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Molecular & Cellular Proteomics 8:232-244, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Glycosylation Specific for Adhesion Molecules in Epidermis and Its Receptor Revealed by Glycoform-focused Reverse Genomics ^*,S

Rie Uematsu, Yasuro Shinohara^,, Hiroaki Nakagawa, Masaki Kurogochi, Jun-ichi Furukawa, Yoshiaki Miura, Masashi Akiyama^¶, Hiroshi Shimizu^¶ and Shin-Ichiro Nishimura^,||

From the Graduate School of Advanced Life Science, Hokkaido University, Sapporo 001-0021, Japan and ^¶ Department of Dermatology, Hokkaido University Graduate School of Medicine, Sapporo 060-8638 Japan

Glycosylation of proteins greatly affects their structure and function, but traditional genomics and transcriptomics are not able to precisely capture tissue- or species-specific glycosylation patterns. We describe here a novel approach to link different "omics" data based on exhaustive quantitative glycomics of murine dermis and epidermis. We first examined the dermal and epidermal N-glycome of mouse by a recently established glycoblotting technique. We found that the Gal1–3Gal epitope was solely expressed in epidermis tissue and was preferentially attached to adhesion molecules in a glycosylation site-specific manner. Clarified glycomic and protemic information combined with publicly available microarray data sets allowed us to identify galectin-3 as a receptor of Gal1–3Gal epitope. These findings provide mechanistic insight into the causal connection between the genotype and the phenotype seen in 3GalT-1-deficient mice and transgenic mice expressing endo-β-galactosidase C. Because humans do not possess the Gal1–3Gal structure on their tissues, we further examined the human dermal and epidermal N-glycome. Comparative glycomics revealed that the GalNAcβ1–4GlcNAc (N,N'-diacetyllactosediamine) epitope, instead of the Gal1–3Gal epitope, was highly expressed in human epidermis.

^|| To whom correspondence may be addressed: Graduate School of Advanced Life Science, Frontier Research Center for Post-Genomic Science and Technology, Hokkaido University, Sapporo 001-0021, Japan. Tel.: 81-11-706-9043; Fax: 81-11-706-9042; E-mail: shin{at}glyco.sci.hokudai.ac.jp

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