Isolation and characterization of two Korean mistletoe lectins

J Biochem Mol Biol. 2007 Nov 30;40(6):959-65. doi: 10.5483/bmbrep.2007.40.6.959.

Abstract

Two isolectins (KML-IIU and the KML-IIL) were individually isolated from the previously reported Korean mistletoe lectin, KML-C, by using an immunoaffinity column. Molecular weights of the KML-IIU and the KML-IIL were 64 kDa and 60 kDa respectively. Both of the lectins were composed of heterogeneous A and B subunits linked with a disulfide bond, and showed the same carbohydrate-binding specificities for Gal and GalNAc. However, they are different not only in biophysical properties (glycosylation and amino acid compositions) but also bioactivities (cell killing and cytokine induction). The KML-IIL showed 17-145 times stronger in cytotoxicities to various human and mouse cancer cell lines than the KML-IIU. The KML-IIL also induced TNF-alpha secretion from mouse peritoneal macrophages 4.5 times better than the KML-IIU. The results demonstrated isolectins in Korean mistletoe were varied in bioactivities and the KML-IIL may be developed as an anti-cancer agent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Antineoplastic Agents, Phytogenic / chemistry
  • Antineoplastic Agents, Phytogenic / isolation & purification
  • Antineoplastic Agents, Phytogenic / pharmacology
  • Cell Line, Tumor
  • Glycosylation
  • Humans
  • In Vitro Techniques
  • Korea
  • Macrophages, Peritoneal / drug effects
  • Macrophages, Peritoneal / immunology
  • Mice
  • Mice, Inbred BALB C
  • Mistletoe / chemistry*
  • Molecular Weight
  • Plant Preparations / chemistry
  • Plant Preparations / isolation & purification*
  • Plant Preparations / pharmacology
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification*
  • Plant Proteins / pharmacology
  • Protein Subunits
  • Ribosome Inactivating Proteins / chemistry
  • Ribosome Inactivating Proteins / isolation & purification*
  • Ribosome Inactivating Proteins / pharmacology
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological / chemistry
  • Toxins, Biological / isolation & purification*
  • Toxins, Biological / pharmacology
  • Tumor Necrosis Factor-alpha / biosynthesis

Substances

  • Amino Acids
  • Antineoplastic Agents, Phytogenic
  • Plant Preparations
  • Plant Proteins
  • Protein Subunits
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological
  • Tumor Necrosis Factor-alpha
  • mistletoe lectin II
  • Ribosome Inactivating Proteins