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Origin of α-mannosidase activity in CSF

Tasegian, Anna, Paciotti, Silvia, Ceccarini, Maria Rachele, Codini, Michela, Moors, Tim, Chiasserini, Davide, Albi, Elisabetta, Winchester, Bryan, van de Berg, Wilma D.J., Parnetti, Lucilla, Beccari, Tommaso
The international journal of biochemistry & cell biology 2017 v.87 pp. 34-37
Parkinson disease, alpha-mannosidase, blood-brain barrier, brain, cerebrospinal fluid, chromatography, humans, isozymes, tissues
The α-mannosidase activity in human frontal gyrus, cerebrospinal fluid and plasma has been analyzed by DEAE-cellulose chromatography to investigate the origin of the α-mannosidase activity in cerebrospinal fluid (CSF). The profile of α-mannosidase isoenzymes obtained in CSF was similar to that in the frontal gyrus but different from that in human plasma. In particular the two characteristic peaks of lysosomal α-mannosidase, A and B, which have a pH-optimum of 4.5 and are found in human tissues, were present in both the frontal gyrus and CSF. In contrast the majority of α-mannosidase activity in human plasma was due to the so called intermediate form, which has a pH-optimum of 5.5. The results suggest that the intermediate form of α-mannosidase in plasma does not cross the blood–brain barrier and that the α-mannosidase activity present in the cerebrospinal fluid is of lysosomal type and of brain origin. Thus the α-mannosidase activity in cerebrospinal fluid might mirror the brain pathological changes linked to neurodegenerative disorders such as Parkinson's disease.