scholarly journals Matthew-Wood Syndrome Is Caused by Truncating Mutations in the Retinol-Binding Protein Receptor Gene STRA6

2007 ◽  
Vol 80 (6) ◽  
pp. 1179-1187 ◽  
Author(s):  
Christelle Golzio ◽  
Jelena Martinovic-Bouriel ◽  
Sophie Thomas ◽  
Soumaya Mougou-Zrelli ◽  
Bettina Grattagliano-Bessières ◽  
...  
Keyword(s):  
Binding Protein ◽  
Receptor Gene ◽  
Retinol Binding Protein ◽  
Protein Receptor

scholarly journals Structural Studies of Retinol-Binding Protein Receptor RBPR2

2018 ◽  
Vol 114 (3) ◽  
pp. 424a
Author(s):  
Jonathan Kim ◽  
Yong Zi Tan ◽  
Brianna Costabile ◽  
Yunting Chen ◽  
Filippo Mancia
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Structural Studies ◽  
Protein Receptor

scholarly journals Mapping the Membrane Topology and Extracellular Ligand Binding Domains of the Retinol Binding Protein Receptor†

Biochemistry ◽  
2008 ◽  
Vol 47 (19) ◽  
pp. 5387-5395 ◽  
Author(s):  
Riki Kawaguchi ◽  
Jiamei Yu ◽  
Patrick Wiita ◽  
Mariam Ter-Stepanian ◽  
Hui Sun
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Membrane Topology ◽  
Retinol Binding Protein ◽  
Binding Domains ◽  
Protein Receptor

scholarly journals Solubilization and purification of the retinol-binding protein receptor from human placental membranes

1994 ◽  
Vol 302 (1) ◽  
pp. 245-251 ◽  
Author(s):  
A Sivaprasadarao ◽  
M Boudjelal ◽  
J B C Findlay
Keyword(s):  
Binding Protein ◽  
Binding Activity ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Sds Page ◽  
Minor Protein ◽  
Membrane Bound ◽  
Placental Membranes ◽  
Poly Ethylene ◽  
Solubilized Form

The membrane receptor for retinol-binding protein (RBP) has been solubilized from human placental brush-border membranes with octyl-beta-glucoside, Nonidet P-40 and CHAPS. A method, based on the preferential precipitation of 125I-RBP-receptor complex with poly(ethylene glycol) 8000, was developed in order to measure the RBP-binding activity in the detergent extracts. The receptor was fairly stable (4 degrees C, 7 days) in octyl-beta-glucoside and Nonidet P-40, but quickly lost activity in CHAPS. The detergent-solubilized form retained all the properties characteristic of the membrane-bound protein, except for a small decrease in affinity for RBP (3- and 7-fold in Nonidet P-40 and octyl-beta-glucoside respectively). The receptor was isolated using recombinant RBP coupled to Reacti-Gel 6X affinity matrix. The purified material contained major and minor protein species of 63 and 55 kDa respectively on SDS/PAGE.

scholarly journals The retinol-binding protein receptor STRA6 regulates diurnal insulin responses

2017 ◽  
Vol 292 (36) ◽  
pp. 15080-15093 ◽  
Author(s):  
Christy M. Gliniak ◽  
J. Mark Brown ◽  
Noa Noy
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Insulin Responses

scholarly journals Cross Talk between Signaling and Vitamin A Transport by the Retinol-Binding Protein Receptor STRA6

2012 ◽  
Vol 32 (15) ◽  
pp. 3164-3175 ◽  
Author(s):  
D. C. Berry ◽  
S. M. O'Byrne ◽  
A. C. Vreeland ◽  
W. S. Blaner ◽  
N. Noy
Keyword(s):  
Vitamin A ◽  
Cross Talk ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Vitamin A Transport

scholarly journals Transthyretin Blocks Retinol Uptake and Cell Signaling by the Holo-Retinol-Binding Protein Receptor STRA6

2012 ◽  
Vol 32 (19) ◽  
pp. 3851-3859 ◽  
Author(s):  
D. C. Berry ◽  
C. M. Croniger ◽  
N. B. Ghyselinck ◽  
N. Noy
Keyword(s):  
Cell Signaling ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor

scholarly journals Tissue distribution of the receptor for plasma retinol-binding protein

1995 ◽  
Vol 305 (2) ◽  
pp. 419-424 ◽  
Author(s):  
S Smeland ◽  
T Bjerknes ◽  
L Malaba ◽  
W Eskild ◽  
K R Norum ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Specific Binding ◽  
Binding Protein ◽  
Cell Types ◽  
Binding Activity ◽  
Retinol Binding Protein ◽  
Scatchard Analysis ◽  
High Binding ◽  
Differentiated Cells ◽  
Protein Receptor

The tissue distribution of the retinol-binding-protein receptor has been studied by using a cell-free binding assay. High binding activity was found in placenta, retina pigment epithelial cells, bone marrow and kidneys. Specific binding activity was also found in the small intestines, spleen and liver, and to a lesser extent in lung. Scatchard analysis revealed that the difference in binding activity was due to variations in receptor level and not affinity changes. When the kidneys were separated into cortex and medulla we found that almost all the specific binding activity present in kidneys was recovered in the cortex. The choroid plexus, an important site in the delivery of nutrients to the cerebrospinal fluid, expressed very high binding activity. The pineal gland, which has been shown to store vitamin A, also showed high binding activity. Testes from immature animals showed higher binding activity than testes from mature rabbits. Cultured undifferentiated kidney keratinocytes showed about 40 times higher binding activity than differentiated cells. Skin fibroblasts demonstrated no binding activity. In conclusion, the data presented in this report show that the level of the retinol-binding-protein receptor varies considerably between cell types. The observed tissue distribution of the receptor agrees well with the present knowledge on retinol function and metabolism by various cells.

scholarly journals A Retinol-Binding Protein Receptor-Mediated Mechanism for Uptake of Vitamin A to Postimplantation Rat Embryos1

1997 ◽  
Vol 57 (4) ◽  
pp. 751-755 ◽  
Author(s):  
Simon J. Ward ◽  
Pierre Chambon ◽  
David E. Ong ◽  
Claes Båvik
Keyword(s):  
Vitamin A ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor
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