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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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LRAT  -  lecithin retinol acyltransferase...

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High impact information on LRAT

  • The villus-crypt gradient of the beta-carotene cleavage enzyme activity corresponded with those of retinal reductase activity and lecithin: retinol acyltransferase (LRAT) activity, but distinct from that of acyl-CoA: retinol acyltransferase (ARAT) activity [1].
  • These results suggest that the beta-carotene cleavage enzyme is coordinately distributed along the villus-crypt axis with retinal reductase and LRAT, the two enzymes which require cellular retinol-binding protein, typeII (CRBPII) as the donor of the substrate [1].
  • Furthermore, the distribution of the content of retinyl esters was similar to that of LRAT activity [1].
  • These developmental inductions of beta-carotene cleavage enzyme and retinal reductase activities in the duodenum coincided with those of cellular retinol-binding protein, type II (CRBPII) and lecithin: retinol acyltransferase (LRAT) [2].
  • The absence of LRAT activity and retinyl esters in the chick lung suggests that the retinol in the chick lung may not be provided from retinyl ester storage, and the retinol transferred directly from serum should be utilized to generate retinoic acid [3].
 

Anatomical context of LRAT

  • Relatively high levels of LRAT activity were present in the duodenum and the liver of chicks as well as in the rat lung [3].
  • The LRAT activity in duodenal microsomes was very low at 18- and 20-day chick embryo, but exhibited a rapid (15-fold) increase during 48 h around hatching, which occurred in parallel with the abrupt elevation of the content of CRBP(II) in chick duodenum [4].
 

Associations of LRAT with chemical compounds

  • These results suggest that duodenal LRAT activity and CRBP(II) are modulated by dietary vitamin A during the perinatal period [4].
  • The LRAT activity was assayed with dilauroyl phosphatidylcholine and either complex of retinol-cellular retinol-binding protein, type two or retinol-cellular retinol-binding protein in microsomal preparations of lung, duodenum and liver of 7-day-old chicks [3].

References

 
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