Variation in the human ApoB signal peptide modulates ApoB17 translocation

Biochemical and Biophysical Research Communications
F BenhiziaP J Talmud

Abstract

The functional effects of the common 27- or 24-amino-acid (aa) variants in the human apoB signal peptide (SP) on intracellular and secreted apoB17 were investigated in vitro. Only in the presence of oleate was a significant difference in intracellular and secreted SP27-B17 compared to SP24-B17 observed (P = 0.01 and P < 0.0007, respectively), although in the presence or absence of oleate mRNA levels from the two constructs were similar. After fractionation, oleate treatment enhanced microsomal SP27-B17 by 150% (P < 0.0005) with a modest but significant effect on SP24-B17 (32% P = 0.007). Oleate stimulated SP24-B17 accumulation in the nonmicrosomal fraction. The data suggest that the presence of oleate leads to inefficient translocation of the 24-amino-acid signal peptide, possibly resulting in increased retrograde translocation into the cytoplasm and reduced intracellular and secreted levels compared to the "wildtype" 27 aa SP. This implies a direct role of the SP variants in the regulation of apoB intracellular metabolism.

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Citations

Apr 28, 2004·International Journal of Obesity and Related Metabolic Disorders : Journal of the International Association for the Study of Obesity·R JemaaF Fumeron
May 15, 2002·The Journal of Biological Chemistry·Edward A Fisher, Henry N Ginsberg
Jun 9, 2005·The Journal of Biological Chemistry·Philippa J TalmudSteve E Humphries
Mar 5, 2020·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·E S AlvesO T Nóbrega
Oct 1, 2003·Experimental Cell Research·Ai-Bing WangChih-Chuan Liang

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