کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10954478 | 1097906 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Essential role of cytoplasmic sequences for cell-surface sorting of the lectin-like oxidized LDL receptor-1 (LOX-1)
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کلمات کلیدی
PBSGFPoxLDLLOX-1lectin-like oxidized LDL receptor-11,1′-dioctadecyl-3,3,3′,3′-tetramethylindocarbocyanine perchlorate - 1،1'-dioctadecyl-3،3،3 '، 3'-tetramethylindocarbocyanine perchlorateBSA - BSADiI - DIIbovine serum albumin - آلبومین سرم گاوCHO cell - سلول CHOChinese hamster ovary cell - سلول تخمدان هامستر چینیOxidized low-density lipoprotein - لیپوپروتئین با چگالی کم اکسید شدهPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریgreen fluorescent protein - پروتئین فلورسنت سبز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Essential role of cytoplasmic sequences for cell-surface sorting of the lectin-like oxidized LDL receptor-1 (LOX-1) Essential role of cytoplasmic sequences for cell-surface sorting of the lectin-like oxidized LDL receptor-1 (LOX-1)](/preview/png/10954478.png)
چکیده انگلیسی
Lectin-like oxidized LDL receptor-1 (LOX-1) is an oxidized low-density lipoprotein (OxLDL) receptor found in endothelial cells and a member of the natural killer (NK) receptor gene complex. Here, we demonstrate that the ability of LOX-1 binding to OxLDL distinguishes it from other NK receptors. Domain swapping of the lectin-like domain between LOX-1 and the NK cell receptors CD94, NKG2D, and LY-49A demonstrated the crucial role of this domain for recognition of OxLDL by LOX-1, but not for the correct cell-surface sorting of LOX-1. Using LOX-1 GFP fusion constructs, we find that the combination of cytoplasmic and transmembrane domains of LOX-1 is sufficient to target the chimeric protein to the cell-surface. Using N-terminal deletions we determined that the correct cell-surface localization is dependent on a positively charged motif present in the cytosolic juxtamembrane region of LOX-1. Furthermore, the extracellular localization of the LOX-1 C-terminus is disrupted when we mutated the cytoplasmic basic amino acids, Lys-22, Lys-23 and Lys-25 to Glu. Collectively, these results indicate that the N-terminal cytoplasmic domain of LOX-1 determines the correct expression of the lectin domain on the cell-surface.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular and Cellular Cardiology - Volume 39, Issue 3, September 2005, Pages 553-561
Journal: Journal of Molecular and Cellular Cardiology - Volume 39, Issue 3, September 2005, Pages 553-561
نویسندگان
Mingyi Chen, Tatsuya Sawamura,