Isolectins from Solanum tuberosum with Different Detailed Carbohydrate Binding Specificities. Unexpected Recognition of Lactosylceramide by N-Acetyllactosamine-Binding Lectins.

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概要

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• Glycosphingolipid recognition by two isolectins from Solanum tuberosum was compared by the chromatogram binding assay. One lectin (PL-I) was isolated from potato tubers by affinity chromatography, and identified by MALDI-TOF mass spectrometry as a homodimer with a subunit molecular mass of 63, 000. The other (PL-II) was a commer-cial lectin, characterized as two homodimeric isolectins with subunit molecular masses of 52, 000 and 55, 000, respectively. Both lectins recognized N-acetyllactosamine-containing glycosphingolipids, but the fine details of their carbohydrate binding specificities differed. PL-II preferentially bound to glycosphingolipids with N-acetyllactosamine branches, as Gal β4GlcNACβ6 (Galβ4G1cNAcβ3) Galβ4G1cβ1Cer. PL-1 also recognized this glycosphingolipid, but bound equally well to the linear glycosphingolipid Galβ4GlcNAc-β3Galβ4GlcNAcβ3Galβ4Glcβ1Cer. Neolactotetraosylceramide and the B 5 pentaglycosyl-ceramide were also bound by PL-I, while other glycosphingolipids with only one N-ace-tyllactosamine unit were non-binding. Surprisingly, both lectins also bound to lactosyl-ceramide, with an absolute requirement for sphingosine and non-hydroxy fatty acids. The inhibition of binding to both lactosylceramide and N-acetyllactosamine-containing glycosphingolipids by N-acetylchitotetraose suggests that lactosylceramide is also acco-modated within the N-acetylchitotetraose/N-acetyllactosamine-binding sites of the lectins. Through docking of glycosphingolipids onto a three-dimensional model of the PL-1 hevein binding domain, a Galβ4GlcNAcβ3Galβ4 binding epitope was defined. Further-more, direct involvement of the ceramide in the binding of lactosylceramide was sug-gested.

• 社団法人 日本生化学会の論文

著者

• Angstrom Jonas

  Institute Of Medical Biochemistry Goteborg University

• Teneberg Susann

  Institute Of Medical Biochemistry Goteborg University

• Gozia Ofelia

  Institute Of Biochemistry Romanian Academy

• Motas Cecilia

  Institute Of Biochemistry Romanian Academy

• Ciopraga Jeana

  Institute Of Biochemistry Romanian Academy

• Larsson Thomas

  Institute Of Medical Biochemistry Goteborg University

• Karlsson Niclas

  Institute Of Medical Biochemistry Goteborg University

• Bergstrom Jorgen

  Institute Of Medical Biochemistry Goteborg University

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• Isolectins from Solanum tuberosum with Different Detailed Carbohydrate Binding Specificities. Unexpected Recognition of Lactosylceramide by N-Acetyllactosamine-Binding Lectins.

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