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Fabp4  -  fatty acid binding protein 4, adipocyte

Rattus norvegicus

Synonyms: A-FABP, AFABP, ALBP, Adipocyte lipid-binding protein, Adipocyte-type fatty acid-binding protein, ...
 
 
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High impact information on Fabp4

 

Biological context of Fabp4

  • Stable transfectants showed integration into the genome for all constructs and type-specific overexpression at the mRNA and protein level for the clones with H-FABP and A-FABP cDNA constructs [5].
  • In conclusion, transfection of L6 myoblasts with A-FABP cDNA does not affect H-FABP content and fatty acid uptake, but changes fatty acid metabolism [5].
  • A very slow cross-reaction was also found with anti-serum to rat ALBP [6].
  • To understand the difference in energy metabolisms in brown (BAT) and white (WAT) adipose tissues, we examined the steady-state transcript levels of the heart-type and adipose-type fatty acid binding proteins (H-FABP and A-FABP, respectively) by Northern blot analysis [7].
 

Anatomical context of Fabp4

  • The rate of proliferation of myoblasts transfected with rat A-FABP cDNA was 2-fold higher compared with all other transfected cells [5].
 

Associations of Fabp4 with chemical compounds

 

Other interactions of Fabp4

  • Among a series of adipocyte transcripts, only the adipocyte lipid binding protein mRNA is also increased by DHA, although later than the PEPCK mRNA and at a much lower extent [10].
  • Finally, the A-FABP proteins, in contrast to the I-FABP proteins, reveal significant heat capacity changes (DeltaCp) upon FA binding, and substitutions at residues Arg106 and Arg126 reduce the magnitude of DeltaCp [2].

References

  1. Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein. Shen, W.J., Sridhar, K., Bernlohr, D.A., Kraemer, F.B. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins. Richieri, G.V., Low, P.J., Ogata, R.T., Kleinfeld, A.M. J. Biol. Chem. (1998) [Pubmed]
  3. Characterization of a cloned cDNA encoding rabbit myelin P2 protein. Narayanan, V., Barbosa, E., Reed, R., Tennekoon, G. J. Biol. Chem. (1988) [Pubmed]
  4. A novel testicular protein, with sequence similarities to a family of lipid binding proteins, is a major component of the rat sperm perinuclear theca. Oko, R., Morales, C.R. Dev. Biol. (1994) [Pubmed]
  5. Transfection of L6 myoblasts with adipocyte fatty acid-binding protein cDNA does not affect fatty acid uptake but disturbs lipid metabolism and fusion. Prinsen, C.F., Veerkamp, J.H. Biochem. J. (1998) [Pubmed]
  6. Presence of a fatty acid-binding protein in the armadillo Harderian gland. Cavagnari, B.M., Córdoba, O.L., Veerkamp, J.H., Santomé, J.A., Affanni, J.M. Int. J. Biochem. Cell Biol. (1998) [Pubmed]
  7. Dramatic enhancement of the specific expression of the heart-type fatty acid binding protein in rat brown adipose tissue by cold exposure. Daikoku, T., Shinohara, Y., Shima, A., Yamazaki, N., Terada, H. FEBS Lett. (1997) [Pubmed]
  8. Dehydroepiandrosterone down-regulates the expression of peroxisome proliferator-activated receptor gamma in adipocytes. Kajita, K., Ishizuka, T., Mune, T., Miura, A., Ishizawa, M., Kanoh, Y., Kawai, Y., Natsume, Y., Yasuda, K. Endocrinology (2003) [Pubmed]
  9. Fatty acid uptake in diabetic rat adipocytes. Fraser, H., Coles, S.M., Woodford, J.K., Frolov, A.A., Murphy, E.J., Schroeder, F., Bernlohr, D.A., Grund, V. Mol. Cell. Biochem. (1997) [Pubmed]
  10. Evidence for selective induction of phosphoenolpyruvate carboxykinase gene expression by unsaturated and nonmetabolized fatty acids in adipocytes. Duplus, E., Glorian, M., Tordjman, J., Berge, R., Forest, C. J. Cell. Biochem. (2002) [Pubmed]
 
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