scholarly journals Lipid Droplet Associated Proteins and Control of Triacylglycerol Metabolism

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Dawn L Brasaemle ◽  
Gabriela Montero‐Moran ◽  
Derek McMahon ◽  
Jorge M Caviglia ◽  
Xiaofang Liang ◽  
...  
2008 ◽  
Vol 154 ◽  
pp. S4
Author(s):  
Dawn L. Brasaemle ◽  
Gabriela Montero-Moran ◽  
J. Matias Caviglia ◽  
Derek McMahon ◽  
Xiaofang Liang ◽  
...  

2018 ◽  
Vol 56 (01) ◽  
pp. E2-E89
Author(s):  
H Witzel ◽  
L Pawella ◽  
V Rausch ◽  
S Mueller ◽  
J Schattenberg ◽  
...  

2022 ◽  
Vol 8 ◽  
Author(s):  
Hai-bo Zhang ◽  
Wen Su ◽  
Hu Xu ◽  
Xiao-yan Zhang ◽  
You-fei Guan

Nonalcoholic fatty liver disease (NAFLD), especially in its inflammatory form (steatohepatitis, NASH), is closely related to the pathogenesis of chronic liver disease. Despite substantial advances in the management of NAFLD/NASH in recent years, there are currently no efficacious therapies for its treatment. The biogenesis and expansion of lipid droplets (LDs) are critical pathophysiological processes in the development of NAFLD/NASH. In the past decade, increasing evidence has demonstrated that lipid droplet-associated proteins may represent potential therapeutic targets for the treatment of NAFLD/NASH given the critical role they play in regulating the biogenesis and metabolism of lipid droplets. Recently, HSD17B13, a newly identified liver-enriched, hepatocyte-specific, lipid droplet-associated protein, has been reported to be strongly associated with the development and progression of NAFLD/NASH in both mice and humans. Notably, human genetic studies have repeatedly reported a robust association of HSD17B13 single nucleotide polymorphisms (SNPs) with the occurrence and severity of NAFLD/NASH and other chronic liver diseases (CLDs). Here we briefly overview the discovery, tissue distribution, and subcellular localization of HSD17B13 and highlight its important role in promoting the pathogenesis of NAFLD/NASH in both experimental animal models and patients. We also discuss the potential of HSD17B13 as a promising target for the development of novel therapeutic agents for NAFLD/NASH.


1993 ◽  
Vol 90 (24) ◽  
pp. 12035-12039 ◽  
Author(s):  
A. S. Greenberg ◽  
J. J. Egan ◽  
S. A. Wek ◽  
M. C. Moos ◽  
C. Londos ◽  
...  

1995 ◽  
Vol 15 (7) ◽  
pp. 3470-3478 ◽  
Author(s):  
R Hopewell ◽  
E B Ziff

Heterodimerization of Max with the nuclear oncoprotein Myc and the differentiation-associated proteins Mad and Mxi1 enables these factors to bind E-box sites in DNA and control genes implicated in cell proliferation and differentiation. We show that in the PC12 pheochromocytoma tumor cell line, functional Max protein is not expressed because of the synthesis of a mutant max transcript. This transcript encodes a protein incapable of homo- or heterodimerization. Furthermore, the mutant Max protein, unlike wild-type Max, is incapable of repressing transcription from an E-box element. Synthesis of mutant max transcripts appears to be due to a homozygous chromosomal alteration within the max gene. Reintroduction of max into PC12 cells results in repression of E-box-dependent transcription and a reduction in growth rate, which may explain the loss of Max expression either during the growth of the pheochromocytoma or in subsequent passage of the PC12 cell line in vitro. Finally, the ability of these cells to divide, differentiate, and apoptose in the absence of Max demonstrates for the first time that these processes can occur via Max- and possibly Myc-independent mechanisms.


2005 ◽  
Vol 46 (5) ◽  
pp. 885-895 ◽  
Author(s):  
Soonkyu Chung ◽  
Jonathan Mark Brown ◽  
Maria Boysen Sandberg ◽  
Michael McIntosh

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