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

• 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, Anckarsäter, Rolf, Blennow, Kaj, Anckarsäter, Henrik, Zetterberg, Henrik, Larson, Göran, Hagberg, Lars, Grahn, Ammi
• Format: Article
• Language: English
• Subjects: Annan klinisk medicin; Infectious Medicine; Infektionsmedicin; Other Clinical Medicine; Psychiatry; Psykiatri
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2011.07.129

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.