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Gene Review

adp  -  adipose

Drosophila melanogaster

Synonyms: CG5124, Dmel\CG5124, anon-WO0196371.1, anon-WO0196371.27, anon-WO0196371.3
 
 
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Disease relevance of adp

  • Here, we report the identification of the adipose (adp) gene, the mutation of which causes obesity in Drosophila [1].
 

High impact information on adp

  • ENC-1 mRNA levels are transiently increased 8-12-fold early in in vitro adipocyte differentiation of primary cells of the adipose-derived stroma-vascular fraction and of 3T3-L1 cells [2].
  • By contrast, adp gain-of-function causes a specific reduction of the fat body in Drosophila. adp encodes an evolutionarily conserved WD40/tetratricopeptide-repeat-domain protein that is likely to represent an intermediate in a novel signalling pathway [1].
  • Ablation of the cholesterol transporter adenosine triphosphate-binding cassette transporter G1 reduces adipose cell size and protects against diet-induced obesity [3].
  • In NZO mice, an Abcg1 variant was identified in a suggestive adiposity quantitative trait locus and was associated with higher expression of the gene in white adipose tissue [3].
  • A genetic analysis shows that heterozygosity for a chromosomal deletion that removes CG3488 dominantly enhances the excess lipid phenotype associated with a mutation in adipose, an uncloned obesity gene [4].
 

Biological context of adp

  • Two mammalian members of this family, Perilipin and adipose differentiation-related protein, are involved in lipid storage and regulate lipolysis [5].
 

Anatomical context of adp

  • The NR1D subgroup is highly enriched in peripheral tissues with onerous energy demands including skeletal muscle, brown and white adipose, brain, liver and kidney [6].
 

Other interactions of adp

  • Spatially, it was ascertained that catalase expression is mostly confined to tissues related to intermediary metabolism, digestive and adipose systems as well as oenocytes [7].

References

  1. Control of triglyceride storage by a WD40/TPR-domain protein. Häder, T., Müller, S., Aguilera, M., Eulenberg, K.G., Steuernagel, A., Ciossek, T., Kühnlein, R.P., Lemaire, L., Fritsch, R., Dohrmann, C., Vetter, I.R., Jäckle, H., Doane, W.W., Brönner, G. EMBO Rep. (2003) [Pubmed]
  2. Transient induction of ENC-1, a Kelch-related actin-binding protein, is required for adipocyte differentiation. Zhao, L., Gregoire, F., Sul, H.S. J. Biol. Chem. (2000) [Pubmed]
  3. Ablation of the cholesterol transporter adenosine triphosphate-binding cassette transporter G1 reduces adipose cell size and protects against diet-induced obesity. Buchmann, J., Meyer, C., Neschen, S., Augustin, R., Schmolz, K., Kluge, R., Al-Hasani, H., Jürgens, H., Eulenberg, K., Wehr, R., Dohrmann, C., Joost, H.G., Schürmann, A. Endocrinology (2007) [Pubmed]
  4. Alpha/beta hydrolase2, a predicated gene adjacent to mad in Drosophila melanogaster, belongs to a new global multigene family and is associated with obesity. Wisotzkey, R.G., Johnson, A.N., Takaesu, N.T., Newfeld, S.J. J. Mol. Evol. (2003) [Pubmed]
  5. Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism. Teixeira, L., Rabouille, C., Rørth, P., Ephrussi, A., Vanzo, N.F. Mech. Dev. (2003) [Pubmed]
  6. The orphan Rev-erb nuclear receptors: a link between metabolism, circadian rhythm and inflammation? Ramakrishnan, S.N., Muscat, G.E. Nuclear receptor signaling [electronic resource] : the e-journal of NURSA. (2006) [Pubmed]
  7. Profiling catalase gene expression in Drosophila melanogaster during development and aging. Klichko, V.I., Radyuk, S.N., Orr, W.C. Arch. Insect Biochem. Physiol. (2004) [Pubmed]
 
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