Vitamin D regulates MerTK-dependent phagocytosis in human myeloid cells
Journal of Immunology, ISSN: 1550-6606, Vol: 205, Issue: 2, Page: 398-406
2020
- 14Citations
- 32Captures
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Metrics Details
- Citations14
- Citation Indexes14
- CrossRef14
- 14
- Captures32
- Readers32
- 32
Article Description
Vitamin D deficiency is a major environmental risk factor for the development of multiple sclerosis. The major circulating metabolite of vitamin D (25-hydroxyvitamin D) is converted to the active form (calcitriol) by the hydroxylase enzyme CYP27B1. In multiple sclerosis lesions, the tyrosine kinase MerTK expressed by myeloid cells regulates phagocytosis of myelin debris and apoptotic cells that can accumulate and inhibit tissue repair and remyelination. In this study, we explored the effect of calcitriol on homeostatic (M-CSF, TGF-β-treated) and proinflammatory (GM-CSF-treated) human monocyte-derived macrophages and microglia using RNA sequencing. Transcriptomic analysis revealed significant calcitriol-mediated effects on both Ag presentation and phagocytosis pathways. Calcitriol downregulated MerTK mRNA and protein expression in both myeloid populations, resulting in reduced capacity of these cells to phagocytose myelin and apoptotic T cells. Proinflammatory myeloid cells expressed high levels of CYP27B1 compared with homeostatic myeloid cells. Only proinflammatory cells in the presence of TNF-α generated calcitriol from 25-hydroxyvitamin D, resulting in repression of MerTK expression and function. This selective production of calcitriol in proinflammatory myeloid cells has the potential to reduce the risk for autoantigen presentation while retaining the phagocytic ability of homeostatic myeloid cells.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85088209320&origin=inward; http://dx.doi.org/10.4049/jimmunol.2000129; http://www.ncbi.nlm.nih.gov/pubmed/32540991; https://journals.aai.org/jimmunol/article/205/2/398/110158/Vitamin-D-Regulates-MerTK-Dependent-Phagocytosis; https://dx.doi.org/10.4049/jimmunol.2000129
Oxford University Press (OUP)
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