In vitro assessment of acetic-acid-soluble proteins (glutenin) toxicity in celiac disease

J Biochem Toxicol. 1996;11(4):205-10. doi: 10.1002/(SICI)1522-7146(1996)11:4<205::AID-JBT7>3.0.CO;2-O.

Abstract

Acetic-acid-soluble storage proteins from gluten of the bread wheat cv. Sprint 3 were fractionated by adsorption chromatography on 2000 A controlled-pore glass (CPG) beads, and glutenin polymers with molecular mass higher than 10(7) Da and free from monomeric gliadins were recovered. The glutenin polymers were found to consist of high-molecular-weight (HMW) and low-molecular-weight (LMW) glutenin subunits. Peptic-tryptic (PT) digests of glutenins were examined for their agglutination activity on human myelogenous leukemia K 562(S) cells, agglutination being strongly correlated with toxicity for the celiac intestine. The peptide fraction at a concentration of 1 g/L of culture medium was able to agglutinate 30% of K 562(S) cells, suggesting a moderate toxic effect. This toxicity may be accounted for by homologies in amino acid sequences between glutenin subunits and alpha/beta- and gamma-gliadins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetic Acid / chemistry
  • Adsorption
  • Agglutination Tests
  • Amino Acid Sequence
  • Celiac Disease / metabolism*
  • Celiac Disease / physiopathology
  • Chemical Fractionation
  • Electrophoresis, Polyacrylamide Gel
  • Glass
  • Gliadin / isolation & purification
  • Gliadin / metabolism
  • Glutens / analogs & derivatives*
  • Glutens / chemistry
  • Glutens / metabolism
  • Humans
  • Leukemia, Myeloid / pathology
  • Microspheres
  • Molecular Weight
  • Polymers
  • Porosity
  • Sequence Homology, Amino Acid
  • Triticum / metabolism

Substances

  • Polymers
  • Glutens
  • Gliadin
  • glutenin
  • Acetic Acid