Glycan-binding profile and cell adhesion activity of american bullfrog (Rana catesbeiana) oocyte galectin-1

Sarkar M.A. Kawsar; Ryo Matsumoto; Yuki Fujii; Hidetaro Yasumitsu; Hideho Uchiyama; Masahiro Hosono; Kazuo Nitta; Jiharu Hamako; Taei Matsui; Noriaki Kojima; Yasuhiro Ozeki

doi:10.2174/092986609788490104

Glycan-binding profile and cell adhesion activity of american bullfrog (Rana catesbeiana) oocyte galectin-1

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

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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.

Original language	English
Pages (from-to)	677-684
Number of pages	8
Journal	Protein and Peptide Letters
Volume	16
Issue number	6
DOIs	https://doi.org/10.2174/092986609788490104
Publication status	Published - 06-2009

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

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title = "Glycan-binding profile and cell adhesion activity of american bullfrog (Rana catesbeiana) oocyte galectin-1",

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.",

author = "Kawsar, {Sarkar M.A.} and Ryo Matsumoto and Yuki Fujii and Hidetaro Yasumitsu and Hideho Uchiyama and Masahiro Hosono and Kazuo Nitta and Jiharu Hamako and Taei Matsui and Noriaki Kojima and Yasuhiro Ozeki",

year = "2009",

month = jun,

doi = "10.2174/092986609788490104",

language = "English",

volume = "16",

pages = "677--684",

journal = "Protein and Peptide Letters",

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T1 - Glycan-binding profile and cell adhesion activity of american bullfrog (Rana catesbeiana) oocyte galectin-1

AU - Kawsar, Sarkar M.A.

AU - Matsumoto, Ryo

AU - Fujii, Yuki

AU - Yasumitsu, Hidetaro

AU - Uchiyama, Hideho

AU - Hosono, Masahiro

AU - Nitta, Kazuo

AU - Hamako, Jiharu

AU - Matsui, Taei

AU - Kojima, Noriaki

AU - Ozeki, Yasuhiro

PY - 2009/6

Y1 - 2009/6

N2 - 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.

AB - 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.

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Glycan-binding profile and cell adhesion activity of american bullfrog (Rana catesbeiana) oocyte galectin-1

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