The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Lrat  -  lecithin-retinol acyltransferase...

Mus musculus

Synonyms: 1300010A18Rik, AI449251, Lecithin retinol acyltransferase, Phosphatidylcholine--retinol O-acyltransferase, Phosphatidylcholine-retinol-O-acyltransferase
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Lrat

  • Despite the absence of significant retinyl ester stores and stellate cell lipid droplets, the livers of Lrat-/- mice upon histologic analysis appear normal and show no histological signs of liver fibrosis [1].
  • Mice lacking the visual cycle enzymes RPE65 or lecithin-retinol acyl transferase (Lrat) have pupillary light responses (PLR) that are less sensitive than those of mice with outer retinal degeneration (rd/rd or rdta) [2].
  • Gene therapy using intraocular injection of recombinant adeno-associated virus carrying the Lrat gene successfully restored electroretinographic responses to approximately 50% of wild-type levels (p < 0.05 versus wild-type and knockout controls), and pupillary light responses (PLRs) of Lrat-/- mice increased approximately 2.5 log units (p < 0.05) [3].
 

High impact information on Lrat

  • RESTs accumulate in Rpe65-/- mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/- mice deficient in retinyl ester synthesis [4].
  • Inner retinal photoresponses are mediated by melanopsin-expressing, intrinsically photosensitive retinal ganglion cells (ipRGCs), suggesting that the melanopsin-dependent photocycle utilizes RPE65 and Lrat [2].
  • Although the Lrat-/- mice possess only trace amounts of retinyl esters in liver, lung, and kidney, they possess elevated (by 2-3-fold) concentrations of retinyl esters in adipose tissue compared with wild type mice [1].
  • Lrat-/- mice absorb dietary retinol primarily as free retinol in chylomicrons; however, retinyl esters are also present within the chylomicron fraction obtained from Lrat-/- mice [1].
  • Examination by electron microscopy reveals a striking total absence of large lipid-containing droplets that normally store hepatic retinoid within the hepatic stellate cells of Lrat-/- mice [1].
 

Biological context of Lrat

  • We disrupted mouse Lrat gene expression by targeted recombination and generated a homozygous Lrat knock-out (Lrat-/-) mouse [5].
  • We have studied Lrat-deficient (Lrat-/-) mice to gain a better understanding of how these mice take up and store dietary retinoids and to determine whether other enzymes may be responsible for retinol esterification in the body [1].
 

Anatomical context of Lrat

 

Associations of Lrat with chemical compounds

  • We conclude that Lrat-/- mice may serve as an animal model with early onset severe retinal dystrophy and severe retinyl ester deprivation [5].
  • Lrat-/- mice have trace levels of all-trans-retinyl esters in the liver, lung, eye, and blood, whereas the circulating all-trans-retinol is reduced only slightly [5].
  • All-trans-13,14-dihydroretinoic acid was detected in vivo in Lrat-/- mice supplemented with retinyl palmitate [6].
 

Other interactions of Lrat

 

Analytical, diagnostic and therapeutic context of Lrat

  • Here, we report that two interventions--intraocular gene therapy and oral pharmacologic treatment with novel retinoid compounds--each restore retinal function to Lrat-/- mice [3].

References

  1. Retinoid absorption and storage is impaired in mice lacking lecithin:retinol acyltransferase (LRAT). O'Byrne, S.M., Wongsiriroj, N., Libien, J., Vogel, S., Goldberg, I.J., Baehr, W., Palczewski, K., Blaner, W.S. J. Biol. Chem. (2005) [Pubmed]
  2. Inner retinal photoreception independent of the visual retinoid cycle. Tu, D.C., Owens, L.A., Anderson, L., Golczak, M., Doyle, S.E., McCall, M., Menaker, M., Palczewski, K., Van Gelder, R.N. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Pharmacological and rAAV gene therapy rescue of visual functions in a blind mouse model of Leber congenital amaurosis. Batten, M.L., Imanishi, Y., Tu, D.C., Doan, T., Zhu, L., Pang, J., Glushakova, L., Moise, A.R., Baehr, W., Van Gelder, R.N., Hauswirth, W.W., Rieke, F., Palczewski, K. PLoS Med. (2005) [Pubmed]
  4. Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye. Imanishi, Y., Batten, M.L., Piston, D.W., Baehr, W., Palczewski, K. J. Cell Biol. (2004) [Pubmed]
  5. Lecithin-retinol acyltransferase is essential for accumulation of all-trans-retinyl esters in the eye and in the liver. Batten, M.L., Imanishi, Y., Maeda, T., Tu, D.C., Moise, A.R., Bronson, D., Possin, D., Van Gelder, R.N., Baehr, W., Palczewski, K. J. Biol. Chem. (2004) [Pubmed]
  6. Metabolism and transactivation activity of 13,14-dihydroretinoic acid. Moise, A.R., Kuksa, V., Blaner, W.S., Baehr, W., Palczewski, K. J. Biol. Chem. (2005) [Pubmed]
  7. Cellular retinol-binding protein type III is needed for retinoid incorporation into milk. Piantedosi, R., Ghyselinck, N., Blaner, W.S., Vogel, S. J. Biol. Chem. (2005) [Pubmed]
 
WikiGenes - Universities