Characterisation of tissue-specific oligosaccharides from rat brain and kidney membrane preparations enriched in Na+,K+-ATPase.
The organ-specific nature of the glycosylation of Na+,K+-ATPase-enriched preparations from kidney and brain tissues has earlier been indicated by the use of lectin-staining techniques. Na+,K+-ATPase is ubiquitous and abundant, and subject to upregulation during cell-division and in certain pathological conditions. Lectins specific for the different carbohydrates displayed by the Na+,K+-ATPases may, therefore, be useful carriers/mediators in tissue-specific targeting. N-linked oligosaccharides purified from Na+,K+-ATPase-enriched preparations from rat brain and kidney were consequently characterised in detail in this study using weak anion exchange and normal phase HPLC (combined with serial glycosidase digestions) and matrix-assisted laser desorption/ionisation mass spectrometry. The oligomannose series of glycans were most abundant in the brain tissue preparation and this contrasted with the renal-associated oligosaccharides that were dominated by families of tetra-antennary glycans (with/without a core fucose) with up to four lactosaminylglycan residues in either branched or linear formation.
Clark
R A
RA
Glycobiology Institute, Department of Biochemistry, University of Oxford, UK.
Küster
B
B
Benallal
M
M
Anner
B M
BM
Dwek
R A
RA
Harvey
D J
DJ
Wing
D R
DR
D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism*; D002236:Carbohydrate Conformation; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000378:metabolism; D007668:Kidney / Q000201:enzymology / Q000378:metabolism*; D013058:Mass Spectrometry; D011134:Polysaccharides / Q000737:chemistry; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D011134:Polysaccharides; D006026:Glycoside Hydrolases; D000254:Sodium-Potassium-Exchanging ATPase