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The N-terminal domain of α-dystroglycan is released as a 38kDa protein and is increased in cerebrospinal fluid in patients with Lyme neuroborreliosis.

Journal article
Authors Camilla Hesse
Inger Johansson
Niklas Mattsson
Daniel Bremell
Ulf Andreasson
Adnan Halim
Rolf Anckarsäter
Kaj Blennow
Henrik Anckarsäter
Henrik Zetterberg
Göran Larson
Lars Hagberg
Ammi Grahn
Published in Biochemical and biophysical research communications
Volume 412
Issue 3
Pages 494–499
ISSN 1090-2104
Publication year 2011
Published at Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine
Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Institute of Biomedicine, Department of Infectious Medicine
Pages 494–499
Language en
Keywords Dystroglycan; Proteolytic processing; Body fluids; Central nervous system; Neuroborreliosis
Subject categories Clinical chemistry, Psychiatry, Infectious Medicine


α-Dystroglycan is an extracellular adhesion protein that is known to interact with different ligands. The interaction is thought to stabilize the integrity of the plasma membrane. The N-terminal part of α-dystroglycan may be proteolytically processed to generate a small 38kDa protein (α-DG-N). The physiological significance of α-DG-N is unclear but has been suggested to be involved in nerve regeneration and myelination and to function as a potential biomarker for neurodegenerative and neuromuscular diseases. In this report we show that α-DG-N is released into different body fluids, such as lachrimal fluid, cerebrospinal fluid (CSF), urine and plasma. To investigate the significance of α-DG-N in CSF we examined the levels of α-DG-N and known neurodegenerative markers in CSF from patients diagnosed with Lyme neuroborreliosis (LNB) and healthy controls. In untreated acute phase LNB patients, 67% showed a significant increase of CSF α-DG-N compared to healthy controls. After treatment with antibiotics the CSF α-DG-N levels were normalized in the LNB patients.

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