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

• 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
• ISSN: 0022-3042; 1471-4159
• DOI: 10.1111/j.1471-4159.2009.06339.x

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.