Literature DB >> 25123033

Sialylation of Thomsen-Friedenreich antigen is a noninvasive blood-based biomarker for GNE myopathy.

Petcharat Leoyklang1, May Christine Malicdan, Tal Yardeni, Frank Celeste, Carla Ciccone, Xueli Li, Rong Jiang, William A Gahl, Nuria Carrillo-Carrasco, Miao He, Marjan Huizing.   

Abstract

AIM: The exact pathomechanism of GNE myopathy remains elusive, but likely involves aberrant sialylation. We explored sialylation status of blood-based glycans as potential disease markers.
METHODS: We employed immunoblotting, lectin histochemistry and mass spectrometry.
RESULTS: GNE myopathy muscle showed hyposialylation of predominantly O-linked glycans. The O-linked glycome of patients' plasma compared with controls showed increased amounts of desialylated Thomsen-Friedenreich (T)-antigen, and/or decreased amounts of its sialylated form, ST-antigen. Importantly, all patients had increased T/ST ratios compared with controls. These ratios were normalized in a patient treated with intravenous immunoglobulins as a source of sialic acid. DISCUSSION: GNE myopathy clinical trial data will reveal whether T/ST ratios correlate to muscle function.
CONCLUSION: Plasma T/ST ratios are a robust blood-based biomarker for GNE myopathy, and may also help explain the pathology and course of the disease.

Entities:  

Keywords:  L–MS/MS; N-acetylmannosamine (ManNAc); ST-antigen; core 1 O-linked glycan; glycosylation; hereditary inclusion body myopathy; lectin; sialic acid

Mesh:

Substances:

Year:  2014        PMID: 25123033      PMCID: PMC4160177          DOI: 10.2217/bmm.14.2

Source DB:  PubMed          Journal:  Biomark Med        ISSN: 1752-0363            Impact factor:   2.851


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