomal intermediate. We performed live-cell microscopy of hepatocytes to monitor the dynamic interactions between lysosomes and LDs in real-time. We additionally used a fluorescent variant of the LD-specific protein (PLIN2) that exhibits altered fluorescence in response to LD interactions with the lysosome. We find that mammalian lysosomes and LDs undergo interactions during which proteins and lipids can be transferred from LDs directly into lysosomes. Electron microscopy (EM) of primary hepatocytes or hepatocyte-derived cell lines supports the existence of these interactions. It reveals a dramatic process whereby the lipid contents of the LD can be “extruded” directly into the lysosomal lumen under nutrient-limited conditions. Significantly, these interactions are not affected by perturbations to crucial components of the canonical macroautophagy machinery and can occur in the absence of double-membrane lipoautophagosomes. These findings implicate the existence of an autophagic mechanism used by mammalian cells for the direct transfer of LD components into the lysosome for breakdown. This process further emphasizes the critical role of lysosomes in hepatic LD catabolism and provides insights into the mechanisms underlying lipid homeostasis in the liver.


1993 ◽  
Vol 31 (1-2) ◽  
pp. 225-228 ◽  
Author(s):  
Sally P. Weaver ◽  
John Hoffpauir ◽  
laura Schweitzer

2008 ◽  
Vol 121 (20) ◽  
pp. 3347-3356 ◽  
Author(s):  
K. Legendre ◽  
S. Safieddine ◽  
P. Kussel-Andermann ◽  
C. Petit ◽  
A. El-Amraoui

2012 ◽  
Vol 102 (12) ◽  
pp. 2715-2724 ◽  
Author(s):  
Christian Corbitt ◽  
Federica Farinelli ◽  
William E. Brownell ◽  
Brenda Farrell

2013 ◽  
Vol 104 (1) ◽  
pp. 8-18 ◽  
Author(s):  
Rei Kitani ◽  
Channy Park ◽  
Federico Kalinec

2003 ◽  
Vol 447 (3) ◽  
pp. 328-336 ◽  
Author(s):  
Tam�s J�zsef Batta ◽  
Gy�rgy Panyi ◽  
Rezso G�sp�r ◽  
Istv�n Sziklai

2010 ◽  
Vol 191 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Elisa Dultz ◽  
Jan Ellenberg

In metazoa, new nuclear pore complexes (NPCs) form at two different cell cycle stages: at the end of mitosis concomitant with the reformation of the nuclear envelope and during interphase. However, the mechanisms of these assembly processes may differ. In this study, we apply high resolution live cell microscopy to analyze the dynamics of single NPCs in living mammalian cells during interphase. We show that nuclear growth and NPC assembly are correlated and occur at a constant rate throughout interphase. By analyzing the kinetics of individual NPC assembly events, we demonstrate that they are initiated by slow accumulation of the membrane nucleoporin Pom121 followed by the more rapid association of the soluble NPC subcomplex Nup107–160. This inverse order of recruitment and the overall much slower kinetics compared with postmitotic NPC assembly support the conclusion that the two processes occur by distinct molecular mechanisms.


1995 ◽  
Vol 82 (1) ◽  
pp. 93-99 ◽  
Author(s):  
Koh Nakazawa ◽  
Samuel S. Spicer ◽  
Bradley A. Schulte

2020 ◽  
Vol 21 (19) ◽  
pp. 7099
Author(s):  
Verena Richter ◽  
Peter Lanzerstorfer ◽  
Julian Weghuber ◽  
Herbert Schneckenburger

Here, we present a simple and robust experimental setup for the super-resolution live cell microscopy of membrane-proximal fluorophores, which is comparably easy to perform and to implement. The method is based on Structured Illumination Microscopy (SIM) with a switchable spatial light modulator (SLM) and exchangeable objective lenses for epi-illumination and total internal reflection fluorescence (TIRF) microscopy. While, in the case of SIM (upon epi-illumination), cell layers of about 1–2 µm in close proximity to the plasma membrane can be selected by software, layers in the 100 nm range are assessed experimentally by TIRF-SIM. To show the applicability of this approach, both methods are used to measure the translocation of the glucose transporter 4 (GLUT4) from intracellular vesicles to the plasma membrane upon stimulation by insulin or insulin-mimetic compounds, with a lateral resolution of around 100 nm and an axial resolution of around 200 nm. While SIM is an appropriate method to visualize the intracellular localization of GLUT4 fused with a green fluorescent protein, TIRF-SIM permits the quantitative evaluation of its fluorescence in the plasma membrane. These imaging methods are discussed in the context of fluorescence lifetime kinetics, providing additional data for the molecular microenvironment.


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