Effects of 1,25(OH) 2 D 3 on lipid droplet growth in adipocytes

BioFactors ◽  
2020 ◽  
Vol 46 (6) ◽  
pp. 943-954
Author(s):  
Wei Xiang ◽  
Shi Cheng ◽  
Yong Zhou ◽  
Ling Ma
Keyword(s):  
2013 ◽  
Vol 24 (4) ◽  
pp. 335-336 ◽  
Author(s):  
William A. Prinz
Keyword(s):  

2015 ◽  
Vol 17 (1) ◽  
pp. 3-3
Author(s):  
Paulina Strzyz

2015 ◽  
Vol 40 (7) ◽  
pp. 641-651 ◽  
Author(s):  
Rebecca E.K. MacPherson ◽  
Sandra J. Peters

The regulation of skeletal muscle lipolysis and fat oxidation is a complex process involving multiple proteins and enzymes. Emerging work indicates that skeletal muscle PLIN proteins likely play a role in the hydrolysis of triglycerides stored in lipid droplets and the passage of fatty acids to the mitochondria for oxidation. In adipocytes, PLIN1 regulates lipolysis by interacting with comparative gene identification-58 (CGI-58), an activator of adipose triglyceride lipase (ATGL). Upon lipolytic stimulation, PLIN1 is phosphorylated, releasing CGI-58 to activate ATGL and initiate triglyceride breakdown. The absence of PLIN1 in skeletal muscle leads us to believe that other PLIN family members undertake this role. The focus of this review is on the PLIN family proteins expressed in skeletal muscle: PLIN2, PLIN3, and PLIN5. To date, most studies involving these PLIN proteins have used nonmuscle tissues and cell cultures to determine their potential roles. Results from work in these models support a role for PLIN proteins in sequestering lipases during basal conditions and in potentially working together for lipase translocation and activity during lipolysis. In skeletal muscle, PLIN2 tends to mirror the lipid content and may play a role in lipid droplet growth and stability through lipase interactions on the lipid droplet surface, whereas the skeletal muscle roles of both PLIN3 and PLIN5 seem to be more complex because they are found not only on the lipid droplet, but also at the mitochondria. Clearly, further work is needed to fully understand the intricate mechanisms by which PLIN proteins contribute to skeletal muscle lipid metabolism.


2011 ◽  
Vol 195 (6) ◽  
pp. 953-963 ◽  
Author(s):  
Jingyi Gong ◽  
Zhiqi Sun ◽  
Lizhen Wu ◽  
Wenyi Xu ◽  
Nicole Schieber ◽  
...  

Lipid droplets (LDs) are dynamic cellular organelles that control many biological processes. However, molecular components determining LD growth are poorly understood. Genetic analysis has indicated that Fsp27, an LD-associated protein, is important in controlling LD size and lipid storage in adipocytes. In this paper, we demonstrate that Fsp27 is focally enriched at the LD–LD contacting site (LDCS). Photobleaching revealed the occurrence of lipid exchange between contacted LDs in wild-type adipocytes and Fsp27-overexpressing cells but not Fsp27-deficient adipocytes. Furthermore, live-cell imaging revealed a unique Fsp27-mediated LD growth process involving a directional net lipid transfer from the smaller to larger LDs at LDCSs, which is in accordance with the biophysical analysis of the internal pressure difference between the contacting LD pair. Thus, we have uncovered a novel molecular mechanism of LD growth mediated by Fsp27.


Cell Reports ◽  
2021 ◽  
Vol 36 (4) ◽  
pp. 109451
Author(s):  
Syed S. Hussain ◽  
Tuyet-Minh Tran ◽  
Timothy B. Ware ◽  
Melissa A. Luse ◽  
Christopher T. Prevost ◽  
...  
Keyword(s):  

2013 ◽  
Vol 24 (4) ◽  
pp. 384-399 ◽  
Author(s):  
Florian Wilfling ◽  
Huajin Wang ◽  
Joel T. Haas ◽  
Natalie Krahmer ◽  
Travis J. Gould ◽  
...  

2016 ◽  
Vol 345 (1) ◽  
pp. 100-107 ◽  
Author(s):  
Kristina Eisinger ◽  
Lisa Rein-Fischboeck ◽  
Rebekka Pohl ◽  
Elisabeth M. Meier ◽  
Sabrina Krautbauer ◽  
...  

2017 ◽  
Vol 47 ◽  
pp. 9-15 ◽  
Author(s):  
David Barneda ◽  
Mark Christian

2020 ◽  
Author(s):  
Syed Hussain ◽  
Tuyet-Minh Tran ◽  
Timothy B. Ware ◽  
Melissa A. Luse ◽  
Christopher T. Prevost ◽  
...  
Keyword(s):  

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