کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9127305 | 1160208 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Overexpression of mouse GlcNAc-1-phosphotransferase-γ subunit in cells induced an I-cell-like phenotype of mucolipidosis
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کلمات کلیدی
PBSM-6-Portho-nitrophenyl-β-d-galactopyranosideGlcNAc-1-phosphotransferaseRFPONPGFCSRT-PCReGFPcDNA - cDNADNA complementary to RNA - DNA مکمل RNALysosomal enzymes - آنزیم های لیزوزومیBase pair(s) - جفت پایه (ها)Curl - حلقهfetal calf serum - سرم گوساله جنینendoplasmic reticulum - شبکه آندوپلاسمی mannose-6-phosphate - مانوز 6-فسفاتPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریProtein sorting - مرتب سازی پروتئینreverse transcription–polymerase chain reaction - واکنش زنجیره ای رونویسی-پلیمراز معکوسenhanced green fluorescence protein - پروتئین فلورسانس سبز افزایش یافته استRed fluorescence protein - پروتئین فلورسانس قرمزGene therapy - ژن درمانیkilobase(s) - کیلو بایت (ها)
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
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چکیده انگلیسی
In a screen of signal peptide-containing proteins from a mouse hypothetical protein library, we identified the mouse UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase-γ chain (GlcNAc-1-phosphotransferase-γ) (GenBank accession no. AAR19081, HYP36 in this study). The mouse GlcNAc-1-phosphotransferase-γ was localized in the Golgi complex in cells and was expressed ubiquitously in mouse tissues, as shown by fluorescence microscope analysis and a semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) assay, respectively. Domain analysis showed that the mouse GlcNAc-1-phosphotransferase-γ had a conserved mannose-6-phosphate (M-6-P)-binding domain. Interestingly, we found that overexpression of the mouse GlcNAc-1-phosphotransferase-γ in fibroblast cell line NIH-3T3 induced accumulation of macromolecules, formation of large cytoplasmic vacuoles and decrease of lysosomal enzymes in cells. This phenotype was reminiscent of inclusion cells (I-cells) that were reported in mucolipidosis diseases caused by abnormal sorting of lysosomal proteins. Transient ectopic expression of GlcNAc-1-phosphotransferase-γ in endoplasmic reticulum (ER) induced lowered lysosomal enzyme activity in cells. These results suggested on one hand that GlcNAc-1-phosphotransferase-γ is an essential subunit of the GlcNAc-1-phosphotransferase, and on the other hand, the molecule might not only recognize the substrates of GlcNAc-1-phosphotransferase, but also the lysosomal proteins with M-6-P residuals.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 347, Issue 1, 28 February 2005, Pages 55-64
Journal: Gene - Volume 347, Issue 1, 28 February 2005, Pages 55-64
نویسندگان
Qiang Sun, Jiang Li, Chunmei Wang, Xiaofeng Huang, Hongyan Huang, Dewei Du, Yingmin Liang, Hua Han,