Mechanism of neutrophil chemiluminescence induced by wheat germ agglutinin: partial characterization of the antigens recognized by wheat germ agglutinin

Journal Article · Thu Nov 01 04:00:00 EST 1984 · Blood; (United States)

OSTI ID:5970682

Ozaki, Y; Iwata, J; Ohashi, T

Wheat germ agglutinin (WGA) stimulated neutrophils to produce significant levels of luminol-dependent chemiluminescence (CL). Since WGA is known to bind N-acetylglucosamine (GlcNAc) oligomers and N-acetylneuraminic acid (NANA), we attempted to determine which binding property of WGA is essential for induction of CL. The succinylated form of WGA (SuWGA), which is no longer able to bind NANA, was still able to induce CL. N-Acetylglucosamine at a concentration of 20 mmol/L almost completely inhibited WGA-induced CL production by neutrophils, whereas bovine submaxillary gland mucin, a potent blocker of NANA binding of WGA, failed to inhibit CL production. Lectins with the GlcNAc-binding property were examined for their ability to induce CL. Those that have higher valences and have a tendency to bind GlcNAc oligomers in the internal portion of glycoconjugates were able to induce CL, whereas those that have low valences and bind terminal GlcNAc of glycoconjugates failed to induce CL even at high concentrations. Attempts were made to characterize the neutrophil membrane proteins recognized by WGA. Glycoproteins with a molecular weight of 25,000 daltons were identified by a 50 mmol/L GlcNAc elution of WGA gels loaded with /sup 125/I-labeled neutrophil membrane proteins. Elution with 500 mumol/L GlcNAc trimer produced several glycoproteins of different molecular weights in addition to the glycoproteins of 25,000 daltons. /sup 125/I-labeled WGA and SuWGA were used for autoradiographic analysis of cell extracts of the neutrophils separated on sodium dodecyl sulfate polyacrylamide gels. WGA recognized multiple glycoproteins of different molecular weights, whereas SuWGA bound only a few of them. Glycoproteins of 25,000 daltons, probably corresponding to those identified by 50 mmol/L GlcNAc elution, were also recognized.

• Research Organization: Univ. of Tokyo, Japan
• OSTI ID: 5970682
• Journal Information: Blood; (United States), Journal Name: Blood; (United States) Vol. 64:5; ISSN BLOOA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AGGLUTININS
ANIMALS
ANTIBODIES
ANTIGEN-ANTIBODY REACTIONS
ANTIGENS
BETA DECAY RADIOISOTOPES
BIOCHEMISTRY
BIOLOGICAL EFFECTS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOHYDRATES
CATTLE
CELL CONSTITUENTS
CELL MEMBRANES
CEREALS
CHEMICAL BONDS
CHEMILUMINESCENCE
CHEMISTRY
DAYS LIVING RADIOISOTOPES
DOMESTIC ANIMALS
ELECTRON CAPTURE RADIOISOTOPES
GLUCOPROTEINS
GRASS
INHIBITION
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LABELLED COMPOUNDS
LECTINS
LEUKOCYTES
LUMINESCENCE
MAMMALS
MATERIALS
MEMBRANES
NEUTROPHILS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PLANTS
PROTEINS
RADIOISOTOPES
RUMINANTS
SACCHARIDES
TRACER TECHNIQUES
VALENCE
VERTEBRATES
WHEAT