|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|2166905||1549397||2016||8 صفحه PDF||سفارش دهید||دانلود رایگان|
• MPO is produced by human lymphocytes.
• MPO from human lymphocytes is present in the nucleus and perinuclear region.
• MPO from human lymphocytes is modulated in infection disease.
Myeloperoxidase (MPO) is an important enzyme in the front-line protection against microorganisms. In peripheral blood, it is accepted that MPO is only produced by myeloid-lineage cells. Thus, MPO presence is unexpected in lymphocytes. We showed recently that B1-lymphocytes from mice have MPO. Here, we showed that subsets of human peripheral B, CD4+ and CD8+ T lymphocytes express MPO. The content of MPO in lymphocytes was very low compared to neutrophils/monocytes with a preferential distribution in the nucleus and perinuclear region. Also, we performed a MPO mRNA expression analysis from human blood cells derived from microarray raw data publicly available, showing that MPO is modulated in infectious disease. MPO was increased in CD4+ T lymphocytes from HIV chronic infection and in CD8+ T lymphocytes from HCV-positive patients. Our study points out MPO as a multifunctional protein due to its subcellular localization and expression modulation in lymphocytes indicating alternative unknown functions for MPO in lymphocytes.
Journal: Cellular Immunology - Volume 300, February 2016, Pages 18–25