Origin of α-mannosidase activity in CSF

Anna Tasegian; Silvia Paciotti; Maria Rachele Ceccarini; Michela Codini; Tim Moors; Davide Chiasserini; Elisabetta Albi; Bryan Winchester; Wilma D J van de Berg; Lucilla Parnetti; Tommaso Beccari

doi:10.1016/j.biocel.2017.03.016

Origin of α-mannosidase activity in CSF

Anna Tasegian, Silvia Paciotti, Maria Rachele Ceccarini, Michela Codini, Tim Moors, Davide Chiasserini, Elisabetta Albi, Bryan Winchester, Wilma D J van de Berg, Lucilla Parnetti, Tommaso Beccari

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Pages (from-to)	34-37
Number of pages	4
Journal	International Journal of Biochemistry & Cell Biology
Volume	87
DOIs	https://doi.org/10.1016/j.biocel.2017.03.016
Publication status	Published - Jun 2017

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10.1016/j.biocel.2017.03.016

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@article{a2bcf7393e064a54b92a698b12e46e27,

title = "Origin of α-mannosidase activity in CSF",

abstract = "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.",

keywords = "Frontal Lobe, Humans, Organ Specificity, alpha-Mannosidase, Journal Article",

author = "Anna Tasegian and Silvia Paciotti and Ceccarini, {Maria Rachele} and Michela Codini and Tim Moors and Davide Chiasserini and Elisabetta Albi and Bryan Winchester and {van de Berg}, {Wilma D J} and Lucilla Parnetti and Tommaso Beccari",

year = "2017",

month = jun,

doi = "10.1016/j.biocel.2017.03.016",

language = "English",

volume = "87",

pages = "34--37",

journal = "International Journal of Biochemistry & Cell Biology",

issn = "1357-2725",

publisher = "Elsevier Limited",

}

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.

In: International Journal of Biochemistry & Cell Biology, Vol. 87, 06.2017, p. 34-37.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Origin of α-mannosidase activity in CSF

AU - Tasegian, Anna

AU - Paciotti, Silvia

AU - Ceccarini, Maria Rachele

AU - Codini, Michela

AU - Moors, Tim

AU - Chiasserini, Davide

AU - Albi, Elisabetta

AU - Winchester, Bryan

AU - van de Berg, Wilma D J

AU - Parnetti, Lucilla

AU - Beccari, Tommaso

PY - 2017/6

Y1 - 2017/6

N2 - 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.

AB - 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.

KW - Frontal Lobe

KW - Humans

KW - Organ Specificity

KW - alpha-Mannosidase

KW - Journal Article

UR - http://www.mendeley.com/research/origin-%CE%B1mannosidase-activity-csf

U2 - 10.1016/j.biocel.2017.03.016

DO - 10.1016/j.biocel.2017.03.016

M3 - Article

C2 - 28359775

VL - 87

SP - 34

EP - 37

JO - International Journal of Biochemistry & Cell Biology

JF - International Journal of Biochemistry & Cell Biology

SN - 1357-2725

ER -