کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9102916 | 1152366 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
2â²,5â²-Oligoadenylate size is critical to protect RNase L against proteolytic cleavage in chronic fatigue syndrome
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی بالینی
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![عکس صفحه اول مقاله: 2â²,5â²-Oligoadenylate size is critical to protect RNase L against proteolytic cleavage in chronic fatigue syndrome 2â²,5â²-Oligoadenylate size is critical to protect RNase L against proteolytic cleavage in chronic fatigue syndrome](/preview/png/9102916.png)
چکیده انگلیسی
A dysregulation in the 2â²,5â²-oligoadenylate (2-5A)-dependent RNase L antiviral pathway has been detected in peripheral blood mononuclear cells (PBMC) of chronic fatigue syndrome (CFS) patients, which is characterized by upregulated 2-5A synthetase and RNase L activities, as well as by the presence of a low molecular weight (LMW) 2-5A-binding protein of 37-kDa related to RNase L. This truncated protein has been shown to originate from proteolytic cleavage of the native 83-kDa RNase L by m-calpain and human leukocyte elastase (HLE). We investigated the possible role of 2-5A oligomers in the proteolytic action toward the endonuclease and show that incubation of CFS PBMC extracts with 2-5A trimer and tetramer, but not with the dimer, results in a significant protection of the native 83-kDa RNase L against cleavage by endogenous and purified proteases. Similar results are obtained with a purified recombinant RNase L. An analysis of the size of 2-5A oligomers produced by the catalytic activity of the 2-5A synthetase present in PBMC extracts further shows that samples containing the 37-kDa RNase L preferentially produce 2-5A dimers instead of higher oligomers. Taken together, our results indicate that homodimerization of RNase L by 2-5A oligomers higher than the dimer prevents its cleavage by proteolytic enzymes. The presence of the truncated 37-kDa RNase L in PBMC extracts is therefore likely to result, not only from the abnormal activation of inflammatory proteases, but also from a dysregulation in 2-5A synthetase induction or activation towards the preferential production of 2-5A dimers.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental and Molecular Pathology - Volume 78, Issue 3, June 2005, Pages 239-246
Journal: Experimental and Molecular Pathology - Volume 78, Issue 3, June 2005, Pages 239-246
نویسندگان
Marc Frémont, Karim El Bakkouri, Freya Vaeyens, C. Vincent Herst, Kenny De Meirleir, Patrick Englebienne,