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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.