دورية أكاديمية
Characterization of a mutant form of human apolipoprotein B (Thr26-Tyr27del) associated with familial hypobetalipoproteinemia
| العنوان: | Characterization of a mutant form of human apolipoprotein B (Thr26-Tyr27del) associated with familial hypobetalipoproteinemia |
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| المؤلفون: | Magnolo, L., Calandra, S., Yao, Z., Tarugi, P., NOTO, Davide, CEFALU', Angelo Baldassare, AVERNA, Maurizio |
| المساهمون: | Magnolo, L., Noto, D., Cefalù, A., Averna, M., Calandra, S., Yao, Z., Tarugi, P. |
| بيانات النشر: | Elsevier |
| سنة النشر: | 2016 |
| المجموعة: | IRIS Università degli Studi di Palermo |
| مصطلحات موضوعية: | Apolipoprotein B mutation, Apolipoprotein B-48 secretion, Hypobetalipoproteinemia, Proteasomal degradation, Apolipoprotein B-100, Apolipoprotein B-48, Cell Line, DNA Mutational Analysi, Endoplasmic Reticulum, Genetic Predisposition to Disease, Heterozygote, Human, Phenotype, Proteasome Endopeptidase Complex, Proteasome Inhibitor, Proteolysi, Time Factor, Transfection, Sequence Deletion, Cell Biology, Molecular Biology, Medicine (all), Settore MED/09 - Medicina Interna |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/26825690; info:eu-repo/semantics/altIdentifier/wos/WOS:000371940300011; volume:1861; issue:4; firstpage:371; lastpage:379; numberofpages:9; journal:BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS; http://hdl.handle.net/10447/183598Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84957875292; www.elsevier.com/locate/bbalip |
| DOI: | 10.1016/j.bbalip.2016.01.014 |
| الإتاحة: | https://doi.org/10.1016/j.bbalip.2016.01.014Test http://hdl.handle.net/10447/183598Test |
| حقوق: | info:eu-repo/semantics/closedAccess |
| رقم الانضمام: | edsbas.EC130CD0 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.bbalip.2016.01.014 |
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