TY - JOUR
T1 - Glycan microarray analysis of P-type lectins reveals distinct phosphomannose glycan recognition
AU - Song, Xuezheng
AU - Lasanajak, Yi
AU - Olson, Linda J.
AU - Boonen, Marielle
AU - Dahms, Nancy M.
AU - Kornfeld, Stuart
AU - Cummings, Richard D.
AU - Smith, David F.
PY - 2009/12/11
Y1 - 2009/12/11
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=70349879814&partnerID=8YFLogxK
U2 - 10.1074/jbc.M109.056119
DO - 10.1074/jbc.M109.056119
M3 - Article
C2 - 19801653
AN - SCOPUS:70349879814
SN - 0021-9258
VL - 284
SP - 35201
EP - 35214
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 50
ER -