scholarly journals Localization of retinaldehyde dehydrogenases and retinoid binding proteins to sustentacular cells, glia, Bowman's gland cells, and stroma: Potential sites of retinoic acid synthesis in the postnatal rat olfactory organ

2006 ◽  
Vol 496 (2) ◽  
pp. 149-171 ◽  
Author(s):  
Mary Ann Asson-Batres ◽  
W. Bradford Smith
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Acid Synthesis ◽  
Olfactory Organ ◽  
Gland Cells ◽  
Sustentacular Cells ◽  
Retinoid Binding Proteins

scholarly journals Retinoid-binding proteins in the cerebellum and choroid plexus and their relationship to regionalized retinoic acid synthesis and degradation

1998 ◽  
Vol 257 (2) ◽  
pp. 344-350 ◽  
Author(s):  
Miyuki Yamamoto ◽  
Ursula C. Drager ◽  
David E. Ong ◽  
Peter McCaffery
Keyword(s):  
Retinoic Acid ◽  
Choroid Plexus ◽  
Binding Proteins ◽  
Acid Synthesis ◽  
Retinoid Binding Proteins ◽  
Synthesis And Degradation

Estrogen regulates the expression of retinoic acid synthesis enzymes and binding proteins in mouse skin

2021 ◽  
Author(s):  
Helen B. Everts ◽  
Kathleen A. Silva ◽  
Adriana N. Schmidt ◽  
Susan Opalenikx ◽  
F. Jason Duncan ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Mouse Skin ◽  
Acid Synthesis

scholarly journals Cellular Retinoid Binding Proteins and Retinoic Acid Receptor β are Modulated by Retinoic Acid and Dexamethasone in Postnatal Rat Lung † 1777

1998 ◽  
Vol 43 ◽  
pp. 303-303
Author(s):  
Donna C Whitney ◽  
Gloria D Massaro ◽  
Donald Massaro ◽  
Linda B Clerch
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Retinoic Acid Receptor ◽  
Rat Lung ◽  
Acid Receptor ◽  
Retinoid Binding Proteins

Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids

1999 ◽  
Vol 55 (11) ◽  
pp. 1850-1857 ◽  
Author(s):  
Barnali Neel Chaudhuri ◽  
Gerard J. Kleywegt ◽  
Isabelle Broutin-L'Hermite ◽  
Terese Bergfors ◽  
Hans Senn ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Specific Protein ◽  
Binding Affinities ◽  
Cellular Processes ◽  
Crabp I ◽  
Retinoid Binding Proteins ◽  
Retinoic Acid Binding Proteins ◽  
Crabp Ii ◽  
Kinetics Of

Retinoids play important roles in diverse cellular processes including growth, cell differentiation and vision. Many natural and synthetic retinoids are used as drugs in dermatology and oncology. A large amount of data has been accumulated on the cellular activity of different synthetic retinoids. They are stabilized and transported inside the cell cytoplasm by binding and transport proteins, such as cellular retinol-binding proteins and cellular retinoic acid binding proteins (CRABPs). The structures of human CRABP II in complex with two different synthetic retinoids, Ro13-6307 and Ro12-7310 (at 2.1 and 2.0 Å resolution, respectively) and of bovine CRABP I in complex with a retinobenzoic acid, Am80 (at 2.8 Å resolution) are described. The binding affinities of human CRABP I and II for the retinoids studied here have been determined. All these compounds have comparable binding affinities (nanomolar range) for both CRABPs. Apart from the particular interactions of the carboxylate group of the retinoids with specific protein groups, each structure reveals characteristic interactions. Studying the atomic details of the interaction of retinoids with retinoid-binding proteins facilitates the understanding of the kinetics of retinoid trafficking inside the cytoplasm.

scholarly journals Differential expression of transcripts encoding retinoid binding proteins and retinoic acid receptors during placentation of the mouse

1997 ◽  
Vol 208 (2) ◽  
pp. 199-210 ◽  
Author(s):  
Vincent Sapin ◽  
Simon J. Ward ◽  
Sylviane Bronner ◽  
Pierre Chambon ◽  
Pascal Dollé
Keyword(s):  
Retinoic Acid ◽  
Differential Expression ◽  
Binding Proteins ◽  
Retinoic Acid Receptors ◽  
Retinoid Binding Proteins

Expression of Epithelial Markers and Retinoid-Binding Proteins in Retinol- or Retinoic Acid-Treated Intestinal Cells in Vitro

1993 ◽  
Vol 208 (1) ◽  
pp. 137-147 ◽  
Author(s):  
Michelina Plateroti ◽  
Yula Sambuy ◽  
Fabio Nobili ◽  
Giovanna Bises ◽  
Giuditta Perozzi
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Intestinal Cells ◽  
Epithelial Markers ◽  
Retinoid Binding Proteins

100. Functions of retinoid binding proteins in maintaining retinoic acid homeostasis

1992 ◽  
Vol 46 (5-7) ◽  
pp. 288
Author(s):  
JL Napoli ◽  
PD Fiorella ◽  
MHEM Boerman ◽  
KC Posch
Keyword(s):  
Retinoic Acid ◽  
Binding Proteins ◽  
Retinoid Binding Proteins

Retinoic acid receptors and cellular retinoid binding proteins. III. Their differential transcript distribution during mouse nervous system development

Development ◽  
1993 ◽  
Vol 118 (1) ◽  
pp. 267-282 ◽  
Author(s):  
E. Ruberte ◽  
V. Friederich ◽  
P. Chambon ◽  
G. Morriss-Kay
Keyword(s):  
Nervous System ◽  
Retinoic Acid ◽  
Nuclear Receptors ◽  
Binding Proteins ◽  
Binding Protein ◽  
Retinoic Acid Receptors ◽  
Type I ◽  
Crabp I ◽  
Retinoid Binding Proteins ◽  
Crabp Ii

We have studied the transcript distribution of the retinoic acid receptors (RARs) and the cytoplasmic retinoid binding proteins during embryonic development of the mouse nervous system. Of the three retinoic acid receptors, only RAR-gamma was not expressed in developing neural structures. RAR-beta and RAR-alpha both showed rostral limits of expression in the medulla oblongata equivalent to their patterns of expression in the neuroepithelium of the early hindbrain neural tube. Within their expression domains in the spinal cord and brain, RAR-alpha was ubiquitously expressed, whereas RAR-beta transcripts showed very specific patterns of expression, suggesting that this receptor is involved in mediating retinoic acid-induced gene expression in relation to the development of specific neural structures or pathways. The cytoplasmic binding proteins, cellular retinoic acid binding proteins type I and II (CRABP I and CRABP II) and cellular retinol binding protein type I (CRBP I), were widely distributed in developing neural structures. Their differential spatiotemporal patterns of expression suggest that fine regional control of availability of retinoic acid (RA) to the nuclear receptors plays an important role in organization and differentiation of the nervous system. For instance, expression of CRABP I in the migrating cells that give rise to the olivary and pontine nuclei, which develop abnormally in conditions of retinoid excess, is consistent with observations from a variety of other systems indicating that CRABP I limits the access of RA to the nuclear receptors in normal physiological conditions. Similarly, expression of CRBP I in the choroid plexuses, which develop abnormally in conditions of vitamin A deficiency, is consistent with observations indicating that this binding protein mediates the synthesis of RA in tissues requiring high levels of RA for their normal developmental programme. RAR-beta and CRABP II, which are both RA-inducible, were coexpressed with CRBP I in the choroid plexus and in many other sites, perhaps reflecting the fact that all three genes are RA-inducible. The function of CRABP II is not well understood; its domains of expression showed overlaps with both CRABP I and CRBP I.

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