CIDE-A is expressed in liver of old mice and in type 2 diabetic mouse liver exhibiting steatosis

Kelder, Bruce; Boyce, Keith; Kriete, Andres; Clark, Ryan; Berryman, Darlene E.; Nagatomi, Sheila; List, Edward O.; Braughler, Mark; Kopchick, John J.

doi:10.1186/1476-5926-6-4

Cited by 25 publications

(26 citation statements)

References 42 publications

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“…No difference in FSP27 or CIDEA transcript level was detected for wild-type vs. ob/ob kidney, nor did we detect CIDEA in either wild-type or ob/ob adipose tissue (data not shown). The upregulation of CIDEA in ob/ob liver is in line with the finding by Kelder et al (22) of enhanced expression of CIDEA in the liver of aged or type 2 diabetic mice exhibiting steatosis. It has also been reported that CIDEA is markedly induced in liver via activation of PPAR␥ and PPAR␣ transcription factors, which interact with their cognate PPREs in the CIDEA 5Ј-flanking region (58).…”

Section: Fsp27 Transcript Level Is Under Tight Regulation By Insulin supporting

confidence: 78%

Assessment of fat-specific protein 27 in the adipocyte lineage suggests a dual role for FSP27 in adipocyte metabolism and cell death

Kim¹,

K²,

Zhou³

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

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Section: Fsp27 Transcript Level Is Under Tight Regulation By Insulin supporting

confidence: 78%

Assessment of fat-specific protein 27 in the adipocyte lineage suggests a dual role for FSP27 in adipocyte metabolism and cell death

Kim¹,

K²,

Zhou³

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

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“…Although FSP27 is generally expressed in adipocytes, high levels are also observed in steatotic livers (31,48; data not shown), suggesting a causative role in hepatic lipid accumulation. Cidea and adipophilin are also highly expressed in steatotic liver (4,34,40,50,51) where they as well as Cideb are involved in hepatic lipid accumulation (4, 49, 52); however, additional experiments are required to test a role for FSP27 in hepatic steatosis.…”

Section: Journal Of Biological Chemistry 14363mentioning

confidence: 99%

“…Other members of the CIDE family, Cidea and Cideb, influence metabolism and whole body lipid homeostasis (3)(4)(5)34). To investigate effects of FSP27 deficiency on metabolic variables in adipocytes, we measured basal and stimulated glucose uptake and lipolysis.…”

Section: Fsp27 Deficiency In 3t3-l1 Adipocytes Inhibits Formation Of mentioning

confidence: 99%

Fat-specific Protein 27 Regulates Storage of Triacylglycerol

Keller

Petrie

Rose

et al. 2008

Journal of Biological Chemistry

176

161

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FSP27 (fat-specific protein 27) is a member of the cell deathinducing DNA fragmentation factor-␣-like effector (CIDE) family. Although Cidea and Cideb were initially characterized as activators of apoptosis, recent studies have demonstrated important metabolic roles for these proteins. In this study, we investigated the function of another member of this family, FSP27 (Cidec), in apoptosis and adipocyte metabolism. Although overexpression of FSP27 is sufficient to increase apoptosis of 293T and 3T3-L1 cells, more physiological levels of expression stimulate spontaneous lipid accumulation in several cell types without induction of adipocyte genes. Increased triacylglycerol is likely due to decreased ␤-oxidation of nonesterified fatty acids. Altered flux of fatty acids into triacylglycerol may be a direct effect of FSP27 function, which is localized to lipid droplets in 293T cells and 3T3-L1 adipocytes. Stable knockdown of FSP27 during adipogenesis of 3T3-L1 cells substantially decreases lipid droplet size, increases mitochondrial and lipid droplet number, and modestly increases glucose uptake and lipolysis. Expression of FSP27 in subcutaneous adipose tissue of a human diabetes cohort decreases with total fat mass but is not associated with measures of insulin resistance (e.g. homeostasis model assessment). Together, these data indicate that FSP27 binds to lipid droplets and regulates their enlargement.The cell death-inducing DNA fragmentation factor-␣-like effector (CIDE) 5 family of proteins shares sequence similarity with DNA fragmentation factors and was initially characterized as mitochondrial activators of apoptosis (1, 2). However, strong metabolic phenotypes of mice lacking Cidea and Cideb indicate that this family plays critical roles in energy balance (3, 4). Cidea knock-out mice are lean and resistant to diet-induced obesity because of increased lipolysis and mitochondrial uncoupling in brown adipose tissue (3). Although expression of Cidea is limited to brown adipocytes in mice, humans express CIDE-A in white adipose tissue, where lower levels are observed with obesity and insulin resistance (5, 6). Although a coding variant of CIDE-A, V115F, is associated with human obesity (7), knockdown of CIDE-A in human adipocytes enhances lipolysis (5).Cideb knock-out mice are also lean and resistant to diet-induced obesity; however, this family member is expressed highly in liver, and the phenotype is because of decreased hepatic lipogenesis, increased fatty acid oxidation, and increased whole body energy expenditure (4). Thus, through a number of mechanisms, the CIDE family appears to have important roles in lipid metabolism. FSP27 (fat-specific protein of 27 kDa or Cidec) is the third member of the CIDE family. FSP27 was identified prior to the other family members based upon induction during adipogenesis (8). CIDE-3, the human version of FSP27, was characterized as 66% homologous to mouse and as an activator of apoptosis when expressed in 293T cells (9). However, the lack of function ascribed to FSP27 limit...

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“…Expression of NF-kB with age is consistent with elevated levels of inflammatory markers and a proinflammatory phenotype. Cytokines and chemokine profiles, likely activated by NF-kB, have been observed in gene expression studies of both human and animal tissues including brain [67], lung [5], liver [54], cartilage [53], and coronary arteries [25]. In fact, a review of gene expressions of nine tissue types in mice and humans revealed that the occurrence of the NF-kB motif was most ubiquitous and strongly associated with age [2].…”

Section: Nf-kb Feedback and Inflammationmentioning

confidence: 95%

Systems Biology of Aging: Opportunities for Parkinson’s Disease

Kriete

2012

Systems Biology of Parkinson's Disease

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Parkinson's disease (PD), like many other dementias, is a disease of old age with neurological-pathological signs and underlying molecular mechanisms that precede cell death. Deciphering PD specifically from an aging perspective has many advantages. PD shares multiple mechanisms with aging, albeit in an accelerated fashion, including accumulation of damage and dysfunction, stress responses, and deficiencies in the maintenance of protein quality. Here, we review the foundations of a new hybrid, phenotypical model, which combines organelle phenotypes with molecular mechanisms associated with the long-term progression of normal aging. Subsequently, we adapt this model to PD and demonstrate the acceleration of dysfunction. On the level of molecular mechanisms, we specifically discuss two pathways that play a key role in the progression of both aging and PD: NF-kB and mTOR. The introduction of comprehensive modeling approaches is expected to make a significant contribution in deciphering the relationship between the different processes and risks factors. In particular, the tight relationship of aging and PD as discussed here sheds new light on future strategies for interventions.

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CIDE-A is expressed in liver of old mice and in type 2 diabetic mouse liver exhibiting steatosis

Cited by 25 publications

References 42 publications

Assessment of fat-specific protein 27 in the adipocyte lineage suggests a dual role for FSP27 in adipocyte metabolism and cell death

Assessment of fat-specific protein 27 in the adipocyte lineage suggests a dual role for FSP27 in adipocyte metabolism and cell death

Fat-specific Protein 27 Regulates Storage of Triacylglycerol

Systems Biology of Aging: Opportunities for Parkinson’s Disease

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