Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL
USA
Email: bdunn@ufl.edu

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Glycan-Binding Profile and Cell Adhesion Activity of American Bullfrog (Rana catesbeiana) Oocyte Galectin-1

Author(s): Sarkar M.A. Kawsar, Ryo Matsumoto, Yuki Fujii, Hidetaro Yasumitsu, Hideho Uchiyama, Masahiro Hosono, Kazuo Nitta, Jiharu Hamako, Taei Matsui, Noriaki Kojima, Yasuhiro Ozeki.

Abstract:

The glycan-binding profile of a β-galactoside-binding 15 kDa lectin (Galectin-1) purified from the oocytes of the American bullfrog, Rana catesbeiana, was studied using 61 pyridyl-aminated oligosaccharides by frontal affinity chromatography. Human blood type-A-hexasaccharide (GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAcβ1-4Galβ1-4Glc) was found to exhibit the strongest ligand binding to the galectin while Forssman antigen (GalNAcα1-3GalNAcβ1-3Galα1- 4Galβ1-4Glc) and type-A-tetrasaccharide (GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAcβ1-4Glc) were also extensively recognized. The kinetics of affinity of galectin-1 to type-A oligosaccharide was analysed by surface plasmon resonance using neoglycoprotein with type-A oligosaccharides. R. catesbeiana oocyte galectin adhered to human rhabdomyosarcoma cells dose dependently and the activity was specifically cancelled by the neoglycoprotein. It was concluded that galectin-1 from R. catesbeiana oocytes possesses different and rare glycan-binding properties from typical members in galectin family.

Keywords: American bullfrog (Rana catesbeiana), blood type-A hexasaccharide, cell adhesion activity, frontal affinity chromatography, galectin-1

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Article Details

VOLUME: 16
ISSUE: 6
Year: 2009
Page: [677 - 684]
Pages: 8
DOI: 10.2174/092986609788490104
Price: $58