Retinoic acid mediates post-transcriptional regulation of keratin 19 mRNA levels

1993 ◽  
Vol 106 (1) ◽  
pp. 183-188 ◽  
Author(s):  
D.L. Crowe
Keyword(s):  
Retinoic Acid ◽  
Mrna Stability ◽  
Specific Pattern ◽  
Mrna Levels ◽  
Site Specific ◽  
Keratin 19 ◽  
Squamous Epithelia ◽  
A Site ◽  
Post Transcriptional Regulation ◽  
Keratin Intermediate Filaments

Stratified squamous epithelia have been shown to preferentially express a site-specific pattern of keratin intermediate filaments. Retinoic acid (RA) is known to modulate expression of the basal cell keratins K19 and K5. Expression of these genes is dependent on extracellular RA concentration. We have found that K19 mRNA levels increase over time in cultured keratinocytes exposed to elevated concentrations of RA. K5 mRNA levels decrease in response to RA in a similar fashion. The observed changes in K5 message are primarily the result of RA-induced alterations in gene transcription. However, the RA-mediated induction of K19 mRNA is not the result of increased transcription but is primarily due to enhanced mRNA stability. These results suggest that an RA-dependent post-transcriptional mechanism modulates K19 intermediate filament expression in stratified squamous epithelia.

Mechanism of all trans-retinoic acid and glucocorticoid regulation of surfactant protein mRNA

1998 ◽  
Vol 274 (4) ◽  
pp. L560-L566 ◽  
Author(s):  
Thomas N. George ◽  
Olga L. Miakotina ◽  
Kelli L. Goss ◽  
Jeanne M. Snyder
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Gene Transcription ◽  
Mrna Stability ◽  
Half Life ◽  
Normal Function ◽  
Mrna Levels ◽  
Trans Retinoic Acid ◽  
All Trans Retinoic Acid ◽  
Mrna Half Life

The surfactant proteins (SPs) are required for the normal function of pulmonary surfactant, a lipoprotein substance that prevents alveolar collapse at end expiration. We characterized the effects of cortisol and all trans-retinoic acid (RA) on SP-A and SP-B gene expression in H441 cells, a human pulmonary adenocarcinoma cell line. Cortisol, at 10−6M, caused a significant inhibition of SP-A mRNA to levels that were 60–70% of controls and a five- to sixfold increase in the levels of SP-B mRNA. RA alone (10−6M) had no effect on SP-A mRNA levels and modestly reduced the inhibitory effect of cortisol. RA alone and the combination of cortisol and RA both significantly increased SP-B mRNA levels. RA had no effect on the rate of SP-A gene transcription or on SP-A mRNA stability. Cortisol alone and the combination of cortisol and RA significantly inhibited the rate of SP-A gene transcription but had no effect on SP-A mRNA half-life. RA at 10−6 M had no effect on the rate of SP-B gene transcription but prolonged SP-B mRNA half-life. Cortisol alone and the combination of cortisol and RA caused a significant increase in the rate of SP-B gene transcription and also caused a significant increase in SP-B mRNA stability. We conclude that RA has no effect on SP-A gene expression and increases SP-B mRNA levels by an effect on SP-B mRNA stability and not on the rate of SP-B gene transcription. In addition, the effects of the combination of RA and cortisol were generally similar to those of cortisol alone.

Comprehensive Analysis of Lysine Acetylome Reveals a Site-Specific Pattern in Rapamycin-Induced Autophagy

2018 ◽  
Vol 18 (3) ◽  
pp. 865-877 ◽  
Author(s):  
Zhuo Zhou ◽  
Yu Chen ◽  
Mengqi Jin ◽  
Jianqin He ◽  
Ayiding Guli ◽  
...  
Keyword(s):  
Specific Pattern ◽  
Comprehensive Analysis ◽  
Site Specific ◽  
A Site

Destabilization of TNF-α mRNA by retinoic acid in hepatic macrophages: implications for alcoholic liver disease

2001 ◽  
Vol 281 (3) ◽  
pp. E420-E429 ◽  
Author(s):  
Kenta Motomura ◽  
Mitsuru Ohata ◽  
Michael Satre ◽  
Hidekazu Tsukamoto
Keyword(s):  
Retinoic Acid ◽  
Liver Disease ◽  
Alcoholic Liver Disease ◽  
Mrna Stability ◽  
Transforming Growth Factor ◽  
Cytokine Expression ◽  
Retinol Binding Protein ◽  
Mrna Levels ◽  
Tnf Α ◽  
Specific Ligand

Retinoic acid (RA) inhibits hepatic macrophage (HM) cytokine expression, and retinoids are depleted in alcoholic liver disease (ALD). However, neither the causal link between the two nor the mechanism underlying RA-mediated HM inhibition is known. The aim of the present study was to determine the mechanism of RA-induced inhibition of HM tumor necrosis factor (TNF)-α expression and the relevance of this regulation to ALD. Treatment with all- trans RA (500 nM) caused a 50% inhibition in lipopolysaccharide (LPS)-stimulated TNF-α expression by cultured normal rat HM. The mRNA levels for inducible nitric oxide synthase, interleukin (IL)-6, IL-1α, and IL-1β were also reduced, whereas those for transforming growth factor-β1, MMP-9, and membrane cofactor protein-1 were unaffected. The inhibitory effect on TNF-α expression was reproduced by LG268, a retinoid X receptor (RXR)-specific ligand, but not by TTNPB, an RA receptor (RAR)-specific ligand. RA did not alter LPS-stimulated NF-kB and activation protein-1 binding but significantly decreased TNF-α mRNA stability in HM. HM isolated from the ALD model showed significant decreases in all- trans RA (−48%) and 9- cis RA (−61%) contents, RA response element (RARE) binding, and mRNA levels for RARβ, RXRα, and cytosolic retinol binding protein-1, whereas TNF-α mRNA expression was induced. TNF-α mRNA stability was increased in these cells, and an ex vivo treatment with all- trans RA normalized both RARβ and TNF-α mRNA levels. These results demonstrate the RA-induced destabilization of TNF-α mRNA by cultured HM and the association of RA depletion with increased TNF-α mRNA stability in HM from experimental ALD. These findings suggest that RA depletion primes HM for proinflammatory cytokine expression in ALD, at least in part, via posttranscriptional regulation.

A type I collagen substrate increases PTH/PTHrP receptor mRNA expression and suppresses PTHrP mRNA expression in UMR106–06 osteoblast-like cells

1996 ◽  
Vol 150 (2) ◽  
pp. 299-308 ◽  
Author(s):  
S Celic ◽  
P J Chilco ◽  
J D Zajac ◽  
T J Martin ◽  
D M Findlay
Keyword(s):  
Retinoic Acid ◽  
Mrna Expression ◽  
Mrna Stability ◽  
Type I Collagen ◽  
Type I ◽  
Mrna Levels ◽  
Receptor Mrna ◽  
Pthrp Receptor ◽  
Camp Levels ◽  
In Cells

Abstract We have previously shown that the response of osteoblasts to parathyroid hormone (PTH) can be influenced at the receptor level by growth on the physiological substrate, type I collagen, or by treatment with retinoic acid. We have also shown differential expression of genes when cells of the osteoblast lineage are grown on type I collagen. The aim of this study was therefore to examine the effect of retinoic acid and growth on type I collagen on PTH/PTH-related protein (PTHrP) receptor mRNA expression in the osteosarcoma osteoblast-like cell line UMR106–06. PTH/PTHrP receptor mRNA levels, as assessed by Northern blot, of cells grown on collagen were increased up to 2-fold compared with cells on plastic and in a concentration-dependent manner with respect to collagen. An increase was seen as early as 6 h and was maintained over a 24 h period. This was not due to increased mRNA stability. Retinoic acid decreased the level of receptor mRNA on both plastic and collagen at each time but did not alter mRNA stability. For all treatments PTH/PTHrP receptor mRNA abundance, relative to glyceraldehyde-3-phosphate dehydrogenase, increased steadily over 24 h after subculture of cells. In contrast, PTHrP mRNA levels were reduced in cells on collagen, compared with plastic. PTH-stimulated cAMP levels of cells grown on collagen were increased compared with plastic at 24 h, but not earlier. Consistent with the mRNA data, retinoic acid decreased the amplitude of cAMP responses in cells on plastic and collagen. There was no evidence for changes in adenylate cyclase per se, since forskolin-induced cAMP levels did not change with either treatment. This study shows that known modulators of osteoblast maturation also affect signal transduction in these cells by regulating gene expression of the PTH/PTHrP receptor as well as the PTHrP ligand. Journal of Endocrinology (1996) 150, 299–308

scholarly journals Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene.

1989 ◽  
Vol 9 (4) ◽  
pp. 1507-1512 ◽  
Author(s):  
H Zhu ◽  
H Conrad-Webb ◽  
X S Liao ◽  
P S Perlman ◽  
R A Butow
Keyword(s):  
Genetic Analysis ◽  
Rna Processing ◽  
Fold Increase ◽  
Functional Expression ◽  
Rrna Gene ◽  
Yeast Mitochondria ◽  
Wild Type ◽  
Site Specific ◽  
Var1 Gene ◽  
A Site

All mRNAs of yeast mitochondria are processed at their 3' ends within a conserved dodecamer sequence, 5'-AAUAAUAUUCUU-3'. A dominant nuclear suppressor, SUV3-I, was previously isolated because it suppresses a dodecamer deletion at the 3' end of the var1 gene. We have tested the effects of SUV3-1 on a mutant containing two adjacent transversions within a dodecamer at the 3' end of fit1, a gene located within the 1,143-base-pair intron of the 21S rRNA gene, whose product is a site-specific endonuclease required in crosses for the quantitative transmission of that intron to 21S alleles that lack it. The fit1 dodecamer mutations blocked both intron transmission and dodecamer cleavage, neither of which was suppressed by SUV3-1 when present in heterozygous or homozygous configurations. Unexpectedly, we found that SUV3-1 completely blocked cleavage of the wild-type fit1 dodecamer and, in SUV3-1 homozygous crosses, intron conversion. In addition, SUV3-1 resulted in at least a 40-fold increase in the amount of excised intron accumulated. Genetic analysis showed that these phenotypes resulted from the same mutation. We conclude that cleavage of a wild-type dodecamer sequence at the 3' end of the fit1 gene is essential for fit1 expression.

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