Characterization of a mutant form of human apolipoprotein B (Thr26-Tyr27del) associated with familial hypobetalipoproteinemia

Angelo Baldassare Cefalu', Davide Noto, Maurizio Averna, Lucia Magnolo, Sebastiano Calandra, Patrizia Tarugi, Zemin Yao

Risultato della ricerca: Articlepeer review

3 Citazioni (Scopus)


We have previously identified a deletion mutant of human apoB [apoB (Thr26-Tyr27del)] in a subject with primary hypobetalipoproteinemia. The present study determined the effect of Thr26-Tyr27del mutation on apoB secretion using transfected McA-RH7777 cells. Transient or stable transfection of apoB-48 containing the Thr26-Tyr27del mutation showed drastically reduced secretion of the mutant as compared to wild-type apoB-48. No lipoproteins containing the mutant apoB-48 were secreted into the medium. Incubation of transfected cells in a lipid-rich medium in the presence of cycloheximide showed rapid turnover of cell-associated mutant apoB-48 as compared to that of wild-type apoB-48. Immunofluorescence experiments showed that the mutant apoB-48 was mostly localized in the endoplasmic reticulum. Treatment with the proteasomal inhibitor MG132 markedly attenuated the turnover of cell-associated mutant apoB-48, whereas treatment with inhibitors of autophagosomal/lysosomal function (e.g. 3-MA or ammonium chloride) had no effect. Taken together, these results indicated that the defective secretion of the Thr26-Tyr27del mutant was associated with increased intracellular degradation of apoB through the proteasome-dependent pathway.
Lingua originaleEnglish
pagine (da-a)371-379
Numero di pagine9
Stato di pubblicazionePublished - 2016

All Science Journal Classification (ASJC) codes

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