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1. chinaXiv:201605.01479 [pdf]

Identification of lipid droplet structure-like/resident proteins in Caenorhabditis elegans

Na, Huimin; Zhang, Peng; Chen, Yong; Zhu, Xiaotong; Liu, Yi; Liu, Yangli; Xie, Kang; Yang, Fuquan; Zhang, Hong; Liu, Pingsheng; Na, Huimin; Zhang, Peng; Zhu, Xiaotong; Liu, Yangli; Xie, Kang; Xu, Ningyi; Mak, Ho Yi; Xu, Ningyi; Mak, Ho Yi; Yu, Yong
Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology

The lipid droplet (LD) is a cellular organelle that stores neutral lipids in cells and has been linked with metabolic disorders. Caenorhabditis elegans has many characteristics which make it an excellent animal model for studying LDs. However, unlike in mammalian cells, no LD structure-like/resident proteins have been identified in C. elegans, which has limited the utility of this model for the study of lipid storage and metabolism. Herein based on three lines of evidence, we identified that MDT-28 and DHS-3 previously identified in C. elegans LD proteome were two LD structure-like/resident proteins. First, MDT-28 and DHS-3 were found to be the two most abundant LD proteins in the worm. Second, the proteins were specifically localized to LDs and we identified the domains responsible for this targeting in both proteins. Third and most importantly, the depletion of MDT-28 induced LD clustering while DHS-3 deletion reduced triacylglycerol content (TAG). We further characterized the proteins finding that MDT-28 was ubiquitously expressed in the intestine, muscle, hypodermis, and embryos, whereas DHS-3 was expressed mainly in intestinal cells. Together, these two LD structure-like/resident proteins provide a basis for future mechanistic studies into the dynamics and functions of LDs in C. elegans. (C) 2015 Elsevier B.V. All rights reserved.

submitted time 2016-05-12 Hits635Downloads281 Comment 0

2. chinaXiv:201605.01235 [pdf]

Lipid droplet remodeling and interaction with mitochondria in mouse brown adipose tissue during cold treatment

Yu, Jinhai; Zhang, Shuyan; Cui, Liujuan; Na, Huimin; Zhu, Xiaotong; Yang, Fuquan; Liu, Pingsheng; Yu, Jinhai; Na, Huimin; Zhu, Xiaotong; Wang, Weiyi; Xu, Guoheng; Li, Linghai; Christian, Mark; Cui, Liujuan
Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology

Brown adipose tissue (BAT) maintains animal body temperature by non-shivering thermogenesis, which is through uncoupling protein 1 (UCP1) that uncouples oxidative phosphorylation and utilizes beta-oxidation of fatty acids released from triacylglycerol (TAG) in lipid droplets (LDs). Increasing BAT activity and "browning" other tissues such as white adipose tissue (WAT) can enhance the expenditure of excess stored energy, and in turn reduce prevalence of metabolic diseases. Although many studies have characterized the biology of BAT and brown adipocytes, BAT LDs especially their activation induced by cold exposure remain to be explored. We have isolated LDs from mouse interscapular BAT and characterized the full proteome using mass spectrometry. Both morphological and biochemical experiments showed that the LDs could tightly associate with mitochondria. Under cold treatment mouse BAT started expressing LD structure protein PLIN-2/ADRP and increased expression of PLIN1 Both hormone sensitive lipase (HSL) and adipose TAG lipase (ATGL) were increased in LDs. In addition, isolated BAT LDs showed increased levels of the mitochondrial protein UCP1, and prolonged cold exposure could stimulate BAT mitochondrial cristae biogenesis. These changes were in agreement with the data from transcriptional analysis. Our results provide the BAT LD proteome for the first time and show that BAT LDs facilitate heat production by coupling increasing TAG hydrolysis through recruitment of ATGL and HSL to the organelle and expression of another LD resident protein PLIN2/ADRP, as well as by tightly associating with activated mitochondria. These findings will benefit the study of BAT activation and the interaction between LDs and mitochondria. (C) 2015 Elsevier B.V. All rights reserved.

submitted time 2016-05-11 Hits403Downloads244 Comment 0

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