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The N-terminal domain of alpha -dystroglycan, released as a 38<ce:hsp sp="0.25"/>kDa protein, is increased in cerebrospinal fluid in patients with Lyme neuroborreliosis

alpha -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 alpha -dystroglycan may be proteolytically processed to generate a small 38kDa protein ( alp...

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Published in:Biochemical and biophysical research communications 2011-09, Vol.412 (3), p.494-499
Main Authors: Hesse, Camilla, Johansson, Inger, Mattsson, Niklas, Bremell, Daniel, Andreasson, Ulf, Halim, Adnan, Anckarsaeter, Rolf, Blennow, Kaj, Anckarsaeter, Henrik, Zetterberg, Henrik, Larson, Goran, Hagberg, Lars, Grahn, Ammi
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Language:English
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Summary:alpha -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 alpha -dystroglycan may be proteolytically processed to generate a small 38kDa protein ( alpha -DG-N). The physiological significance of alpha -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 alpha -DG-N is released into different body fluids, such as lachrimal fluid, cerebrospinal fluid (CSF), urine and plasma. To investigate the significance of alpha -DG-N in CSF we examined the levels of alpha -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 alpha -DG-N compared to healthy controls. After treatment with antibiotics the CSF alpha -DG-N levels were normalized in the LNB patients.
ISSN:0006-291X
DOI:10.1016/j.bbrc.2011.07.129