کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9886168 | 1537497 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Do clustered β-propeller domains within the N-terminus of LRP1 play a functional role?
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کلمات کلیدی
EGFPAGELDLRHBSSTCALRP1RAPPNGaseFFBSDMEMpeptide: N-glycosidase FPBSα2M - a2mBSA - BSADulbecco's modified Eagle Medium - Eagle Medium اصلاح شده DulbeccoHanks balanced salt solution - Hanks محلول نمک را تعویض می کندα2-macroglobulin - α2-ماگروگلوبولینβ-Propeller - β-پروانهbovine serum albumin - آلبومین سرم گاوtrichloroacetic acid - اسید ترشکلراکتیکpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدEndo H - اندو هendoglycosidase H - اندوگلیکوزیداز HCho - برایChinese Hamster Ovary - تخمدان هامستر چینیfetal bovine serum - سرم جنین گاوendoplasmic reticulum - شبکه آندوپلاسمی epidermal growth factor - عامل رشد اپیدرمیTrafficking - قاچاقPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریReceptor-associated protein - پروتئین مرتبط با گیرندهLow density lipoprotein receptor-related protein 1 - پروتئین مرتبط با گیرنده پروتئینی لیپوپروتئین پایین 1low density lipoprotein receptor - گیرنده لیپوپروتئین چگالی کم
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The six β-propellers located within the N-terminus of low density lipoprotein receptor-related protein 1 (LRP1) are arranged in two clusters that contain two and four β-propellers, respectively. Working with LRP1 deletion mutants, we found that randomly removing large segments of amino acid sequences did not affect the intracellular trafficking of LRP1 as long as the clustered β-propeller domains were retained. However, deletion mutants with crippled β-propeller clusters invariably exhibited retarded exit from the endoplasmic reticulum (ER). To determine potential functions of the clustered β-propellers, we generated a series of deletion mutants in which the β-propellers were systematically removed from the C-terminal end of the second cluster. The resulting minireceptors, designated LRPβ1-6, β1-5, β1-4, β1-3, and β1-2 containing decreasing numbers of the β-propellers, were stably expressed in LRP1-null CHO cells. Binding/degradation assays with receptor-associated protein or α2-macroglobulin showed that removing one or more β-propellers had little effect on binding or degradation of these ligands. However, minireceptors containing odd number of β-propellers (i.e., LRPβ1-3 and β1-5) showed prolonged retention within the ER and remained endoglycosidase H-sensitive, whereas minireceptors containing even number of β-propellers (i.e., LRPβ1-2, β1-4 and β1-6) exited ER at variable rates. Cell surface biotinylation experiments showed that LRPβ1-3 was absent from the cell surface. Prolonged retention of LRPβ1-3 within the ER was accompanied by increased association with molecular chaperone Grp78/Bip. These results suggest that the clustered β-propellers may play a role in folding and intracellular trafficking of LRP1.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1721, Issues 1â3, 18 January 2005, Pages 139-151
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1721, Issues 1â3, 18 January 2005, Pages 139-151
نویسندگان
Fengcheng Sun, Rita Kohen Avramoglu, Gerard Vassiliou, Robert J. Brown, Kerry W.S. Ko, Ruth McPherson, Zemin Yao,