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

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

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 languageEnglish
Pages (from-to)677-684
Number of pages8
JournalProtein and Peptide Letters
Volume16
Issue number6
DOIs
Publication statusPublished - 06-2009

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

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