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Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease
Retinol binding protein 4 (RBP4) is the specific transport protein of the lipophilic vitamin A, retinol, in blood. Circulating RBP4 originates from the liver. It is secreted by hepatocytes after it has been loaded with retinol and binding to transthyretin (TTR). TTR association prevents renal filtra...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8951293/ https://www.ncbi.nlm.nih.gov/pubmed/35334893 http://dx.doi.org/10.3390/nu14061236 |
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author | Steinhoff, Julia S. Lass, Achim Schupp, Michael |
author_facet | Steinhoff, Julia S. Lass, Achim Schupp, Michael |
author_sort | Steinhoff, Julia S. |
collection | PubMed |
description | Retinol binding protein 4 (RBP4) is the specific transport protein of the lipophilic vitamin A, retinol, in blood. Circulating RBP4 originates from the liver. It is secreted by hepatocytes after it has been loaded with retinol and binding to transthyretin (TTR). TTR association prevents renal filtration due to the formation of a higher molecular weight complex. In the circulation, RBP4 binds to specific membrane receptors, thereby delivering retinol to target cells, rendering liver-secreted RBP4 the major mechanism to distribute hepatic vitamin A stores to extrahepatic tissues. In particular, binding of RBP4 to ‘stimulated by retinoic acid 6’ (STRA6) is required to balance tissue retinoid responses in a highly homeostatic manner. Consequently, defects/mutations in RBP4 can cause a variety of conditions and diseases due to dysregulated retinoid homeostasis and cover embryonic development, vision, metabolism, and cardiovascular diseases. Aside from the effects related to retinol transport, non-canonical functions of RBP4 have also been reported. In this review, we summarize the current knowledge on the regulation and function of RBP4 in health and disease derived from murine models and human mutations. |
format | Online Article Text |
id | pubmed-8951293 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89512932022-03-26 Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease Steinhoff, Julia S. Lass, Achim Schupp, Michael Nutrients Review Retinol binding protein 4 (RBP4) is the specific transport protein of the lipophilic vitamin A, retinol, in blood. Circulating RBP4 originates from the liver. It is secreted by hepatocytes after it has been loaded with retinol and binding to transthyretin (TTR). TTR association prevents renal filtration due to the formation of a higher molecular weight complex. In the circulation, RBP4 binds to specific membrane receptors, thereby delivering retinol to target cells, rendering liver-secreted RBP4 the major mechanism to distribute hepatic vitamin A stores to extrahepatic tissues. In particular, binding of RBP4 to ‘stimulated by retinoic acid 6’ (STRA6) is required to balance tissue retinoid responses in a highly homeostatic manner. Consequently, defects/mutations in RBP4 can cause a variety of conditions and diseases due to dysregulated retinoid homeostasis and cover embryonic development, vision, metabolism, and cardiovascular diseases. Aside from the effects related to retinol transport, non-canonical functions of RBP4 have also been reported. In this review, we summarize the current knowledge on the regulation and function of RBP4 in health and disease derived from murine models and human mutations. MDPI 2022-03-15 /pmc/articles/PMC8951293/ /pubmed/35334893 http://dx.doi.org/10.3390/nu14061236 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Steinhoff, Julia S. Lass, Achim Schupp, Michael Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title | Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title_full | Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title_fullStr | Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title_full_unstemmed | Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title_short | Retinoid Homeostasis and Beyond: How Retinol Binding Protein 4 Contributes to Health and Disease |
title_sort | retinoid homeostasis and beyond: how retinol binding protein 4 contributes to health and disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8951293/ https://www.ncbi.nlm.nih.gov/pubmed/35334893 http://dx.doi.org/10.3390/nu14061236 |
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