scholarly journals Retinoid metabolism in human leucocytes

1995 ◽  
Vol 73 (6) ◽  
pp. 889-895 ◽  
Author(s):  
D. Sklan ◽  
S. Trifon ◽  
O. Kedar ◽  
N. Vaisman ◽  
Y. Berner
Keyword(s):  
Retinoic Acid ◽  
Young Children ◽  
Binding Proteins ◽  
Plasma Concentrations ◽  
Protein Fractions ◽  
Retinoid Metabolism ◽  
Retinoid Binding Proteins

Leucocytes from subjects from 0 to 80 years old were separated into mononuclear and granulocyte fractions and the retinoids and retinoid-binding fractions were examined. Both leucocyte ractions were found to contain retinol, retinoic acid and an additional retinoid; retinoic acid Comprised 40% of retinoids in some samples. The protein fractions containing retinoids included a 200 k Da protein and several 14–18 k Da proteins. Plasma concentrations of retinol changed little with increasing age. In contrast, leucocyte concentrations of retinoids and retinoid-binding proteins increased quadratically with age. However, in granulocytes from young children retinoids were almost undetectable.

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.

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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