Porcine conceptus and endometrial retinoid-binding proteins

1994 ◽  
Vol 6 (2) ◽  
pp. 211 ◽  
Author(s):  
JP Harney ◽  
M Ali ◽  
WV Vedeckis ◽  
FW Bazer
Keyword(s):  
Retinoic Acid ◽  
Blot Analysis ◽  
Retinoic Acid Receptor ◽  
Retinol Binding Protein ◽  
Secretory Proteins ◽  
Binding Studies ◽  
Fetal Tissues ◽  
Porcine Conceptus ◽  
Retinoid Binding Proteins ◽  
Regulatory Effects

Porcine conceptus secretory proteins were obtained from medium in which pig conceptuses, collected on Day 15 of pregnancy, were cultured for 30 h. Culture medium was pooled, dialysed and concentrated by Amicon ultrafiltration for retinol and retinoic acid (RA) binding studies. Proteins in the 20-kDa range, conceptus-secreted retinol-binding protein (RBP), bound both [3H]retinol and [3H]RA specifically. Cross-competition experiments indicate that [3H]RA was completely displaced with excess cold retinol; however, excess cold RA did not completely displace [3H]retinol, suggesting that conceptus RBP has greater affinity for retinol than RA. Cellular RBP and retinoic acid receptor (RAR)-alpha and RAR-gamma mRNA transcripts (0.7 kb; 3.8 and 2.8 kb; 3.4 kb respectively) were detected in poly (A)+ RNA isolated from Day-15 conceptus, Day-15 pregnant endometrium, late pregnant myometrium and late pregnant fetal tissues of pigs by Northern blot analysis. RAR-alpha and RAR-gamma immunoreactive proteins were detected in extracts of Day-15 conceptus, Day-15 pregnant endometrium and late pregnant fetal tissues by Western blot analysis. Collectively, results indicate that biochemical molecules required for retinoid transport, metabolism and regulatory effects are present in porcine conceptus and endometrial tissues during early pregnancy in swine.

Lung retinol storing cells synthesize and secrete retinoic acid, an inducer of alveolus formation

2004 ◽  
Vol 286 (2) ◽  
pp. L249-L256 ◽  
Author(s):  
Ghenima Dirami ◽  
Gloria DeCarlo Massaro ◽  
Linda Biadasz Clerch ◽  
Una S. Ryan ◽  
Peter R. Reczek ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Retinol Binding Protein ◽  
Microvascular Endothelial Cell ◽  
Alveolar Wall ◽  
Retinoid Signaling ◽  
All Trans Retinoic Acid ◽  
Wall Cell ◽  
Pulmonary Microvascular Endothelial Cell ◽  
Storage Granules

Retinoids play a key role in the formation of pulmonary alveoli. Lipid interstitial cells (LICs) of the alveolar wall store retinol and are concentrated at sites of alveolus formation, suggesting they are an endogenous source of retinoids for alveolus formation. We show in cultured rat lung cells that LICs synthesize and secrete all- trans retinoic acid (ATRA); its secretion is halved by dexamethasone, an inhibitor of alveolus formation. In a second alveolar wall cell, the pulmonary microvascular endothelial cell (PMVC), ATRA increases expression of the mRNA of cellular retinol binding protein-I (CRBP-I), a protein involved in ATRA synthesis. Serum-free, exogenous ATRA-free medium conditioned by LICs rich in retinol storage granules caused a 10-fold greater increase of CRBP-I mRNA in PMVCs than media conditioned by LICs with few retinol storage granules. This action of medium conditioned by retinol storage granule-rich LICs is decreased by a retinoic acid receptor pan-antagonist and by a retinoid X receptor pan-antagonist, suggesting the responsible molecule(s) is a retinoid and that retinoid signaling occurs in a paracrine fashion.

scholarly journals Specific interaction of ivermectin with retinol-binding protein from filarial parasites

1988 ◽  
Vol 249 (3) ◽  
pp. 929-932 ◽  
Author(s):  
B P Sani ◽  
A Vaid
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Specific Interaction ◽  
Retinol Binding Protein ◽  
Binding Affinities ◽  
Binding Studies ◽  
Retinoic Acid Binding Proteins ◽  
Parasitic Worms ◽  
Host Tissues

Specific cellular binding proteins for retinol and retinoic acid from mammalian and avian species may mediate the action of retinoids in the control of epithelial differentiation, growth and tumorigenesis. Parasite retinol-binding protein (PRBP) and parasite retinoic acid-binding protein (PRABP) isolated and characterized from parasitic worms of the family Filarioidea might be involved in some possible action of vitamin A compounds in these parasites. Ivermectin, a potent and widely used anti-parasitic drug, competes efficiently with retinol for retinol-binding sites on PRBP, but not for the host-tissue retinol-binding-protein sites. The drug has no affinity for retinoic acid-binding proteins from either parasite or host tissues. Binding studies using radiolabelled ivermectin and retinol reveal that ivermectin has a higher affinity than retinol for PRBP. A correlation exists between the binding affinities of ivermectin analogues and their anti-parasitic activities. A binding-protein-mediated interrelationship may exist between the actions of retinol and ivermectin in the parasites, but not in the host tissues.

Temporal/spatial expression of retinoid binding proteins and RAR isoforms in the postnatal lung

2002 ◽  
Vol 282 (3) ◽  
pp. L468-L476 ◽  
Author(s):  
Matthew Hind ◽  
Jonathan Corcoran ◽  
Malcolm Maden
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Retinoic Acid Receptor ◽  
Rt Pcr ◽  
Spatial Expression ◽  
Retinoid Signaling ◽  
Adult Rat ◽  
Receptor Isoforms ◽  
Retinoid Binding Proteins ◽  
Temporal And Spatial

Endogenous retinoids have been implicated in alveologenesis in both the rat and the mouse, and exogenous retinoic acid (RA) can reverse or partially reverse experimental emphysema in adult rat and mouse models by an unknown mechanism. In this study, we examine the cellular and molecular biology of retinoid signaling during alveologenesis in the mouse. We describe the temporal and spatial expression of the retinoid binding proteins CRBP-I, CRBP-II, and CRABP-I using RT-PCR and immunohistochemistry. We identify the retinoic acid receptor isoforms RAR-α1, RAR-β2, RAR-β4, and RAR-γ2 and describe their temporal and spatial expression using RT-PCR and in situ hybridization. We demonstrate that both retinoid binding proteins and RAR isoforms are temporally regulated and found within the alveolar septal regions during alveologenesis. These data support a role of dynamic endogenous RA signaling during alveolar formation.

scholarly journals Retinoic acid response element in the human alcohol dehydrogenase gene ADH3: implications for regulation of retinoic acid synthesis.

1991 ◽  
Vol 11 (3) ◽  
pp. 1638-1646 ◽  
Author(s):  
G Duester ◽  
M L Shean ◽  
M S McBride ◽  
M J Stewart
Keyword(s):  
Retinoic Acid ◽  
Alcohol Dehydrogenase ◽  
Retinoic Acid Receptor ◽  
Acid Synthesis ◽  
Deletion Mapping ◽  
Acid Activation ◽  
Binding Studies ◽  
Human Hepatoma Cells ◽  
Response Element ◽  
Retinoic Acid Response Element

Retinoic acid regulation of one member of the human class I alcohol dehydrogenase (ADH) gene family was demonstrated, suggesting that the retinol dehydrogenase function of ADH may play a regulatory role in the biosynthetic pathway for retinoic acid. Promoter activity of human ADH3, but not ADH1 or ADH2, was shown to be activated by retinoic acid in transient transfection assays of Hep3B human hepatoma cells. Deletion mapping experiments identified a region in the ADH3 promoter located between -328 and -272 bp which confers retinoic acid activation. This region was also demonstrated to confer retinoic acid responsiveness on the ADH1 and ADH2 genes in heterologous promoter fusions. Within a 34-bp stretch, the ADH3 retinoic acid response element (RARE) contains two TGACC motifs and one TGAAC motif, both of which exist in RAREs controlling other genes. A block mutation of the TGACC sequence located at -289 to -285 bp eliminated the retinoic acid response. As assayed by gel shift DNA binding studies, the RARE region (-328 to -272 bp) of ADH3 bound the human retinoic acid receptor beta (RAR beta) and was competed for by DNA containing a RARE present in the gene encoding RAR beta. Since ADH catalyzes the conversion of retinol to retinal, which can be further converted to retinoic acid by aldehyde dehydrogenase, these results suggest that retinoic acid activation of ADH3 constitutes a positive feedback loop regulating retinoic acid synthesis.

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