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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 |
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Main Authors: | , , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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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. |
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ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2011.07.129 |