SECRETION OF APOLIPOPROTEIN B-CONTAINING LIPOPROTEINS FROM HELA-CELLS IS DEPENDENT ON EXPRESSION OF THE MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN AND IS REGULATED BY LIPID AVAILABILITY

被引:196
作者
GORDON, DA [1 ]
JAMIL, H [1 ]
SHARP, D [1 ]
MULLANEY, D [1 ]
YAO, ZM [1 ]
GREGG, RE [1 ]
WETTERAU, J [1 ]
机构
[1] UNIV ALBERTA, HERITAGE MED RES CTR, LIPID & LIPOPROT RES GRP, EDMONTON T6G 2S2, AB, CANADA
关键词
LIPOPROTEIN ASSEMBLY; LIPOPROTEIN SECRETION; LIPID TRANSFER;
D O I
10.1073/pnas.91.16.7628
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
To elucidate the role of the microsomal triglyceride transfer protein (MTP) in lipoprotein assembly, MTP and apolipoprotein B-53 (apoB 53; the N-terminal 53% of apoB) were expressed in HeLa cells. The results showed that apoB-53 could be expressed in HeLa cells with or without expression of MTP. In contrast, efficient secretion of apoB-53 required expression of MTP. Ultracentrifugal density flotation analysis showed that apoB-53 was secreted predominantly as a particle with the density of high density lipoprotein. An essentially identical apoB-53 particle density distribution was obtained after transient expression of apoB-53 in McArdle RH-7777 rat hepatoma cells. The mass of apoB-53 secreted was greater, and the flotation density was lower, from cells fed lipid, suggesting that apoB secretion in HeLa cells was regulated by lipid availability, similar to what has been described for lipoprotein-producing cell lines. These results indicate that MTP is necessary and sufficient to direct the regulated secretion of apoB-53 in HeLa cells.
引用
收藏
页码:7628 / 7632
页数:5
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