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.

DOI Web Site 被引用文献2件
  • D A Gordon
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • H Jamil
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • D Sharp
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • D Mullaney
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • Z Yao
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • R E Gregg
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.
  • J Wetterau
    Department of Metabolic Diseases, Bristol-Myers Squibb, Princeton, NJ 08543-4000.

説明

<jats:p>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.</jats:p>

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