Literature DB >> 2064786

[3H]-13-cis-retinoic acid covalently binds to thioredoxin reductase in human keratinocytes.

K U Schallreuter1, T Grebe, M R Pittelkow, J M Wood.   

Abstract

13-cis-Retinoic acid is a stereospecific suicide inhibitor of thioredoxin reductase. [3H]-labeled 13-cis-retinoic acid has been used to covalently label thioredoxin reductase in human keratinocytes. The acid-soluble cytosol fraction of human keratinocytes contained three radioactive proteins labeled by the addition of high-specific-activity [3H]-13-cis-retinoic acid to cell cultures. One of these proteins was identified as cytosolic keratinocyte thioredoxin reductase by fast-protein liquid chromatography and SDS-gel radioautography. The inhibition of thioredoxin reductase by 13-cis-retinoic acid may explain the known cytostatic and teratogenic properties attributed to this retinoid.

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Year:  1991        PMID: 2064786     DOI: 10.1159/000210919

Source DB:  PubMed          Journal:  Skin Pharmacol        ISSN: 1011-0283


  2 in total

1.  Covalent modification of proteins by ligands of steroid hormone receptors.

Authors:  N Takahashi; T R Breitman
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-15       Impact factor: 11.205

2.  Nuclear MEK1 sequesters PPARγ and bisects MEK1/ERK signaling: a non-canonical pathway of retinoic acid inhibition of adipocyte differentiation.

Authors:  Sandeep Dave; Ravikanth Nanduri; Hedwin Kitdorlang Dkhar; Ella Bhagyaraj; Alka Rao; Pawan Gupta
Journal:  PLoS One       Date:  2014-06-24       Impact factor: 3.240

  2 in total

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