Metabolic effects of tumour necrosis factor-α on rat brown adipose tissue

1995 ◽  
Vol 143 (2) ◽  
pp. 113-118 ◽  
Author(s):  
Joaquín López-Soriano ◽  
Josep M. Argilés ◽  
Francisco J. López-Soriano
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Metabolic Effects ◽  
Tumour Necrosis Factor Α ◽  
Brown Adipose ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Downregulation of zinc-α2-glycoprotein in adipose tissue and liver of obese ob/ob mice and by tumour necrosis factor-α in adipocytes

2009 ◽  
Vol 204 (2) ◽  
pp. 165-172 ◽  
Author(s):  
T Mracek ◽  
D Gao ◽  
T Tzanavari ◽  
Y Bao ◽  
X Xiao ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Protein Content ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Zucker Rats ◽  
Potential Candidate ◽  
Mrna Levels ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Zinc-α2-glycoprotein (ZAG, also listed as AZGP1 in the MGI Database), a lipid-mobilising factor, has recently been suggested as a potential candidate in the modulation of body weight. We investigated the effect of increased adiposity on ZAG expression in adipose tissue and the liver and on plasma levels in obese (ob/ob) mice compared with lean siblings. The study also examined the effect of the pro-inflammatory cytokine tumour necrosis factor-α (TNFα) on ZAG expression in adipocytes. Zag mRNA levels were significantly reduced in subcutaneous (fourfold) and epididymal (eightfold) fat of ob/ob mice. Consistently, ZAG protein content was decreased in both fat depots of ob/ob mice. In the liver of obese animals, steatosis was accompanied by the fall of both Zag mRNA (twofold) and ZAG protein content (2.5-fold). Plasma ZAG levels were also decreased in obese mice. In addition, Zag mRNA was reduced in epididymal (fivefold) and retroperitoneal (fivefold) adipose tissue of obese (fa/fa) Zucker rats. In contrast to Zag expression, Tnfα mRNA levels were elevated in adipose tissue (twofold) and the liver (2.5-fold) of ob/ob mice. Treatment with TNFα reduced Zag gene expression in differentiated adipocytes, and this inhibition was chronic, occurring at 24 and 48 h following TNFα treatment. It is concluded that ZAG synthesis in adipose tissue and the liver is downregulated, as are its circulating levels, in ob/ob mice. The reduced ZAG production may advance the susceptibility to lipid accumulation in these tissues in obesity, and this could be at least in part attributable to the inhibitory effect of TNFα.

scholarly journals Tumour necrosis factor-α (TNF-α) polymorphisms -857C/A and -863C/A are associated with TNF-α secretion from human adipose tissue

Diabetologia ◽  
2001 ◽  
Vol 44 (5) ◽  
pp. 654-655 ◽  
Author(s):  
T. Skoog ◽  
P. Eriksson ◽  
J. Hoffstedt ◽  
M. Rydén ◽  
A. Hamsten ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Human Adipose Tissue ◽  
Tumour Necrosis Factor Α ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Anti-Tumour Necrosis Factor-α Treatment Interferes with Changes in Lipid Metabolism in a Tumour Cachexia Model

1994 ◽  
Vol 87 (3) ◽  
pp. 349-355 ◽  
Author(s):  
Neus Carbó ◽  
Paola Costelli ◽  
Luciana Tessitore ◽  
Gregory J. Bagby ◽  
Francisco J. López-Soriano ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Tumour Necrosis Factor ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Lipoprotein Lipase Activity ◽  
Tumour Bearing ◽  
Factor Α ◽  
Necrosis Factor

1. Rats bearing the Yoshida ascites hepatoma AH-130 showed an important decrease in white adipose tissue lipoprotein lipase activity as compared with non-tumour bearing rats. This was associated with a lower adipose tissue mass, as estimated from the weight of the lumbar fat-pads. Conversely, lipoprotein lipase activity was markedly increased in brown adipose tissue and heart. 2. These changes were associated with a distinct hyperlipaemia, essentially manifested as an increase in circulating triacylglycerol levels, whereas no changes were observed in glycaemia. 3. Tumour-bearing rats were treated with a polyclonal anti-murine tumour necrosis factor-α antibody or with a non-immune IgG preparation. Control animals were either untreated or received a nonimmune IgG preparation. Anti-tumour necrosis factor-α treatment resulted in a significant increase in lipoprotein lipase activity in white adipose tissue in animals bearing a tumour growing exponentially (day 4 after inoculation) as compared with the animals receiving a non-immune goat IgG preparation. In addition, animals bearing an stationary tumour (day 7 after inoculation) and submitted to anti-tumour necrosis factor-α treatment had a higher adipose tissue lipoprotein lipase activity as compared with the IgG- or the non-treated groups. Correspondingly, circulating triacylglycerol levels were markedly decreased, with a lower hyperlipaemia than in control tumour-bearing rats. 4. These observations suggest that tumour necrosis factor-α is involved in activating the lipid metabolic changes that develop in rats after transplantation of a fast-growing tumour.

Metabolic Effects of Tumour Necrosis Factor-α (Cachectin) and Interleukin-1

1989 ◽  
Vol 77 (4) ◽  
pp. 357-364 ◽  
Author(s):  
Rhys D. Evans ◽  
Josep M. Argilés ◽  
Dermot H. Williamson
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Interleukin 1 ◽  
Metabolic Effects ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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