Proteomic analysis of adipocyte differentiation: Evidence that α2 macroglobulin is involved in the adipose conversion of 3T3 L1 preadipocytes

PROTEOMICS ◽  
2004 ◽  
Vol 4 (6) ◽  
pp. 1840-1848 ◽  
Author(s):  
Kai-Luk Choi ◽  
Yu Wang ◽  
Cynthia A. Tse ◽  
Karen S. L. Lam ◽  
Garth J. S. Cooper ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Adipocyte Differentiation ◽  
Α2 Macroglobulin ◽  
Adipose Conversion

Proteomic analysis for inhibitory effect of chitosan oligosaccharides on 3T3-L1 adipocyte differentiation

PROTEOMICS ◽  
2008 ◽  
Vol 8 (3) ◽  
pp. 569-581 ◽  
Author(s):  
Md. Atiar Rahman ◽  
Suresh G. Kumar ◽  
Sang Woo Kim ◽  
Hye Jin Hwang ◽  
Yu Mi Baek ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Adipocyte Differentiation ◽  
Inhibitory Effect ◽  
Chitosan Oligosaccharides

Amine oxidase substrates mimic several of the insulin effects on adipocyte differentiation in 3T3 F442A cells

2001 ◽  
Vol 356 (3) ◽  
pp. 769-777 ◽  
Author(s):  
Emi FONTANA ◽  
Jérémie BOUCHER ◽  
Luc MARTI ◽  
José Miguel LIZCANO ◽  
Xavier TESTAR ◽  
...  
Keyword(s):  
Glucose Transport ◽  
Glucose Transporter ◽  
Adipocyte Differentiation ◽  
Amine Oxidase ◽  
Chronic Administration ◽  
Mao Inhibitor ◽  
Amine Oxidation ◽  
Adipose Conversion ◽  
Triacylglycerol Accumulation ◽  
Stimulation Of

We have previously reported that substrates of monoamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) exert short-term insulin-like effects in rat adipocytes, such as stimulation of glucose transport. In the present work, we studied whether these substrates could also mimic long-term actions of insulin. Adipose differentiation of 3T3 F442A cells, which is highly insulin-dependent, served as a model to test the effects of sustained administration of amine oxidase substrates. Daily treatment of confluent cells with 0.75mM tyramine (a substrate of MAO and SSAO) or benzylamine (a substrate of SSAO) over 1 week caused the acquisition of typical adipocyte morphology. The stimulation of protein synthesis and triacylglycerol accumulation caused by tyramine or benzylamine reached one half of that promoted by insulin. This effect was insensitive to pargyline (an MAO inhibitor), but was inhibited by semicarbazide (an SSAO inhibitor) and by N-acetylcysteine (an antioxidant agent), suggesting the involvement of the H2O2 generated during SSAO-dependent amine oxidation. Chronic administration of amine oxidase substrates also induced the emergence of adipose conversion markers, such as aP2, glycerol-3-phosphate dehydrogenase, the glucose transporter GLUT4, and SSAO itself. Moreover, cells treated with amines acquired the same insulin sensitivity regarding glucose transport as adipocytes classically differentiated with insulin. In all, most of the adipogenic effects of amines were additive to insulin. Our data reveal that amine oxidase substrates partially mimic the adipogenic effect of insulin in cultured preadipocytes. Furthermore, they suggest that SSAO not only represents a novel late marker of adipogenesis, but could also be directly involved in the triggering of terminal adipocyte differentiation.

Semicarbazide-sensitive amine oxidase activation promotes adipose conversion of 3T3-L1 cells

2001 ◽  
Vol 358 (2) ◽  
pp. 335-342 ◽  
Author(s):  
Nathalie MERCIER ◽  
Marthe MOLDES ◽  
Khadija EL HADRI ◽  
Bruno FÈVE
Keyword(s):  
Potential Role ◽  
Adipocyte Differentiation ◽  
Amine Oxidase ◽  
Monoamine Oxidase Inhibitor ◽  
Oxidase Inhibitor ◽  
Dependent Manner ◽  
Adipose Conversion ◽  
Adipose Tissue Development ◽  
Dose Dependent

Semicarbazide-sensitive amine oxidase (SSAO) is an amine oxidase related to the copper-containing amine oxidase family. The tissular form of SSAO is located at the plasma membrane, and is mainly expressed in vascular smooth muscle cells and adipocytes. Recent studies have suggested that SSAO could activate glucose transport in fat cells. In the present work, we investigated the potential role of a chronic SSAO activation on adipocyte maturation of the 3T3-L1 pre-adipose cell line. Exposure of post-confluent 3T3-L1 pre-adipocytes to methylamine, a physiological substrate of SSAO, promoted adipocyte differentiation in a time- and dose-dependent manner. This effect could be related to SSAO activation, since it was antagonized in the presence of the SSAO inhibitor semicarbazide, but not in the presence of the monoamine oxidase inhibitor pargyline. In addition, methylamine-induced adipocyte maturation was mimicked by 3T3-L1 cell treatment with other SSAO substrates. Finally, the large reversion of methylamine action by catalase indicated that hydrogen peroxide generated by SSAO was involved, at least in part, in the modulation of adipocyte maturation. Taken together, our results suggest that SSAO may contribute to the control of adipose tissue development.

scholarly journals C/EBPalpha regulation of the growth-arrest-associated gene gadd45.

1996 ◽  
Vol 16 (7) ◽  
pp. 3878-3883 ◽  
Author(s):  
C M Constance ◽  
J I Morgan ◽  
R M Umek
Keyword(s):  
Dna Damage ◽  
Adipocyte Differentiation ◽  
Growth Arrest ◽  
Dominant Negative ◽  
Developmental Expression ◽  
Tumor Suppressor P53 ◽  
Enhancer Binding Protein ◽  
Adipose Conversion ◽  
Adipocyte Development ◽  
Inducible Gene

CCAAT/enhancer-binding protein alpha (C/EBPalpha) is expressed in postmitotic, differentiated adipocytes and is required for adipose conversion of 3T3-L1 cells in culture. Temporal misexpression of C/EBPalpha in undifferentiated adipoblasts leads to mitotic growth arrest. We report here that growth arrest- and DNA damage-inducible gene 45 (gadd45) is preferentially expressed in differentiated 3T3-L1 adipocytes similar to phenotype-associated genes. Furthermore, C/EBPalpha transactivates a reporter plasmid containing 1.5 kb of the gadd45 promoter region. The proto-oncogene myc, which inhibits adipocyte differentiation, abrogates C/EBPalpha activation of gadd45. gadd45 is known to be a target of the tumor suppressor p53 in a G1 checkpoint activated by DNA damage. Immunoprecipitation of radiolabeled proteins with conformation-specific antibodies revealed that wild-type p53 is expressed throughout 3T3-L1 adipocyte development, including the postmitotic period characterized by the accumulation of gadd45 and C/EBPalpha. A stable 3T3-L1 subline was engineered to express a dominant negative p53, human p53(143ala). The p53(143ala) subline differentiated to adipocytes and showed appropriate developmental expression of gadd45. These findings suggest that postmitotic growth arrest is coupled to adipocyte differentiation via C/EBPalpha stimulation of growth arrest-associated and phenotype-associated genes.

scholarly journals Proprotein convertases are important mediators of the adipocyte differentiation of mouse 3T3-L1 cells

2002 ◽  
Vol 115 (6) ◽  
pp. 1203-1211 ◽  
Author(s):  
Gilles Croissandeau ◽  
Ajoy Basak ◽  
Nabil G. Seidah ◽  
Michel Chrétien ◽  
Majambu Mbikay
Keyword(s):  
Adipocyte Differentiation ◽  
Nuclear Translocation ◽  
Proprotein Convertases ◽  
Proteolytic Activation ◽  
Synthetic Inhibitor ◽  
Igf Receptors ◽  
Adipose Conversion ◽  
Fibroblastic Cells

Mouse 3T3-L1 cells are widely used to study adipocyte differentiation in vitro. When treated with insulin, dexamethasone and isobutylmethylxanthine these fibroblastic cells differentiate into round triglyceride-rich adipocytes. Because several proteins implicated in adipocyte differentiation(e.g. type 1 IGF receptors) are proteolytically activated by endoproteinases of the proprotein convertase family, we sought to determine whether these endoproteinases are crucial for adipose conversion. In this study, we show that expression of the proprotein convertases PACE4, PC7 and furin increases when 3T3-L1 cells are induced to differentiate into adipocytes. The differentiation was blocked in transfected cells expressingα1-antitrypsin Portland or in normal cells pre-treated with the synthetic inhibitor decanoyl-RVKR-chloromethylketone. Both inhibitors are known to specifically inactivate proprotein convertases. The block was associated with impaired proteolytic activation of proIGF-1 receptor, absence of induction of the adipogenic transcriptional factor PPARγ and marked reduction of the nuclear translocation of the C/EBPβ factor. Taken together, these data constitute evidence that proprotein convertases are crucial mediators of adipogenesis.

Enhancement of differentiation of cultured adipogenic cells (TA1) by pertussis toxin

1992 ◽  
Vol 70 (8) ◽  
pp. 650-655 ◽  
Author(s):  
Osamu Shinohara ◽  
Yoh-Ichi Murata ◽  
Makoto Shimizu
Keyword(s):  
G Proteins ◽  
Pertussis Toxin ◽  
Adipocyte Differentiation ◽  
Dibutyryl Camp ◽  
Gtp Binding ◽  
Dose Dependent Fashion ◽  
Adipose Conversion ◽  
Adipocyte Cell ◽  
Dose Dependent

Differentiation of adipocytes is controlled by a variety of hormones and growth factors. To investigate the possible role of GTP-binding proteins (G proteins) in the process of adipose conversion, we studied the effect of pertussis toxin on differentiation of the fibroblast/adipocyte cell line (TA1). Pertussis toxin potentiated dexamethasone- and indomethacin-induced adipocyte differentiation in a time- and dose-dependent fashion. Addition of dibutyryl cAMP or forskolin inhibited adipose conversion, indicating that an abolishment of inhibitory control of adenylate cyclase is not responsible for the action of pertussis toxin. The B oligomer of the toxin did not mimic the effect of the holotoxin. Pertussis toxin catalyzed ADP-ribosylation of 40 000 molecular mass protein of the membrane fraction was dose-dependently inhibited by the pretreatment of the cells with the toxin. These results indicate the possible involvement of pertussis toxin-sensitive G proteins in adipogenesis.Key words: adipose tissue, pertussis toxin, GTP-binding protein.

895: Proteomic Analysis of Sera from Bladder Cancer Patients with MALDI-TOF-MS

2007 ◽  
Vol 177 (4S) ◽  
pp. 297-297
Author(s):  
Kristina Schwamborn ◽  
Rene Krieg ◽  
Ruth Knüchel-Clarke ◽  
Joachim Grosse ◽  
Gerhard Jakse
Keyword(s):  
Bladder Cancer ◽  
Cancer Patients ◽  
Proteomic Analysis ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms
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