Sialidase occurs in both membranes of the nuclear envelope and hydrolyzes endogenous GD1a

Previous reports indicated the presence of both gangliosides and sialidase in the nuclear envelope (NE) of primary neurons and the NG108-15 neural cell line. GM1, one of the major gangliosides of this membrane, was shown to be tightly associated with a sodium-calcium exchanger in the inner membrane...

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Bibliographic Details
Published in:Journal of neurochemistry 2009-10, Vol.111 (2), p.547-554
Main Authors: Wang, Jianfeng, Wu, Gusheng, Miyagi, Taeko, Lu, Zi-Hua, Ledeen, Robert W
Format: Article
Language:English
Subjects:
Animals
Antibodies - pharmacology
Antibody Specificity
Biochemistry
Blotting, Western
Cell Line, Tumor
Cellular biology
gangliosides
Gangliosides - metabolism
GD1a
Glioma
GM1
Humans
Hybrid Cells
Hydrolysis
Immunohistochemistry
Isoenzymes - immunology
Isoenzymes - metabolism
Membranes
neuraminidase
Neuraminidase - immunology
Neuraminidase - metabolism
Neuroblastoma
Neurology
nuclear envelope
Nuclear Envelope - enzymology
nuclear membrane
Rodentia
sialidase
Sodium
Substrate Specificity
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Summary:Previous reports indicated the presence of both gangliosides and sialidase in the nuclear envelope (NE) of primary neurons and the NG108-15 neural cell line. GM1, one of the major gangliosides of this membrane, was shown to be tightly associated with a sodium-calcium exchanger in the inner membrane of the NE and to potentiate exchanger activity. GD1a was the other major ganglioside detected in the NE and, like GM1, occurs in both inner and outer membranes. A subsequent report indicated the presence of sialidase activity in the NE without specification as to which of the two membranes express it. The present study was undertaken to determine the nature and locus of this activity within the NE of two cell lines: NG108-15 and SH-SY5Y. Western blot analysis of the separated membranes revealed occurrence of Neu3 in the inner membrane and Neu1 in the outer membrane of the NE. Moreover, sialidase activity at both sites was shown capable of catalyzing conversion of endogenous GD1a to GM1.
ISSN:0022-3042
1471-4159
DOI:10.1111/j.1471-4159.2009.06339.x