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GRP94 is an ATP-dependent chaperone able to regulate pro-oncogenic signaling pathways. Previous studies have shown a critical role of GRP94 in brain metastasis (BrM) pathogenesis and progression. In this work, an untargeted lipidomic analysis revealed that some lipid species were altered in GRP94-deficient cells, specially GM2 and GM3 gangliosides. The catalytic pathway of GM2 is affected by the low enzymatic activity of β-Hexosaminidase (HexA), responsible for the hydrolysis of GM2 to GM3. Moreover, a deficiency of the GM2-activator protein (GM2-AP), the cofactor of HexA, is observed without alteration of gene expression, indicating a post-transcriptional alteration of GM2-AP in the GRP94-ablated cells. One plausible explanation of these observations is that GM2-AP is a client of GRP94, resulting in defective GM2 catabolic processing and lysosomal accumulation of GM2 in GRP94-ablated cells. Overall, given the role of gangliosides in cell surface dynamics and signaling, their imbalance might be linked to modifications of cell behaviour acquired in BrM progression. This work indicates that GM2-AP could be an important factor in ganglioside balance maintenance. These findings highlight the relevance of GM3 and GM2 gangliosides in BrM and reveal GM2-AP as a promising diagnosis and therapeutic target in BrM research.
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http://dx.doi.org/10.1038/s41598-019-50761-5 | DOI Listing |
Neurol Sci
November 2022
Cytogenetic, medical genetic and reproductive biology department, Hôpital de la Mère et de l'Enfant, CHU Dupuytren, 87042 Limoges, France, Limoges University, CNRS, XLIM, UMR 7252, F-87000, Limoges, France.
AB variant is the rarest form of GM2 gangliosidosis, neurodegenerative diseases caused by lysosomal accumulation of GM2 gangliosides. Less than thirty cases are referenced in the literature, and to date, no late-onset form has been described. Our proband is a 22-year-old male with spinocerebellar ataxia and lower limbs motor deficiency.
View Article and Find Full Text PDFSci Rep
October 2019
Laboratory of Molecular and Translational Oncology, Institut d'Investigacions Biomèdiques August Pi i Sunyer-IDIBAPS, Centre de Recerca Biomèdica CELLEX, Barcelona, E-08036, Spain.
GRP94 is an ATP-dependent chaperone able to regulate pro-oncogenic signaling pathways. Previous studies have shown a critical role of GRP94 in brain metastasis (BrM) pathogenesis and progression. In this work, an untargeted lipidomic analysis revealed that some lipid species were altered in GRP94-deficient cells, specially GM2 and GM3 gangliosides.
View Article and Find Full Text PDFReprod Biol
December 2017
Department of Cellular and Structural Biology, Tulane University School of Medicine, New Orleans, LA 70112, USA.
The GM2-activator protein (GM2-AP), revealed by Li et al. in 1973 in human liver, was initially identified as a protein cofactor that stimulated β-hexosaminidase A to hydrolyze N-acetylgalactosamine from GM2 ganglioside. This cofactor was found to be missing in human variant AB Tay-Sachs disease.
View Article and Find Full Text PDFJ Mol Biol
December 2000
Department of Pharmacology, X-ray Crystallography Laboratory, University of Virginia, Charlottesville, VA 22908-0735, USA.
GM2 activator protein (GM2-AP) belongs to a small group of non- enzymatic lysosomal proteins that act as cofactors in the sequential degradation of gangliosides. It has been postulated that GM2-AP extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-d-galactosamine and conversion to GM3. The high affinity of GM2-AP for GM2 is based on specfic recognition of the oligosaccharide moiety as well as the ceramide lipid tail.
View Article and Find Full Text PDFJ Biol Chem
November 2000
Kekulé Institute for Organic Chemistry and Biochemistry, Gerhard Domagk Strasse 1, 53121 Bonn, Germany.
According to our hypothesis (Fürst, W., and Sandhoff, K. (1992) Biochim.
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