Inversely related expression of epidermal- and heart-type fatty acid binding proteins during myogenic differentiation of C2C12 myoblasts

Bleck, Bertram; Buhlmann, Carsten; Hohoff, Carsten; Müller, Martin; Börchers, Torsten; Spener, Friedrich

doi:10.1002/1438-9312(200202)104:2<88::aid-ejlt88>3.0.co;2-g

Cited by 3 publications

(1 citation statement)

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“…This appeared to be a more physiological approach as we had found earlier that E-and H-FABP genes are inversely expressed in this muscle cell line during differentiation from myoblast to myotube stages [28]. Moreover, C 2 C 12 cells express all PPAR subtypes (results not shown).…”

Section: Figure 2 Dependence Of Transactivation Potentials Of Ppar/rxmentioning

confidence: 99%

Functional analysis of peroxisome-proliferator-responsive element motifs in genes of fatty acid-binding proteins

Schachtrup

Emmler

Bleck

et al. 2004

Biochemical Journal

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Retinoic acids and long-chain fatty acids are lipophilic agonists of nuclear receptors such as RXRs (retinoic X receptors) and PPARs (peroxisome-proliferator-activated receptors) respectively. These agonists are also ligands of intracellular lipid-binding proteins, which include FABPs (fatty acid-binding proteins). We reported previously that L (liver-type)-FABP targets fatty acids to the nucleus of hepatocytes and affects PPARα activation, which binds together with an RXR subtype to a PPRE (peroxisome-proliferator-responsive element). In the present study, we first determined the optimal combination of murine PPAR/RXR subtypes for binding to known murine FABP-PPREs and to those found by computer search and then tested their in vitro functionality. We show that all PPARs bind to L-FABP-PPRE, PPARα, PPARγ 1 and PPARγ 2 to A (adipocyte-type)-FABP-PPRE. All PPAR/RXR heterodimers transactivate L-FABP-PPRE, best are combinations of PPARα with RXRα or RXRγ . In contrast, PPARα heterodimers do not transactivate A-FABP-PPRE, best combinations are of PPARγ 1 with RXRα and RXRγ , and of PPARγ 2 with all RXR subtypes. We found that the predicted E (epidermal-type)-and H (heart-type)-FABP-PPREs are not activated by any PPAR/RXR combination without or with the PPAR pan-agonist bezafibrate. In the same way, C 2 C 12 myoblasts transfected with promoter fragments of E-FABP and H-FABP genes containing putative PPREs are also not activated through stimulation of PPARs with bezafibrate applied to the cells. These results demonstrate that only PPREs of L-and A-FABP promoters are functional, and that binding of PPAR/RXR heterodimers to a PPRE in vitro does not necessarily predict transactivation.

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Section: Figure 2 Dependence Of Transactivation Potentials Of Ppar/rxmentioning

confidence: 99%