Co-expression in rat heart and skeletal muscle of four genes coding for proteins implicated in long-chain fatty acid uptake

被引:37
作者
Van Nieuwenhoven, FA [1 ]
Willemsen, PHM [1 ]
Van der Vusse, GJ [1 ]
Glatz, JFC [1 ]
机构
[1] Maastricht Univ, Cardiovasc Res Inst Maastricht, CARIM, Dept Physiol, NL-6200 MD Maastricht, Netherlands
关键词
membrane transport; sarcolemma; experimental diabetes; development; lipid metabolism;
D O I
10.1016/S1357-2725(98)00122-8
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
It has been suggested that specific membrane-associated and cytoplasmic proteins cooperate in the uptake of long-chain fatty acids by cardiac and skeletal muscle cells. A prerequisite for this hypothesis would be the co-occurrence of these proteins in muscle. Thus, we studied the possible co-expression in rat muscles of the genes coding for the integral membrane proteins fatty acid transport protein (FATP) and fatty acid translocase (FAT), the membrane-associated plasmalemmal fatty acid-binding protein (FABP(pm)) and the cytoplasmic heart-type fatty acid-binding protein (H-FABP(c)). The transcripts of the four proteins were assessed in heart and skeletal muscles of adult Wistar rats, in isolated cells and cell lines from rat heart and also in rat heart during development and upon streptozotocin-induced diabetes. All four genes showed high expression levels in heart, somewhat lower in red skeletal muscle (soleus) and appreciably lower in white skeletal muscle (extensor digitorum longus). FATP, FAT and H-FABP(c) showed a 3- to 5-fold increase in mRNA expression during maturational growth of the heart, while the FABP(pm) expression remained virtually constant. In the heart, streptozotocin-diabetes induced a slight, but statistically not significant, increase in the expression of all four genes. In conclusion, this study shows the co-expression of FATP, FAT, FABP(pm) and H-FABP(c) in rat muscles. This finding supports the possible cooperation of these proteins in the uptake of long-chain fatty acids by muscle cells. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:489 / 498
页数:10
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