Induction of the Adipose Differentiation-Related Protein in Liver of Etomoxir-Treated Rats

Steiner, Sandra; Wahl, Daniel R.; Mangold, B. L. K.; Robison, Rodney L.; Raymackers, Jos; Meheus, Lydie; Anderson, N. Leigh; André, Carl

doi:10.1006/bbrc.1996.0138

Cited by 65 publications

(40 citation statements)

References 5 publications

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“…6), oxidized low-density lipoprotein (LDL; see Ref. 49), and several pharmacological stimuli, including peroxisome proliferator-activated receptor (PPAR) ligands (2,6,8), cyclooxygenase inhibitors (53), etmoxir (46), and phorbol 12-myristate 13-acetate (PMA) (50). In a previous study, we elucidated, using a mouse RAW264.7 macrophage cell line, the molecular mechanisms of PMA-induced ADRP expression (50).…”

Section: Most Types Of Cells Store Lipid Droplets In Their Cytoplasmmentioning

confidence: 99%

Pycnogenol, an extract from French maritime pine, suppresses Toll-like receptor 4-mediated expression of adipose differentiation-related protein in macrophages

Ikuyama

Wei

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

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Adipose differentiation-related protein (ADRP) is highly expressed in macrophages and human atherosclerotic lesions. We demonstrated that Toll-like receptor (TLR) 4-mediated signals, which are involved in atherosclerosis formation, enhanced the expression of ADRP in macrophages. Lipopolysaccharide (LPS) enhanced the ADRP expression in RAW264.7 cells or peritoneal macrophages from wild-type mice, but not in macrophages from TLR4-deficient mice. Actinomycin D almost completely abolished the LPS effect, whereas cycloheximide decreased the expression at 12 h, indicating that the LPS-induced ADRP expression was stimulated at the transcriptional level and was also mediated by new protein synthesis. LPS enhanced the ADRP promoter activity, in part, by stimulating activator protein (AP)-1 binding to the Ets/AP-1 element. In addition, preceding the increase of the ADRP mRNA, LPS induced the expression of interleukin (IL)-6, IL-1α, and interferon-β mRNAs, all of which stimulated the ADRP expression. Antibodies against these cytokines or inhibitors of c-Jun NH2-terminal kinase and nuclear factor (NF)-κB suppressed the ADRP mRNA level. Thus TLR4 signals stimulate the ADRP expression both in direct and indirect manners. Pycnogenol (PYC), an extract of French maritime pine, suppressed the expression of ADRP and the above-mentioned cytokines. PYC suppressed the ADRP promoter activity and enhancer activity of AP-1 and NF-κB, whereas it did not affect the LPS-induced DNA binding of these factors. In conclusion, TLR4-mediated signals stimulate the ADRP expression in macrophages while PYC antagonizes this process. PYC, a widely used dietary supplement, might be useful for prevention of atherosclerosis.

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Section: Most Types Of Cells Store Lipid Droplets In Their Cytoplasmmentioning

confidence: 99%

Pycnogenol, an extract from French maritime pine, suppresses Toll-like receptor 4-mediated expression of adipose differentiation-related protein in macrophages

Ikuyama

Wei

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

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“…Subsequently, others speculated that TIP47 may also localize to lipid droplets (10,22). Cellular levels of ADPH have been shown to correlate with lipid accumulation in a variety of cells and tissues (23)(24)(25)(26)(27)(28)(29). This protein localizes to CLD in many mammalian cell types, including mammary epithelial cells, and is hypothesized to play a key role in CLD formation (16,17,30,31).…”

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confidence: 99%

Cytoplasmic lipid droplet accumulation in developing mammary epithelial cells: roles of adipophilin and lipid metabolism

Russell

Palmer

Orlicky

et al. 2007

Journal of Lipid Research

135

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PAT proteins (perilipin, adipophilin, and TIP47) are hypothesized to be critical regulators of lipid accumulation in eukaryotic cells. We investigated the developmental relationships between the expression of these proteins and cytoplasmic lipid droplet (CLD) accumulation in differentiating secretory epithelial cells in mouse mammary glands. Adipophilin (ADPH) specifically localized to CLD in differentiating and lactating mammary glands and was found exclusively in the secreted lipid droplet fraction of mouse milk. ADPH transcripts were selectively detected in secretory epithelial cells, and steady-state levels of both ADPH mRNA and protein increased during secretory differentiation in patterns consistent with functional linkage to CLD accumulation. TIP47 also was detected in secretory epithelial cells; however, it had a diffuse punctate appearance, and its mRNA and protein expression patterns did not correlate with CLD accumulation. Perilipin-positive adipose cells and steady-state levels of perilipin mRNA and protein decreased during mammary gland differentiation, suggesting a progressive loss of adipose lipid storage during this process.Collectively, these data demonstrate that increased ADPH expression is a specialized property of differentiated secretory epithelial cells and provide developmental evidence specifically linking increased ADPH expression to increased CLD accumulation. In addition, evidence is presented that the epithelial and adipose compartments of the mammary gland undergo concerted, developmentally regulated shifts in lipid metabolism that increase the availability of fatty acids necessary for lipid synthesis by milk-secreting cells.-

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“…In addition, it has been reported to be associated with milk fat globules in human milk (14). ADPH is hypothesized to play a key role in CLD formation: it localizes to CLDs in many mammalian cell types, including mammary epithelial cells (5,7,8,15,16), and cellular levels of ADPH have been shown to correlate with lipid accumulation in a variety of cells and tissues (17)(18)(19)(20)(21)(22)(23). We have shown that ADPH is selectively expressed by secretory epithelial cells in the mouse mammary gland and that its expression is developmentally linked to CLD accumulation during the differentiation of the mammary gland into a secretory organ during the last half of pregnancy (5).…”

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confidence: 99%

Mammary glands of adipophilin-null mice produce an amino-terminally truncated form of adipophilin that mediates milk lipid droplet formation and secretion

Russell

Palmer

Orlicky

et al. 2008

Journal of Lipid Research

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Adipophilin (ADPH), a member of the perilipin family of lipid droplet-associated proteins, is hypothesized to mediate milk lipid formation and secretion. Unexpectedly, the fat content of milk from ADPH-null mice was only modestly lower than that of wild-type controls, and neither TIP47 nor perilipin appeared to fully compensate for ADPH loss. This prompted us to investigate the possibility that the mutated ADPH gene was not a genuine null mutation. ADPH transcripts were detected in ADPH-null mammary tissue by quantitative real-time PCR, and C-terminal-specific, but not N-terminal-specific, ADPH antibodies detected a single lower molecular weight product and immunostained cytoplasmic lipid droplets (CLDs) and secreted milk fat globules in ADPH-null mammary tissue. Furthermore, stable cell lines expressing cDNA constructs corresponding to the ADPH-null mutation produced a product comparable in size to the one detected in ADPH-null mammary glands and localized to CLDs. Based on these data, we conclude that ADPH-null mice express an N-terminally truncated form of ADPH that retains the ability to promote the formation and secretion of milk lipids.-Russell, T.

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Induction of the Adipose Differentiation-Related Protein in Liver of Etomoxir-Treated Rats

Cited by 65 publications

References 5 publications

Pycnogenol, an extract from French maritime pine, suppresses Toll-like receptor 4-mediated expression of adipose differentiation-related protein in macrophages

Pycnogenol, an extract from French maritime pine, suppresses Toll-like receptor 4-mediated expression of adipose differentiation-related protein in macrophages

Cytoplasmic lipid droplet accumulation in developing mammary epithelial cells: roles of adipophilin and lipid metabolism

Mammary glands of adipophilin-null mice produce an amino-terminally truncated form of adipophilin that mediates milk lipid droplet formation and secretion

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