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Glycobiology, 2000, Vol. 10, No. 6 551-557
© 2000 Oxford University Press

High-mannose-type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS

Dorota Hoja-Lukowicz1, Dorota Ciolczyk2, Jonas Bergquist3, Anna Lityñska and Piotr Laidler2

Department of Animal Physiology, Institute of Zoology, Jagiellonian University, Ingardena 6, 30–060 Kraków, Poland, 2Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kopernika 7, 31–034 Kraków, Poland, and 3Department of Psychiatry and Neurochemistry, Institute of Clinical Neuroscience, Göteborg University, Sahlgrenska University Hospital/Mölndal, S–431 80 Mölndal, Sweden

Despite numerous studies on arylsulfatase A, the structure of its glycans is not well understood. It has been shown that the concentration of arylsulfatase A increases in the body fluids of patients with some forms of cancer, and the carbohydrate component of arylsulfatase A synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. To understand the significance of any changes in the glycosylation of arylsulfatase A in cancer, it is important to know the structure of its carbohydrate component in normal tissue. In the present study we have analyzed carbohydrate moieties of human placental arylsylfatase A using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE) followed by Western blotting on Immobilon P and on-blot deglycosylation using PNGase F for glycan release. Profiles of N-glycans were obtained by matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). Oligosaccharides were sequenced using specific exoglycosidases, and digestion products were analyzed by MALDI MS and the computer matching of the resulting masses with those derived from a sequence database. Fifty picomoles (6 µg) of arylsulfatase A applied to the gel were sufficient to characterize its oligosaccharide content. The results indicated that human placental arylsulfatase A possesses only high-mannose-type oligosaccharides, of which almost half are core fucosylated. In addition, there was a minor species of high-mannose-type glycan bearing six mannose residues with a core fucose. This structure was not expected since high-mannose-type oligosaccharides basically have not been recognized as a substrate for the {alpha}1,6-fucosyltransferase.

1 To whom correspondence should be addressed


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