Vitamin A transport: in vitro models for the study of RBP secretion

被引：36

作者：

Bellovino, D. ^{[1
]}

Apreda, M. ^{[1
]}

Gragnoli, S. ^{[1
]}

Massimi, M. ^{[2
]}

Gaetani, S. ^{[1
]}

机构：

[1] Ist Nazl Ric Alimenti & Nutr, Rome, Italy

[2] Univ Aquila, I-67100 Laquila, Italy

来源：

MOLECULAR ASPECTS OF MEDICINE | 2003年 / 24卷 / 06期

关键词：

Vitamin A; Retinol-binding protein; Hepatic cell lines;

D O I：

10.1016/S0098-2997(03)00037-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Retinol-binding protein (RBP) is the specific plasma carrier of retinol, encharged of the vitamin transport from the liver to target cells. Ligand binding influences the RBP affinity for transthyretin (TTR), a homotetrameric protein involved in the RBP/TTR circulating complex, and the secretion rate of RBP. In fact, in vitamin A deficiency, the RBP release from the hepatocytes dramatically decreases and the protein accumulates in the cells, until retinol is available again. The mechanism is still not clear and new cellular models are needed to understand in detail how the soluble RBP can be retained inside the cell. In fish, a vitamin A transport system similar to that of higher vertebrates is emerging, although with significant differences. (C) 2003 Published by Elsevier Ltd.

引用

页码：411 / 420

页数：10

共 42 条

[1] Transgenic expression in the liver of truncated Met blocks apoptosis and permits immortalization of hepatocytes [J].