| Literature DB >> 26632272 |
Sabrina Sayori Okada1, Edson Mendes de Oliveira1, Tomaz Henrique de Araújo2, Maria Rita Rodrigues3, Renata Chaves Albuquerque1, Renato Arruda Mortara4, Noemi Nosomi Taniwaki5, Helder Imoto Nakaya6, Ana Campa1, Ana Carolina Ramos Moreno7.
Abstract
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.Entities:
Keywords: Electron microscopy; FACS; Fluorescence microscopy; Moonlighting protein; Subcellular localization
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Year: 2015 PMID: 26632272 DOI: 10.1016/j.cellimm.2015.11.003
Source DB: PubMed Journal: Cell Immunol ISSN: 0008-8749 Impact factor: 4.868