Glycan microarray analysis of P-type lectins reveals distinct phosphomannose glycan recognition. J Biol Chem 2009 Dec 11;284(50):35201-14
Date
10/06/2009Pubmed ID
19801653Pubmed Central ID
PMC2787380DOI
10.1074/jbc.M109.056119Scopus ID
2-s2.0-70349879814 (requires institutional sign-in at Scopus site) 61 CitationsAbstract
The specificity of the cation-independent and -dependent mannose 6-phosphate receptors (CI-MPR and CD-MPR) for high mannose-type N-glycans of defined structure containing zero, one, or two Man-P-GlcNAc phosphodiester or Man-6-P phosphomonoester residues was determined by analysis on a phosphorylated glycan microarray. Amine-activated glycans were covalently printed on N-hydroxysuccinimide-activated glass slides and interrogated with different concentrations of recombinant CD-MPR or soluble CI-MPR. Neither receptor bound to non-phosphorylated glycans. The CD-MPR bound weakly or undetectably to the phosphodiester derivatives, but strongly to the phosphomonoester-containing glycans with the exception of a single Man7GlcNAc2-R isomer that contained a single Man-6-P residue. By contrast, the CI-MPR bound with high affinity to glycans containing either phospho-mono- or -diesters although, like the CD-MPR, it differentially recognized isomers of phosphorylated Man7GlcNAc2-R. This differential recognition of phosphorylated glycans by the CI- and CD-MPRs has implications for understanding the biosynthesis and targeting of lysosomal hydrolases.
Author List
Song X, Lasanajak Y, Olson LJ, Boonen M, Dahms NM, Kornfeld S, Cummings RD, Smith DFAuthors
Nancy M. Dahms PhD Professor in the Biochemistry department at Medical College of WisconsinLinda J. Olson PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnimalsCarbohydrate Conformation
Carbohydrate Sequence
Lectins
Microarray Analysis
Molecular Sequence Data
Oligosaccharides
Phosphorylation
Polysaccharides
Protein Isoforms
Receptor, IGF Type 2
