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NEU1 is more abundant in uveitic retina with concomitant desialylation of retinal cells.
Glycobiology 31, 873-883 (2021)
Verlagsversion
Forschungsdaten
DOI
PMC
Desialylation of cell surface glycoproteins carried out by sialidases affects various immunological processes. However, the role of neuraminidase 1 (NEU1), one of four mammalian sialidases, in inflammation and autoimmune disease is not completely unraveled to date. In this study, we analyzed retinal expression of NEU1 in equine recurrent uveitis (ERU), a spontaneous animal model for autoimmune uveitis. Mass spectrometry revealed significantly higher abundance of NEU1 in retinal Müller glial cells (RMG) of ERU-diseased horses compared to healthy controls. Immunohistochemistry uncovered NEU1 expression along the whole Müller cell body in healthy and uveitic state and confirmed higher abundance in inflamed retina. Müller glial cells are the principal macroglial cells of the retina and play a crucial role in uveitis pathogenesis. To determine whether higher expression levels of NEU1 in uveitic RMG correlate with desialylation of retinal cells, we performed lectin binding assays with sialic acid-specific lectins. Through these experiments we could demonstrate a profound loss of both α2-3- and α2-6-linked terminal sialic acids in uveitis. Hence, we hypothesize that higher abundance of NEU1 in uveitic RMG plays an important role in the pathogenesis of uveitis by desialylation of retinal cells. As RMG become activated in the course of uveitis and actively promote inflammation, we propose that NEU1 might represent a novel activation marker for inflammatory RMG. Our data provide novel insights in the expression and implication of NEU1 in inflammation and autoimmune disease.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Neuraminidase 1 ; Retinal Müller Glia ; Retinal Inflammation ; Sialic Acids ; Spontaneous Autoimmune Disease; Human Lysosomal Neuraminidase; Equine Recurrent Uveitis; Glial-cells; Sialidase; Expression; Lymphocytes; Activation; Requires; Roles
ISSN (print) / ISBN
0959-6658
e-ISSN
1460-2423
Zeitschrift
Glycobiology
Quellenangaben
Band: 31,
Heft: 7,
Seiten: 873-883
Verlag
Oxford Univ Press Inc
Verlagsort
Oxford, UK
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
CF Metabolomics & Proteomics (CF-MPC)
Förderungen
Deutsche Forschungsgemeinschaft