کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5917031 | 1163768 | 2014 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity
ترجمه فارسی عنوان
مولکول شناسایی الگوی فیکلین-1 نشان دهنده اتصال دیفرانسیل به زیرمجموعه های لنفوسیت است، و یک ارتباط جدید بین ایمنی ذاتی و انعطاف پذیر ارائه می دهد
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کلمات کلیدی
mAbFITCGlcNAcflourescein isothiocyanateN-acetyl-d-glucosaminePWMPattern recognition moleculeMASPFCSPRMPBMCsMBLSNAMonoclonal antibody - آنتی بادی مونوکلونالInteraction - اثر متقابلInnate immunity - ایمنی ذاتیadaptive immunity - ایمنی سازگاریFibrinogen-like domain - دامنه فیبریژن مانندfetal calf serum - سرم گوساله جنینperipheral blood mononuclear cells - سلول های تک هسته ای خون محیطیLymphocytes - لنفوسیت هاMannose-binding lectin - لکتین اتصال دهنده مانوزpokeweed mitogen - ماتوژن pokeweedComplement - متممlectin pathway - مسیر لکتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
چکیده انگلیسی
Ficolin-1 is a soluble pattern recognition molecule synthesized by myeloid cells and capable of activating the lectin pathway of complement on the surface of pathogens. It is tethered to the membranes of monocytes and granulocytes; however, the biological significance of cell-associated ficolin-1 is unknown. Recognition of healthy host cells by a pattern recognition molecule constitutes a potential hazard to self cells and tissues, emphasizing the importance of further elucidating the reported self-recognition. In the current study we investigated the potential recognition of lymphocytes by ficolin-1 and demonstrated that CD56dim NK-cells and both CD4+ and CD8+ subsets of activated T-cells were recognized by ficolin-1. In contrast we did not detect binding of ficolin-1 to CD56bright NK-cells, NKT-cells, resting T-cells or B-cells. Furthermore, we showed that the protein-lymphocyte interaction occurred via the pathogen-recognition domain of ficolin-1 to sialic acid on the cell surface. Thus, the differential binding of ficolin-1 to lymphocyte subsets suggests ficolin-1 as a novel link between innate and adaptive immunity. Our results provide new insight about the recognition properties of ficolin-1 and point toward additional immune modulating functions of the molecule besides its role in pathogen recognition.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular Immunology - Volume 57, Issue 2, February 2014, Pages 181-190
Journal: Molecular Immunology - Volume 57, Issue 2, February 2014, Pages 181-190
نویسندگان
Ninette Genster, Ying Jie Ma, Lea Munthe-Fog, Peter Garred,