Cell death–inducing DFF45-like effector C is reduced by caloric restriction and regulates adipocyte lipid metabolism

Magnusson, Björn; Gummesson, Anders; Glad, Camilla A M; Goedecke, Julia H.; Jernås, Margareta; Lystig, Theodore C.; Carlsson, Björn; Fagerberg, Björn; Carlsson, Lena; Svensson, Per‐Arne

doi:10.1016/j.metabol.2008.04.028

Cited by 48 publications

(46 citation statements)

References 25 publications

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“…The reduced calorific intake was correlated with a decrease in CIDEC mRNA in subcutaneous adipose tissue. 16) This study also showed a positive correlation between PPARg and CIDEC expression in adipose tissue. A strong negative correlation between the expression levels of human CIDEA/CIDEC/perilipin and an index of insulin resistance (HOMA) was also demonstrated in obese patients matched for BMI.…”

Section: Obesity and Cidecsupporting

confidence: 59%

“…12) Similar to FSP27, human CIDEC was predominantly expressed in subcutaneous adipose tissue from obese subjects. [16][17][18] CIDEC was also observed at a lower level in heart, lung, skeletal muscle, small intestine, and colon as a distinct expression with FSP27. 9) Further, CIDEC mRNA was also observed in several cancer cell lines, e.g., hepatocellular carcinoma cell line HepG2, malignant melanoma cell line A375, and tongue squamous cell carcinoma cell line Tca8113.…”

Section: Tissue-specific Expression Of Fsp27/cidecmentioning

confidence: 95%

“…The CIDE-N domain of CIDEA, CIDEB and FSP27 shows homology with DFF45 as 39%, 29% and 38% amino acid identity, respectively. Furthermore, the CIDE-C domain of CIDEA and CIDEB share amino acid homology (54% and BAT 12,20) Higher metabolic rate and body temperature 20) CIDEB Mouse 24.8 Mitochondria, 11) LD, ER 21) Liver, kidney, colon 10,12) TG accumulation in liver, impaired VLDL release 21) FSP27 Mouse 27.3 LD 15) WAT, BAT, [12][13][14] fatty liver 12) Small WAT, improved obesity 13,14) CIDEC Human 26.7 N.D. WAT, colon, heart, small intestine 9,16) LD, lipid droplets; ER, endoplasmic reticulum; BAT, brown adipose; WAT, white adipose, N.D., not determined.…”

Section: Isolation Of Fsp27/cidecmentioning

confidence: 99%

“…12,23) The mechanism for transcriptional regulation of human CIDEC remains unclear. Since the CIDEC is expressed in adipocytes in a similar pattern to FSP27, 16) it is likely that PPARg could also directly regulate the expression of CIDEC.…”

Section: Transcriptional Regulation Of Fsp27/ Cidecmentioning

confidence: 99%

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A Physiological Role for Fat Specific Protein 27/Cell Death-Inducing DFF45-Like Effector C in Adipose and Liver

Matsusue

2010

Biological & Pharmaceutical Bulletin

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Fat specific protein 27 (FSP27) was originally isolated by screen for genes specifically expressed in fully differentiated mouse adipocytes. FSP27 and cell death-inducing DFF45-like effector C (CIDEC), the human homologue of FSP27, belong to the CIDE family. The FSP27 in adipocytes was recently reported to be a lipid droplet (LD)-associated protein, that promotes the formation of unilocular LDs. An FSP27 knockout mouse demonstrated lean phenotypes with atrophic adipose tissue as a result of high-energy expenditure; this mouse line was also resistant to diet-induced obesity and insulin resistance. Interestingly, FSP27 was also expressed in the steatoic liver of a type II diabetes model mouse. The expression of FSP27 was markedly decreased in livers lacking the nuclear receptor peroxisome proliferator-activated receptor g g. Forced expression of FSP27 in hepatocytes in vitro or in vivo led to an increase of LD through increased triglyceride levels. The current status of the physiological roles of FSP27/CIDEC in adipose tissue and liver are discussed along with its significance as a factor involved in the development of metabolic disorders.

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Section: Obesity and Cidecsupporting

confidence: 59%

Section: Tissue-specific Expression Of Fsp27/cidecmentioning

confidence: 95%

Section: Isolation Of Fsp27/cidecmentioning

confidence: 99%

Section: Transcriptional Regulation Of Fsp27/ Cidecmentioning

confidence: 99%

See 2 more Smart Citations

A Physiological Role for Fat Specific Protein 27/Cell Death-Inducing DFF45-Like Effector C in Adipose and Liver

Matsusue

2010

Biological & Pharmaceutical Bulletin

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“…はいずれも retinoid X receptor (RXR）とヘテロダ 14) BAT, 11,12) mammary gland 14) higher metabolic rate and body temperature, 12) secretion of milk lipids 14) CIDEB mouse 24.8 mitochondria, 15) LD, ER 16) liver, kidney, colon, 11,17) pancreas 18) impaired VLDL release 16) fsp27 mouse 27.3 LD, 19) nucleus 14) WAT, BAT, 11,20,21) fatty liver 11) small WAT, improved obesity 20,21) CIDEC human 26.7 N.D. WAT, colon, heart small intestine, 22,23) fatty liver 24) LD, lipid droplets; ER, endoplasmic reticulum; BAT, brown adipose; WAT, white adipose, N.D., not determine. Induction of hepatic PPARg appears to be a trigger for the activation of PPARg-fsp27 signal.…”

mentioning

confidence: 99%

A Novel Mechanism for Hepatic Lipid Accumulation: A Physiological Role for Hepatic PPARγ-fsp27 Signal

公彦

2012

YAKUGAKU ZASSHI

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Fat-speciˆc protein 27 (fsp27) was originally isolated by screening for genes speciˆcally expressed in fully diŠeren-tiated mouse adipocytes. Fsp27 and cell death-inducing DFF45-like eŠector (CIDE) C, the human homologue of fsp27, belong to the CIDE family. Fsp27, which is highly expressed in mouse white and brown adipose tissues, was recently reported to be a lipid droplet (LD)-binding protein that promotes lipid accumulation in adipocytes. In contrast, we showed that fsp27 was also expressed in the fatty liver of the ob/ob type II diabetes model mouse. The expression of fsp27 was markedly decreased in livers lacking the nuclear receptor peroxisome proliferator-activated receptor g (PPARg). A functional PPAR response element site was identiˆed in the fsp27 promoter region. Forced expression of fsp27 in hepatocytes in vitro or in vivo led to increased LD through increased triglyceride levels. The current status of the physiological roles of the PPARg-fsp27 signal in fatty liver are discussed along with its signiˆcance as a factor involved in the development of metabolic disorders.

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Partial lipodystrophy and insulin resistant diabetes in a patient with a homozygous nonsense mutation in CIDEC

et al. 2009

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Lipodystrophic syndromes are characterized by adipose tissue deficiency. Although rare, they are of considerable interest as they, like obesity, typically lead to ectopic lipid accumulation, dyslipidaemia and insulin resistant diabetes. In this paper we describe a female patient with partial lipodystrophy (affecting limb, femorogluteal and subcutaneous abdominal fat), white adipocytes with multiloculated lipid droplets and insulin-resistant diabetes, who was found to be homozygous for a premature truncation mutation in the lipid droplet protein cell death-inducing Dffa-like effector C (CIDEC) (E186X). The truncation disrupts the highly conserved CIDE-C domain and the mutant protein is mistargeted and fails to increase the lipid droplet size in transfected cells. In mice, Cidec deficiency also reduces fat mass and induces the formation of white adipocytes with multilocular lipid droplets, but in contrast to our patient, Cidec null mice are protected against diet-induced obesity and insulin resistance. In addition to describing a novel autosomal recessive form of familial partial lipodystrophy, these observations also suggest that CIDEC is required for unilocular lipid droplet formation and optimal energy storage in human fat.

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Cell death–inducing DFF45-like effector C is reduced by caloric restriction and regulates adipocyte lipid metabolism

Cited by 48 publications

References 25 publications

A Physiological Role for Fat Specific Protein 27/Cell Death-Inducing DFF45-Like Effector C in Adipose and Liver

A Physiological Role for Fat Specific Protein 27/Cell Death-Inducing DFF45-Like Effector C in Adipose and Liver

A Novel Mechanism for Hepatic Lipid Accumulation: A Physiological Role for Hepatic PPARγ-fsp27 Signal

Partial lipodystrophy and insulin resistant diabetes in a patient with a homozygous nonsense mutation in CIDEC

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