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The Direct Peroxisome Proliferator-activated Receptor Target Fasting-induced Adipose Factor (FIAF/PGAR/ANGPTL4) Is Present in Blood Plasma as a Truncated Protein That Is Increased by Fenofibrate Treatment

Mandard, Stéphane, Zandbergen, Fokko, Tan, Nguan Soon, Escher, Pascal, Patsouris, David, Koenig, Wolfgang, Kleemann, Robert, Bakker, Arjen, Veenman, Frank, Wahli, Walter, Müller, Michael, Kersten, Sander·2004·Journal of Biological Chemistry
DOI 10.1074/jbc.m403058200
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FIG. 2 FIAF is a probable PPAR 𝛄 target in human adipocytes. Stromal vascular cells were isolated from subcutaneous ( solid line ) and visceral ( dotted line ) adipose tissue from three subjects and put into culture. Cells were differentiated into adipocytes by incubation with adipogenic medium. Expression is expressed relative to glyceraldehyde-3-phosphate dehydrogenase. Human SGBS differentiated adipocytes (day 13) were treated for 40 h with different concentrations of rosiglitazone ( B ) or L165041 ( C ). Concentrations are indicated in 𝛍 M. FIAF gene expression was determined by quantitative RT-PCR.
FIG. 2 FIAF is a probable PPAR 𝛄 target in human adipocytes. Stromal vascular cells were isolated from subcutaneous ( solid line ) and visceral ( dotted line ) adipose tissue from three subjects and put into culture. Cells were differentiated into adipocytes by incubation with adipogenic medium. Expression is expressed relative to glyceraldehyde-3-phosphate dehydrogenase. Human SGBS differentiated adipocytes (day 13) were treated for 40 h with different concentrations of rosiglitazone ( B ) or L165041 ( C ). Concentrations are indicated in 𝛍 M. FIAF gene expression was determined by quantitative RT-PCR.CC-BY · From the PDF
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FIG. 3 FIAF up-regulation by PPAR 𝛂 is mediated by a PPRE present in intron 3. A , alignment of the PPRE present in intron 3 of the human and mouse FIAF gene with known PPREs. Cons ., consensus. B , binding of the PPAR/RXR heterodimer to putative PPRE as determined by gel shift. A double-stranded response element containing the human ( left ) or mouse ( right ) FIAF PPRE was incubated with in vitro transcribed/translated hPPAR 𝛂 and hRXR 𝛂 , and binding complexes were resolved on a 6% nondenaturing polyacrylamide gel. -Fold excess of specific (malic enzyme PPRE) or nonspecific (ETS oligonucleotide) cold probe is indicated. C , HepG2 cells were transfected with a SEAP reporter vector containing a 350-nucleotide fragment of intron 3 of the human ( left ) or mouse ( right ) FIAF gene and a PPAR expression vector. SEAP activity was determined in the medium 24-48 h post-transfection.
FIG. 3 FIAF up-regulation by PPAR 𝛂 is mediated by a PPRE present in intron 3. A , alignment of the PPRE present in intron 3 of the human and mouse FIAF gene with known PPREs. Cons ., consensus. B , binding of the PPAR/RXR heterodimer to putative PPRE as determined by gel shift. A double-stranded response element containing the human ( left ) or mouse ( right ) FIAF PPRE was incubated with in vitro transcribed/translated hPPAR 𝛂 and hRXR 𝛂 , and binding complexes were resolved on a 6% nondenaturing polyacrylamide gel. -Fold excess of specific (malic enzyme PPRE) or nonspecific (ETS oligonucleotide) cold probe is indicated. C , HepG2 cells were transfected with a SEAP reporter vector containing a 350-nucleotide fragment of intron 3 of the human ( left ) or mouse ( right ) FIAF gene and a PPAR expression vector. SEAP activity was determined in the medium 24-48 h post-transfection.CC-BY · From the PDF
FIG. 4 PPAR 𝛂 and PPAR 𝛄 bind to the PPRE within intron 3 of the FIAF gene in vivo . Chromatin immunoprecipitation of PPRE within intron 3 of the FIAF gene using antibodies against PPAR 𝛂 or PPAR 𝛄 . The gene sequence spanning the putative PPRE and a random control sequence were analyzed by PCR in the immunoprecipitated chromatin of HepG2 cells treated with Wy14643 ( A ), livers of wild-type and PPAR 𝛂 null mice treated or not with WY14643 ( B ), livers of fed or fasted wild-type and PPAR 𝛂 null mice ( C ), or 3T3-L1 preadipocytes and adipocytes ( D ). Preimmune serum was used as a control. PI , preimmune serum; Cntl , random control sequence; Veh , vehicle; WT , wild type; KO , knock-out.
FIG. 4 PPAR 𝛂 and PPAR 𝛄 bind to the PPRE within intron 3 of the FIAF gene in vivo . Chromatin immunoprecipitation of PPRE within intron 3 of the FIAF gene using antibodies against PPAR 𝛂 or PPAR 𝛄 . The gene sequence spanning the putative PPRE and a random control sequence were analyzed by PCR in the immunoprecipitated chromatin of HepG2 cells treated with Wy14643 ( A ), livers of wild-type and PPAR 𝛂 null mice treated or not with WY14643 ( B ), livers of fed or fasted wild-type and PPAR 𝛂 null mice ( C ), or 3T3-L1 preadipocytes and adipocytes ( D ). Preimmune serum was used as a control. PI , preimmune serum; Cntl , random control sequence; Veh , vehicle; WT , wild type; KO , knock-out.CC-BY · From the PDF
Image 9
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FIG. 6 The truncated form of FIAF is up-regulated in concert with FIAF mRNA by synthetic RXR/PPAR agonists. mFIAF protein (30 𝛍 g of total protein loaded per lane) and mRNA expression in differentiated 3T3-L1 adipocytes (day 10) after treatment for 48 h with 5 𝛍 M Lg100268 ( A ) or rosiglitazone ( B ) as assessed by Western blot and quantitative RT-PCR are shown. C , mFIAF protein (12 𝛍 g of total protein loaded per lane) and mRNA in liver of mice fed WY14643 (0.1%) for 5 days. D , Western blot of mouse plasma using anti-mFIAF antibody in the absence or presence of the peptide epitope. E , presence of truncated mFIAF variants in mouse white adipose tissue, blood plasma, and mouse liver. The position of native mFIAF is shown by transfection of pcDNA3 expressing mFIAF into HEK293 cells. Medium was collected, precipitated using trichloroacetic acid, and prepared for SDS-PAGE.
FIG. 6 The truncated form of FIAF is up-regulated in concert with FIAF mRNA by synthetic RXR/PPAR agonists. mFIAF protein (30 𝛍 g of total protein loaded per lane) and mRNA expression in differentiated 3T3-L1 adipocytes (day 10) after treatment for 48 h with 5 𝛍 M Lg100268 ( A ) or rosiglitazone ( B ) as assessed by Western blot and quantitative RT-PCR are shown. C , mFIAF protein (12 𝛍 g of total protein loaded per lane) and mRNA in liver of mice fed WY14643 (0.1%) for 5 days. D , Western blot of mouse plasma using anti-mFIAF antibody in the absence or presence of the peptide epitope. E , presence of truncated mFIAF variants in mouse white adipose tissue, blood plasma, and mouse liver. The position of native mFIAF is shown by transfection of pcDNA3 expressing mFIAF into HEK293 cells. Medium was collected, precipitated using trichloroacetic acid, and prepared for SDS-PAGE.CC-BY · From the PDF
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Metadata

Authors
Mandard, S., Zandbergen, F., Tan, N. S., Escher, P., Patsouris, D., Koenig, W., Kleemann, R., Bakker, A., Veenman, F., Wahli, W., Müller, M., & Kersten, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-08
Volume
279
Issue
33
Pages
34411-34420
ISSN
0021-9258
DOI
10.1074/jbc.m403058200
Cited by
231
References
2
Language
en
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