کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1952863 | 1057235 | 2008 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of endogenous and recombinant human calpain-10
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کلمات کلیدی
ALLNsoluble NSF attachment receptorCalpain-10CAPN10CAPN1DMEDNEAANi-NTANADH dehydrogenase subunit 6ND6PBSTMVNDUFV2SNAP-25SDSTBSSNAREDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده Dulbecconon-essential amino acids - اسید آمینه غیر ضروریTris buffered saline - تریس نمک بافرTnT - تی ان تیsodium dodecyl sulfate - سدیم دودسیل سولفاتUbiquitin-proteasome system - سیستم Ubiquitin-proteasomeProteolytic activity - فعالیت پروتئولیتیکUTR یا untranslated regions - منطقه ترجمه نشدهuntranslated region - منطقه غیر ترجمهTobacco mosaic virus - ویروس موزائیک توتونsynaptosome-associated protein of 25 kDa - پروتئین مرتبط با سیناپتوزوم 25 کیلو دالتونRandom peptide library - کتابخانه پپتیدهای تصادفیUPS - یو پی اس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Calpain-10 is a novel ubiquitous calpain family member that has been implicated as a susceptibility gene for type 2 diabetes. One of the major challenges is that the function of calpain-10 is not yet known. To address this problem, we purified human calpain-10 from different sources, including the endogenous and the recombinant calpain-10 from HeLa S3 and 293F cells, respectively. Both endogenous and recombinant calpain-10 were present as two major forms with different origins. Interestingly, radiolabeled calpain-10 was found to be efficiently cleaved at the N-terminal region by calpain-2, but not by other proteases. None of these calpain-10 proteins have putative proteolytic activity under in vitro conditions when examined using different peptide substrates, including more than 70 in vitro translated, radiolabeled oligopeptides. Our results raise the possibility that calpain-10 may require a special intracellular localization or interacting partner(s) to acquire proteolytic activity, or it functions by interacting with other proteins rather than through its proteolytic activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 90, Issue 9, September 2008, Pages 1362-1371
Journal: Biochimie - Volume 90, Issue 9, September 2008, Pages 1362-1371
نویسندگان
Biao Dong, Rihe Liu,