کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10738342 | 1046702 | 2011 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Vascular peroxidase-1 is rapidly secreted, circulates in plasma, and supports dityrosine cross-linking reactions
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کلمات کلیدی
VPO1Glycosylated proteinTPOTMBEPORT-PCRLPOPBSHEK293MPO - DFOSDS–PAGE - SDS-PAGEeosinophil peroxidase - ائوزینوفیل پراکسیدازsodium dodecyl sulfate–polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدBiosynthesis - بیوسنتزThyroid peroxidase - تیروئید پراکسیدازFree radicals - رادیکال آزادhuman embryonic kidney 293 cell line - سلول انسانی جنین 293 سلولی استPlasma concentration - غلظت پلاسماLactoperoxidase - لاکتوپروکسیدازPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریmyeloperoxidase - میلوپراکسیداز reverse transcription-polymerase chain reaction - واکنش زنجیره ای رونویسی-پلیمراز معکوس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Members of the peroxidase-cyclooxygenase superfamily catalyze biochemical reactions essential to a broad spectrum of biological processes, including host defense, thyroid hormone biosynthesis, and modification of extracellular matrix, as well as contributing to the pathogenesis of chronic inflammatory diseases. We recently identified a novel member of this family, vascular peroxidase-1 (VPO1), that is highly expressed in the human cardiovascular system. Its biosynthesis and enzymatic properties are largely unknown. Here, we report that VPO1 was rapidly and efficiently secreted into the extracellular space when the gene was stably expressed in human embryonic kidney (HEK) cells. Secreted VPO1 is a monomer with complex N-linked oligosaccharides and exhibits peroxidase activity. Biosynthesis of endogenous VPO1 by cultured human umbilical vein endothelial cells (HUVECs) shares features exhibited by heterologous expression of recombinant VPO1 (rVPO1) in HEK cells. The proinflammatory agents lipopolysaccharide and tumor necrosis factor-α induce expression of VPO1 mRNA and protein in HUVECs. Furthermore, murine and bovine sera and human plasma contain enzymatically active VPO1. rVPO1 exhibits spectral and enzymatic properties characteristic of the peroxidase-cyclooxygenase family, except with regard to its heat stability. rVPO1 catalyzes tyrosyl radical formation and promotes dityrosine cross-linking. Taken together, these data demonstrate that VPO1 is a glycosylated heme peroxidase that is actively secreted into circulating plasma by vascular endothelial cells and shares several features with other members of the peroxidase-cyclooxygenase family, including the catalysis of dityrosine formation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 51, Issue 7, 1 October 2011, Pages 1445-1453
Journal: Free Radical Biology and Medicine - Volume 51, Issue 7, 1 October 2011, Pages 1445-1453
نویسندگان
Guangjie Cheng, Hong Li, Zehong Cao, Xiaoyun Qiu, Sally McCormick, Victor J. Thannickal, William M. Nauseef,