Investigations concerning vitamin A transport in rheumatic diseases

1982 ◽  
Vol 1 (3) ◽  
pp. 190-193 ◽  
Author(s):  
M. Mezes ◽  
B. Bartosiewicz
Keyword(s):  
Vitamin A ◽  
Rheumatic Diseases ◽  
Vitamin A Transport

Influence of aging on vitamin a transport into the lymphatic circulation

1990 ◽  
Vol 25 (1) ◽  
pp. 61-65 ◽  
Author(s):  
Daniel Hollander ◽  
Violetta Dadufalza
Keyword(s):  
Vitamin A ◽  
Lymphatic Circulation ◽  
Vitamin A Transport

Comparative investigations on vitamin A level of plasma in some rheumatic diseases

1986 ◽  
Vol 5 (2) ◽  
pp. 221-224 ◽  
Author(s):  
M. Mézes ◽  
G. Bartosiewicz ◽  
J. Németh
Keyword(s):  
Vitamin A ◽  
Rheumatic Diseases

scholarly journals Intact vitamin A transport is critical for cold-mediated adipose tissue browning and thermogenesis

2020 ◽  
Vol 42 ◽  
pp. 101088
Author(s):  
Anna Fenzl ◽  
Oana Cristina Kulterer ◽  
Katrin Spirk ◽  
Goran Mitulović ◽  
Rodrig Marculescu ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Vitamin A ◽  
Vitamin A Transport ◽  
Tissue Browning

Plasma vitamin A transport and visual dark adaptation in diseases of the intestine and liver

1978 ◽  
Vol 38 (4) ◽  
pp. 301-308 ◽  
Author(s):  
A. Vahlquist ◽  
K. Sjölund ◽  
Å. Nordén ◽  
P. A. Peterson ◽  
G. Stigmar ◽  
...  
Keyword(s):  
Vitamin A ◽  
Dark Adaptation ◽  
Plasma Vitamin ◽  
Vitamin A Transport

scholarly journals Vitamin A transport in plasma of diabetic patients.

1986 ◽  
Vol 149 (2) ◽  
pp. 133-143 ◽  
Author(s):  
YUTAKA WAKO ◽  
KENICHI SUZUKI ◽  
YOSHIO GOTO ◽  
SHUICHI KIMURA
Keyword(s):  
Vitamin A ◽  
Diabetic Patients ◽  
Vitamin A Transport

Regulation of Vitamin A Transport into Cultured Stellate Cells of Rat Liver: Studies by Anchored Cell Analysis and Sorting System

1993 ◽  
Vol 209 (1) ◽  
pp. 33-37 ◽  
Author(s):  
Tomokazu Matsuura ◽  
Seishi Nagamori ◽  
Satoshi Hasumura ◽  
Hajime Sujino ◽  
Minoru Niiya ◽  
...  
Keyword(s):  
Vitamin A ◽  
Rat Liver ◽  
Stellate Cells ◽  
Cell Analysis ◽  
Sorting System ◽  
Vitamin A Transport

scholarly journals A Functional Binding Domain in the Rbpr2 Receptor is Required for Vitamin A Transport, Ocular Retinoid Homeostasis, and Photoreceptor Cell Survival in Zebrafish

2020 ◽  
Author(s):  
Ashish K. Solanki ◽  
Altaf A Kondkar ◽  
Joseph Fogerty ◽  
Yanhui Su ◽  
Seok-hyung Kim ◽  
...  
Keyword(s):  
Vitamin A ◽  
Cell Survival ◽  
Photoreceptor Cell ◽  
Binding Protein ◽  
Binding Domain ◽  
Human Vision ◽  
Retinol Binding Protein ◽  
Dietary Vitamin ◽  
Binding Residues ◽  
Vitamin A Transport

Dietary vitamin A/all-trans retinol/ROL plays a critical role in human vision. ROL circulates bound to the plasma retinol-binding protein (RBP4) as RBP4-ROL. In the eye, the STRA6 membrane receptor binds to circulatory RBP4 and internalizes ROL. STRA6 is however not expressed in systemic tissues, where there is high-affinity RBP4 binding and ROL uptake. We tested the hypothesis, that the second retinol-binding protein 4 receptor 2 (Rbpr2) which is highly expressed in systemic tissues of zebrafish and mouse, contains a functional RBP4 binding domain, critical for ROL transport. As for STRA6, modeling and docking studies confirmed three conserved RBP4 binding residues in zebrafish Rbpr2. In cell culture studies, disruption of the RBP4 binding residues on Rbpr2 almost completely abolished uptake of exogenous vitamin A. CRISPR generated rbpr2-RBP4 domain zebrafish mutants showed microphthalmia, shorter photoreceptor outer segments, and decreased opsins, that were attributed to impaired ocular retinoid content. Injection of WT-Rbpr2 mRNA into rbpr2 mutant or all-trans retinoic acid treatments rescued the mutant eye phenotypes. In conclusion, zebrafish Rbpr2 contains a putative extracellular RBP4-ROL ligand-binding domain, critical for yolk vitamin A transport to the eye for ocular retinoid production and homeostasis, for photoreceptor cell survival.

scholarly journals A Functional Binding Domain in the Rbpr2 Receptor Is Required for Vitamin A Transport, Ocular Retinoid Homeostasis, and Photoreceptor Cell Survival in Zebrafish

Cells ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 1099
Author(s):  
Ashish K. Solanki ◽  
Altaf A. Kondkar ◽  
Joseph Fogerty ◽  
Yanhui Su ◽  
Seok-Hyung Kim ◽  
...  
Keyword(s):  
Vitamin A ◽  
Cell Survival ◽  
Photoreceptor Cell ◽  
Binding Protein ◽  
Binding Domain ◽  
Human Vision ◽  
Retinol Binding Protein ◽  
Dietary Vitamin ◽  
Binding Residues ◽  
Vitamin A Transport

Dietary vitamin A/all-trans retinol/ROL plays a critical role in human vision. ROL circulates bound to the plasma retinol-binding protein (RBP4) as RBP4-ROL. In the eye, the STRA6 membrane receptor binds to circulatory RBP4 and internalizes ROL. STRA6 is, however, not expressed in systemic tissues, where there is high affinity RBP4 binding and ROL uptake. We tested the hypothesis that the second retinol binding protein 4 receptor 2 (Rbpr2), which is highly expressed in systemic tissues of zebrafish and mouse, contains a functional RBP4 binding domain, critical for ROL transport. As for STRA6, modeling and docking studies confirmed three conserved RBP4 binding residues in zebrafish Rbpr2. In cell culture studies, disruption of the RBP4 binding residues on Rbpr2 almost completely abolished uptake of exogenous vitamin A. CRISPR-generated rbpr2-RBP4 domain zebrafish mutants showed microphthalmia, shorter photoreceptor outer segments, and decreased opsins, which were attributed to impaired ocular retinoid content. Injection of WT-Rbpr2 mRNA into rbpr2 mutant or all-trans retinoic acid treatment rescued the mutant eye phenotypes. In conclusion, zebrafish Rbpr2 contains a putative extracellular RBP4-ROL ligand-binding domain, critical for yolk vitamin A transport to the eye for ocular retinoid production and homeostasis, for photoreceptor cell survival.

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