Evaluation of cellular retinoic acid binding protein 2 gene expression through the retinoic acid pathway by co-incubation of Blastocystis ST-1 with HT29 cells in vitro

2016 ◽  
Vol 115 (5) ◽  
pp. 1965-1975
Author(s):  
Chen-Chieh Liao ◽  
Eing-Ju Song ◽  
Tsuey-Yu Chang ◽  
Wei-Chen Lin ◽  
Hsiao-Sheng Liu ◽  
...  
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Binding Protein ◽  
Acid Binding Protein ◽  
Ht29 Cells ◽  
Acid Pathway

scholarly journals Overexpression of the cellular retinoic acid binding protein-I (CRABP-I) results in a reduction in differentiation-specific gene expression in F9 teratocarcinoma cells.

1991 ◽  
Vol 112 (5) ◽  
pp. 965-979 ◽  
Author(s):  
J F Boylan ◽  
L J Gudas
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Binding Protein ◽  
Expression Vectors ◽  
Specific Gene ◽  
Specific Gene Expression ◽  
Acid Binding Protein ◽  
Retinoic Acid Response Element ◽  
Crabp I ◽  
F9 Teratocarcinoma

Treatment of F9 teratocarcinoma stem cells with retinoic acid (RA) causes their irreversible differentiation into extraembryonic endoderm. To elucidate the role of the cellular retinoic acid binding protein-I (CRABP-I) in this differentiation process, we have generated several different stably transfected F9 stem cell lines expressing either elevated or reduced levels of functional CRABP-I protein. Stably transfected lines expressing elevated levels of CRABP-I exhibit an 80-90% reduction in the RA induced expression of retinoic acid receptor (RAR) beta, laminin B1, and collagen type IV (alpha 1) mRNAs at low exogenous RA concentrations, but this reduction is eliminated at higher RA concentrations. Thus, greater expression of CRABP-I reduces the potency of RA in this differentiation system. Moreover, transfection of a CRABP-I expression vector into F9 cells resulted in five- and threefold decreases in the activation of the laminin B1 RARE (retinoic acid response element) and the RAR beta RARE, respectively, as measured from RARE/CAT expression vectors in transient transfection assays. These results support the idea that CRABP-I sequesters RA within the cell and thereby prevents RA from acting to regulate differentiation specific gene expression. Our data suggest a mechanism whereby the level of CRABP-I can regulate responsiveness to RA during development.

Nuclear retinoic acid binding protein in human prostate adenomas

1985 ◽  
Vol 105 (2) ◽  
pp. 157-162 ◽  
Author(s):  
D. Boyd ◽  
G. D. Chisholm ◽  
F. K. Habib
Keyword(s):  
Retinoic Acid ◽  
Nuclear Protein ◽  
Enzyme Inhibitors ◽  
Binding Protein ◽  
Sodium Molybdate ◽  
Human Prostate ◽  
Acid Binding Protein ◽  
All Trans Retinoic Acid ◽  
Prostate Adenoma

ABSTRACT A retinoic acid binding protein has been detected in salt extracts of nuclei obtained from human prostate adenoma. The binding was characterized by competition experiments, temperature/time studies and saturation analysis. Substantial binding was only observed after sonication of nuclei and charcoal-pretreatment of a salt extract. The binding of radiolabelled all-transretinoic acid was displaced by all-trans-retinoic acid, retinol and to a lesser extent retinal and two synthetic retinoids, RO 10-1670 and RO 13-7410. Testosterone and dihydrotestosterone, at a 100-fold excess, had little effect on the binding. The association between retinoic acid and nuclear protein was both temperature and time dependent. At 37 °C, equilibrium was rapidly reached (30 min) whereas at 4 and 25 °C, ligand binding occurred at a slower rate. Saturation analysis performed under steady-state conditions yielded a dissociation constant of 15 ±2 nmol/l. Metabolism studies failed to show conversion of either radiolabelled all-trans-retinol or [3H]retinoic acid in vitro; these data suggest that both acid and alcohol forms of vitamin A are recognized by the extracted nuclear protein. The effect of three enzyme inhibitors on [3H]retinoic acid binding was studied. Binding was unaltered in the presence of aprotinin and phenylmethylsulphonyl fluoride but sodium molybdate (10 mmol/l) increased binding by 18%. The presence of a specific retinoid binding protein in prostate nuclei suggests that retinoids may play some role in the function of the gland. J. Endocr. (1985) 105, 157–162

scholarly journals Molecular Cloning and Hormonal Regulation of a Murine Epididymal Retinoic Acid-Binding Protein Messenger Ribonucleic Acid

Endocrinology ◽  
1998 ◽  
Vol 139 (6) ◽  
pp. 2971-2981 ◽  
Author(s):  
Jean-Jacques Lareyre ◽  
Weng-Li Zheng ◽  
Guang-Quan Zhao ◽  
Susan Kasper ◽  
Marcia E. Newcomer ◽  
...  
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Secretory Protein ◽  
Primary Amino Acid Sequence ◽  
Acid Binding Protein ◽  
Primary Amino ◽  
Caput Epididymidis

Abstract A complementary DNA encoding the mouse epididymal secretory protein MEP 10 (mouse epididymal protein 10) was cloned and is now renamed murine epididymal retinoic acid binding protein (mE-RABP). The analysis of the predicted primary amino acid sequence showed that mE-RABP has a 75% identity with rat ESP I (epididymal secretory protein I), another epididymal retinoic acid-binding protein. The homology strongly suggests that mE-RABP is the mouse orthologue of rat ESP I. A computer analysis of the predicted three-dimensional structure confirmed that mE-RABP can accommodate retinoic acid as ligand. In the rat, ESP I messenger RNA (mRNA) is expressed in the efferent ducts and in the entire caput epididymidis. However, in the mouse, the expression of a 950-bp mE-RABP mRNA was detected only in principal cells of the mid/distal caput epididymidis, suggesting that the regulation of region-specific expression is different in rat and mouse. Northern blot analyses showed that mE-RABP gene expression is no longer detected 10 days after castration but progressively rebounds between days 15 and 60. However, mE-RABP protein could not be detected by Western blot 30 days after castration. Androgen replacement, begun 5 days after castration and continued for 4 days restored significant expression of mE-RABP mRNA. Efferent duct ligation for 10 days did not affect gene expression. Taken together, these results indicate that mE-RABP mRNA expression is regulated by androgens but not by testicular factors. The overall similarity in the primary amino acid sequence of mE-RABP with ESP I and other members of the lipocalin superfamily suggests that they are evolutionarily related.

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