Effects of retinoic acid onN-glycosylation and mRNA stability of the liver/bone/kidney alkaline phosphatase in neuronal cells

2000 ◽  
Vol 182 (1) ◽  
pp. 50-61 ◽  
Author(s):  
Walter H. Mueller ◽  
Dagmar Kleefeld ◽  
Barbara Khattab ◽  
Joachim D. Meissner ◽  
Renate J. Scheibe
Keyword(s):  
Alkaline Phosphatase ◽  
Retinoic Acid ◽  
Mrna Stability ◽  
Neuronal Cells ◽  
Kidney Alkaline Phosphatase

scholarly journals Evidence for the importance of arginine residues in pig kidney alkaline phosphatase

1979 ◽  
Vol 181 (1) ◽  
pp. 137-142 ◽  
Author(s):  
M N Woodroofe ◽  
P J Butterworth
Keyword(s):  
Alkaline Phosphatase ◽  
Active Site ◽  
Competitive Inhibitor ◽  
Arginine Residue ◽  
Pig Kidney ◽  
Close Proximity ◽  
Arginine Residues ◽  
Km Value ◽  
Uncompetitive Inhibitor ◽  
Kidney Alkaline Phosphatase

The arginine-specific reagents 2,3-butanedione and phenylglyoxal inactivate pig kidney alkaline phosphatase. As inactivation proceeds there is a progressive fall in Vmax. of the enzyme, but no demonstrable change in the Km value for substrate. Pi, a competitive inhibitor, and AMP, a substrate of the enzyme, protect alkaline phosphatase against the arginine-specific reagents. These effects are explicable by the assumption that the enzyme contains an essential arginine residue at the active site. Protection is also afforded by the uncompetitive inhibitor NADH through a partially competive action against the reagents. Enzyme that has been exposed to the reagents has a decreased sensitivity to NADH inhibition. It is suggested that an arginine residue is important for NADH binding also, although this residue is distinct from that at the catalytic site. The protection given by NADH against loss of activity is indicative of the close proximity of the active and NADH sites.

Interleukin-1β enhances retinoic acid-mediated expression of bone-type alkaline phosphatase in rat IEC-6 cells

2001 ◽  
Vol 280 (3) ◽  
pp. G510-G517 ◽  
Author(s):  
Takeshi Nikawa ◽  
Madoka Ikemoto ◽  
Kaori Tokuoka ◽  
Shigetada Teshima ◽  
David H. Alpers ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Transcript Level ◽  
Intestinal Epithelial ◽  
Alp Activity ◽  
Kinase C ◽  
Fetal Rat ◽  
Epidermal Growth

We previously showed that vitamin A upregulated the expression of bone-type alkaline phosphatase (ALP) in fetal rat small intestine and rat intestinal IEC-6 cells. In this study, we examined interactions between retinoic acid (RA) and several growth factors/cytokines on the isozyme expression in IEC-6 cells. Epidermal growth factor and interleukins (ILs)-2, -4, -5, and -6 completely blocked the RA-mediated increase in ALP activity. In contrast, IL-1β markedly increased the activity, protein, and mRNA of the bone-type ALP only when RA was present. IL-1β and/or RA did not change the type 1 IL-1 receptor transcript level, whereas IL-1β enhanced the RA-induced expressions of retinoic acid receptor-β (RAR-β) and retinoid X receptor-β (RXR-β) mRNAs and RA-mediated RXR response element binding. The synergism of IL-1β and RA on ALP activity was completely blocked by protein kinase C (PKC) inhibitors. Our results suggest that IL-1β may modify the ALP isozyme expression in small intestinal epithelial cells by stimulating PKC-dependent, RAR-β- and/or RXR-β-mediated signaling pathways.

scholarly journals Retinoic acid induces liver/bone/kidney-type alkaline phosphatase gene expression in F9 teratocarcinoma cells

1991 ◽  
Vol 274 (3) ◽  
pp. 673-678 ◽  
Author(s):  
M Gianni ◽  
M Studer ◽  
G Carpani ◽  
M Terao ◽  
E Garattini
Keyword(s):  
Alkaline Phosphatase ◽  
Retinoic Acid ◽  
De Novo ◽  
F9 Cells ◽  
Alp Activity ◽  
Mrna Induction ◽  
All Trans Retinoic Acid ◽  
Teratocarcinoma Cells ◽  
F9 Teratocarcinoma ◽  
De Novo Protein Synthesis

All-trans retinoic acid (RA) induces alkaline phosphatase (ALP) activity by 3-8-fold in murine F9 teratocarcinoma cells, in parallel with their differentiation towards primitive endoderm. The elevation of ALP activity is associated with increases in the amounts of liver/bone/kidney-type ALP protein and the respective transcript. These effects of RA are due to activation of ALP gene transcription rather than to an increase in the half-life of the mRNA. Induction of ALP mRNA does not require de novo protein synthesis, since it is not blocked by treatment with cycloheximide. Dibutyryl cyclic AMP, which is known to induce further differentiation of F9 cells from the primitive to the parietal endoderm, blocks the induction of ALP mRNA by RA.

Identification of Functional Groups of Pig Kidney Alkaline Phosphatase by Specific Inhibitors

1975 ◽  
Vol 30 (11-12) ◽  
pp. 829-831 ◽  
Author(s):  
Jan Ahlers
Keyword(s):  
Alkaline Phosphatase ◽  
Functional Groups ◽  
Pig Kidney ◽  
Kidney Alkaline Phosphatase ◽  
Specific Inhibitors ◽  
Regulatory Sites

Abstract Inactivation studies with 17 group-specific inhibitors showed that amino, hystidyl and tyrosyl residues probably are components of the active and/or regulatory sites of pig kidney alkaline phosphatase.

scholarly journals Rapid Effects of Retinoic Acid on CREB and ERK Phosphorylation in Neuronal Cells

2004 ◽  
Vol 15 (12) ◽  
pp. 5583-5592 ◽  
Author(s):  
Estela Cañón ◽  
Jose Miguel Cosgaya ◽  
Sona Scsucova ◽  
Ana Aranda
Keyword(s):  
Retinoic Acid ◽  
Transcriptional Activity ◽  
Target Genes ◽  
Primary Cultures ◽  
Neuronal Cells ◽  
Neuronal Cell ◽  
Direct Stimulation ◽  
Creb Phosphorylation ◽  
Response Elements ◽  
Stimulation Of

Retinoic acid (RA) is a potent regulator of neuronal cell differentiation. RA normally activates gene expression by binding to nuclear receptors that interact with response elements (RAREs) in regulatory regions of target genes. We show here that in PC12 cell subclones in which the retinoid causes neurite extension, RA induces a rapid and sustained phosphorylation of CREB (cyclic AMP response element binding protein), compatible with a nongenomic effect. RA also causes a rapid increase of CREB phosphorylation in primary cultures of cerebrocortical cells and of dorsal root ganglia neurons from rat embryos. RA-mediated phosphorylation of CREB leads to a direct stimulation of CREB-dependent transcriptional activity and to activation of the expression of genes such as c-fos, which do not contain RAREs but contain cAMP response elements (CREs) in their promoters. CREB is a major target of extracellular signal regulated kinase ERK1/2 signaling in neuronal cells, and we demonstrate here that RA induces an early stimulation of ERK1/2, which is required both for CREB phosphorylation and transcriptional activity. These results demonstrate that RA, by a nongenomic mechanism, stimulates signaling pathways that lead to phosphorylation of transcription factors, which in turn activate the transcription of genes involved in neuronal differentiation.

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