کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10537072 | 962666 | 2009 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Proteomic profiling of phosphoproteins and glycoproteins responsive to wild-type alpha-synuclein accumulation and aggregation
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کلمات کلیدی
SDSTETIEFPAGEBCAα-SynIMACTBSACNSKP2-DSn1THs - THSα-synuclein - α-سینوکلینbicinchoninic acid assay - آزمون اسید بیستینکونینیکAcetonitrile - استونیتریلFormic acid - اسید فرمیکpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدAlzheimer's disease - بیماری آلزایمرParkinson's disease - بیماری پارکینسونTetracycline - تتراسایکلینTris-buffered saline - تریس بافر شورisoelectric focusing - تمرکز ذره ای الکتریکیThioflavin S - تیوفلاوین Stwo-dimensional - دو بعدیsodium dodecyl sulfate - سدیم دودسیل سولفاتPhosphoprotein - فسفوپروتئینwild-type - نوع وحشیProteomic - پروتئومیکimmobilized metal ion affinity chromatography - کروماتوگرافی جذب یون فلز بی حرکتیGlycoprotein - گلیکوپروتئین
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Proteomic profiling of phosphoproteins and glycoproteins responsive to wild-type alpha-synuclein accumulation and aggregation Proteomic profiling of phosphoproteins and glycoproteins responsive to wild-type alpha-synuclein accumulation and aggregation](/preview/png/10537072.png)
چکیده انگلیسی
A tetracycline inducible transfectant cell line (3D5) capable of producing soluble and sarkosyl-insoluble assemblies of wild-type human alpha-synuclein (α-Syn) upon differentiation with retinoic acid was used to study the impact of α-Syn accumulation on protein phosphorylation and glycosylation. Soluble proteins from 3D5 cells, with or without the induced α-Syn expression were analyzed by two-dimensional gel electrophoresis and staining of gels with dyes that bind to proteins (Sypro ruby), phosphoproteins (Pro-Q diamond) and glycoproteins (Pro-Q emerald). Phosphoproteins were further confirmed by binding to immobilized metal ion affinity column. α-Syn accumulation caused differential phosphorylation and glycosylation of 16 and 12, proteins, respectively, whose identity was revealed by mass spectrometry. These proteins, including HSP90, have diverse biological functions including protein folding, signal transduction, protein degradation and cytoskeletal regulation. Importantly, cells accumulating α-Syn assemblies with different abilities to bind thioflavin S displayed different changes in phosphorylation and glycosylation. Consistent with the cell-based studies, we demonstrated a reduced level of phosphorylated HSP90 α/β in the substantia nigra of subjects with Parkinson's disease as compared to normal controls. Together, the results indicate that α-Syn accumulation causes complex cellular responses, which if persist may compromise cell viability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 211-224
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 211-224
نویسندگان
Jayanarayan Kulathingal, Li-wen Ko, Bernadette Cusack, Shu-Hui Yen,