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PubMed1990

Development of wheat-sensitive enteropathy in Irish Setters: morphologic changes.

Morphologic changes in the small intestine were investigated during development of naturally acquired wheat-sensitive enteropathy in Irish Setters. To distinguish underlying morphologic abnormalities from nonspecific effects of intestinal damage, progeny of affected dogs reared on a normal wheat-containing diet were compared with their own littermates reared on a cereal-free diet and with age-matched clinically normal Irish Setters fed the same wheat-containing diet. Peroral jejunal biopsy specimens were taken sequentially between 4 months and 1 year of age. At 4 months of age, there were no differences in villus height, comparing the 3 groups, but increased numbers of intraepithelial lymphocytes and goblet cells were already present in biopsy specimens from the affected Irish Setters fed wheat. Dietary wheat resulted in a progressive reduction in villus height in the jejunum of affected Irish Setters from 6 months onward. Underlying morphologic abnormalities were not found, and the characteristic morphologic changes of this enteropathy were secondary to the presence of dietary wheat. However, development of partial villus atrophy was preceded by increased numbers of intraepithelial lymphocytes and goblet cells.

Age Factors↗

PubMed1983

Enhancement of rat colon carcinogenesis by wheat bran consumption during the stage of 1,2-dimethylhydrazine administration.

The effect on intestinal carcinogenesis of feeding a 20% wheat bran dietary supplement, either during and/or after the stage of carcinogen administration with 1,2-dimethylhydrazine, was examined in 48 male Sprague-Dawley rats fed defined diets for 31 weeks. Nutrient intake and body weight gain were equivalent in all groups of animals. In the rats fed bran during carcinogen administration, tumor yield was significantly greater. Benign and malignant tumors increased by 3.4-fold (p less than 0.005), adenomas by 3.5-fold (p less than 0.025), and adenocarcinomas by 3.25-fold (p less than 0.05) over the yield found in the group fed a fiber-free diet. Consumption of wheat bran, after completion of carcinogen exposure, reduced the yield of benign adenomas by 71.4% when compared with the group fed the fiber-free diet (p less than 0.025). Those rats fed a wheat bran supplement during carcinogen administration and then switched to a fiber-free diet afterwards had the highest tumor yield, 4.5 times as many benign and malignant tumors as in those rats consistently fed the fiber-free diet (p less than 0.05) and at least 6 times as many adenomas as any of the other dietary groups (p less than 0.05). These results demonstrate that dietary wheat bran, a fiber which produces a hyperproliferative response in the colon, significantly increases colon carcinogenesis when fed to rats during the stage of carcinogen administration. This effect appears to be further enhanced when the wheat bran is totally removed from the diet following the stage of carcinogen administration. These data indicate that the hyperproliferative effects of wheat bran appear to outweigh any preventive actions that bran may have on colon carcinogenesis by altering the bulk of intestinal contents and their transit time through the bowel.

1,2-Dimethylhydrazine↗

PubMed1978

Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents.

Plant lectins are known to have potent biological actions of normal and malignant cells. High concentrations of these lectins are present in many types of high residue diets. The specific binding of wheat germ agglutinin, a dietary plant lectin, to N-acetylglucosamine was used as the basis for purification of this lectin by biospecific chitin affinity chromatography. Subsequently, methods were developed for the extraction, purification, and identification of wheat germ agglutinin from fecal samples. Biologically intact wheat germ agglutinin was detected in ileostomy effluent and fecal collections from human subjects consuming a diet containing wheat germ. These studies demonstrate that wheat germ agglutinin can traverse the human small intestine intact. It is feasible that orally ingested wheat germ agglutinin and other plant lectins which interact with a wide variety of cell membranes may alter intestinal epithelial or bacterial cell function in the human bowel.

Feces↗

PubMed1982

Studies on an endogenous substrate of wheat germ protein kinase.

An endogenous phosphoryl acceptor has been purified 138-fold from wheat germ extracts. This protein, termed T-substrate, is far more effective than casein or phosvitin as a phosphoryl acceptor for a wheat germ kinase recently purified by our laboratory. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicates that the T-substrate preparation is not homogeneous. The T-substrate, which migrates at a Mr = 48,000, constitutes about 90% of the total protein stain on the gel and is the only protein component which is phosphorylated by the wheat germ kinase. The hydrodynamic properties of the T-substrate have been determined by gel filtration and glycerol density gradient centrifugation. The protein exhibits a Stokes radius of 65.5 A, a sedimentation coefficient of 3.85 S, a frictional ratio of 2.11, and a molecular weight of approximately 104,000. The results suggest that the wheat germ T-substrate is a dimer. The protein exhibits a greater substrate specificity for the wheat germ kinase than for the cyclic AMP-dependent and several independent protein kinases isolated from rabbit skeletal muscle and human erythrocytes. The T-substrate can be maximally phosphorylated by the wheat germ kinase to the extent of about 8 mol of phosphate/48,000 g of protein. Complete dephosphorylation of the phospho-T-substrate occurred upon treatment with phosphatases. The phosphorylated amino acid was identified by high voltage electrophoresis of an acid hydrolysate of 32P-T-substrate. The results indicate that phosphorylation occurs mainly on the seryl residues of T-substrate.

Animals↗

PubMed1981

Gas chromatography with electron capture and mass spectrometric detection of deoxynivalenol in wheat and other grains.

A method for determining deoxynivalenol (DON) in wheat has been developed in conjunction with an assessment of contamination in Canada. The sample is extracted with methanol-water; the extract is treated with 30% aqueous ammonium sulfate solution and extracted with 4 portions of ethyl acetate. After further cleanup by column chromatography, the sample extract is derivatized with N-heptafluorobutyrylimidazole, and the DON tris-heptafluorobutyrate is determined by gas-liquid chromatography with electron capture detection. Mass spectrometric single ion monitoring at m/z 884 is used for confirmation. Detection limits are less than or equal to 0.01 microgram DON/g and recoveries from wheat, using the proposed method, averaged 72 and 80% in 2 different laboratories, with coefficients of variation of 10.2 and 10.0%, respectively. The method is also applicable to determining DON in barley and corn and T-2 toxin in wheat. Virtually 100% contamination by DON of the 1980 Ontario white winter wheat and Quebec red spring wheat crops was found, based on 72 analyses made in this laboratory, but western Canadian wheat contained little or no DON.

Edible Grain↗

PubMedDate not supplied

Determination of deoxynivalenol in 1991 U.S. winter and spring wheat by high-performance thin-layer chromatography.

A thin-layer chromatographic (TLC) method was modified for determination of deoxynivalenol (DON) in 1991 U.S. winter and spring wheat. After extraction with acetonitrile-water (84 + 16) and cleanup on a charcoal-alumina-Celite (7 + 5 + 3) column, acetonitrile was used instead of ethyl acetate to transfer the concentrated extract containing DON. After the extract was evaporated to dryness, the residue was dissolved in methanol and an aliquot was spotted on a high-performance TLC plate. After development with chloroform-acetone-2-propanol (8 + 1 + 1), the plates were sprayed with aluminum chloride solution and heated; DON was quantitated by fluorodensitometry. Average recoveries of DON added to duplicate test portions of wheat at 200, 400, and 800 ng/g were 83, 82, and 72%, respectively. The detection limit was 40 ng/g. The method was applied to 81 test samples of spring and winter wheat. The wheat contained DON levels that ranged from nondetectable to 9330 ng/g (average 1570 ng/g). The results indicate that DON levels were higher in wheat from Missouri, North Dakota, and Tennessee than in wheat from 7 other states. The identity of DON, which was isolated from 21 of the extracts by preparatory TLC, was confirmed by gas chromatography/mass spectrometry in all 21 test samples.

Chromatography, High Pressure Liquid↗

PubMed1997

[Selenium content in wheat and rye flow from Russia, cis nations and Baltic countries].

Selenium concentrations in wheat and rhy flour of Russia and CSC vary from 46 to 577 mg/kg and from 6 to 87 mg/kg correspondingly. The highest wheat flour selenium--300-600 mg/kg--is typical to wheat, imported from USA and Canada. Low values of selenium wheat flour (34-64 mg/kg) and of selenium rhy flour (5-20 mg/kg) from Kaliningrad, Novgorod, Pskov, Leningrad regions, Altay, Byelorussia and Baltic countries show the possibility of low selenium consumption by the population of these regions. Low selenium is demonstrated for wheat flour imported to Kirghizia - 81 +/- 31 mg/kg and produced in north-western part of Ukrain: Volinsk, Sumi, Kiev regions--64-78 mg Se/kg. Sakhalin and selenium-deficient Buryatia utilize predominently imported wheat flour with high selenium content - 250-260 mg/kg. Native grain with relatively high selenium is found in Kurgan, Orenburg, Lipetsk, Tambov regions, Tataria and Uzbekistan - 160-185 mg/kg.

Baltic States↗

PubMed1998

Accumulation of cadmium from wheat bran, sugar-beet fibre, carrots and cadmium chloride in the liver and kidneys of mice.

The gastrointestinal absorption and organ distribution of Cd after exposure for 9 weeks to three fibre-rich foodstuffs (wheat bran, sugar-beet fibre and carrots) were determined in mice. Groups of eight mice were given a diet containing 0.05 mg Cd/kg from wheat bran, sugar-beet fibre, carrots or CdCl2 mixed in a semi-synthetic, low-Cd (< 0.007 mg/kg) feed. A control group was fed on the low-Cd semi-synthetic feed. The water consumption, food consumption and the weight of the animals were monitored throughout the study. The feed was changed once weekly and Cd was analysed in the feed at each change. myo-Inositol phosphates (hexa-, penta-, tetra- and tri-) and Zn, Cu, Fe and Ca were also analysed in the diets. After 9 weeks, the mice were killed and liver and kidneys were sampled and analysed for Cd. The group receiving the wheat-bran diet had significantly lower fractional Cd accumulation (% total Cd intake) in the liver and kidneys than the other groups, indicating a lower fractional absorption of Cd. The wheat-bran diet had markedly higher levels of inositol hexa- and pentaphosphates (phytates) and a Zn level that was twice as high as those in the other diets. The higher levels of myo-inositol hexa- and pentaphosphates in the wheat-bran diet most probably contributed more to the lower fractional absorption of Cd than the elevated Zn level, due to the formation of insoluble Cd-phytate complexes. Compared with the wheat-bran diet, the sugar-beet-fibre and carrot diets contained very low levels of myo-inositol penta- and hexaphosphates, and consequently the fractional Cd absorption from these diets was higher.

Animals↗

PubMed1998

High plains disease of corn and wheat: ultrastructural and serological aspects.

Virus-like particles with unique size and morphology were consistently associated with a new eriophyid mite-borne disease of maize and wheat, the high plains disease. In cells of symptomatic leaves, double membrane-bound particles (DMPs), quasi-spherical structures 120-200 nm in diameter, were present throughout the cytoplasm in association with electron-dense amorphous inclusions. No DMPs and inclusions were observed in symptomless plants. The DMPs were morphologically indistinguishable from those associated with eriophyid mite-borne diseases of uncertain etiology: fig mosaic, rose rosette, yellow ringspot of redbud, thistle mosaic, wheat spot chlorosis and wheat spot mosaic diseases. The DMPs and associated viroplasm-like inclusions in maize and wheat were specifically immunogold labeled in situ with an antiserum to the 32 kDa protein associated specifically with the high plains disease. Thread-like structures, present in the purified preparations from diseased maize were also immunogold labeled with the antiserum. It is suggested that the thread-like structures are derived from the DMPs. In many cells of symptomatic maize and wheat samples, DMPs occurred together with flexuous rod-shaped particles and cylindrical inclusions of wheat streak mosaic potyvirus (WSMV), indicating that these cells are infected doubly with WSMV and the agent represented by the DMPs.

Immunohistochemistry↗

PubMed1986

A quantitative electron microscopic study of the intracellular localization of wheat germ agglutinin in retinal neurons.

Previous work has established that, following endocytosis, wheat germ agglutinin, like a number of other plasma membrane bound ligands, is transported to the Golgi apparatus-complex. Previous studies that provided qualitative information about the intracellular distribution of internalized wheat germ agglutinin used techniques that precluded any quantitative conclusions about the relative magnitude of the labeling of endosomes, lysosomes, and the Golgi apparatus-complex. Using quantitative ultrastructural autoradiography, this study compares the time course and relative magnitude of labeling of various intracellular compartments to the labeling in the Golgi area. Fifteen minutes after intraocular injection, wheat germ agglutinin is confined to the inner surface of the retina and the immediate subsurface neuropil with little labeling of the retinal ganglion cell perikarya. Thirty minutes after injection, the plasma membrane (6.97 +/- 1.17), endosomes (10.27 +/- 3.98), smooth vesicles and tubules (1.94 +/- 1.66), and lysosomes (2.42 +/- 1.21) of the retinal ganglion cells are labeled, while the Golgi apparatus-complex is not labeled (0.29 +/- 0.25). (Figures in parentheses are the calculated relative radioactive source density +/- the standard deviation.) The relative labeling density of the plasma membrane and endosomes decreases somewhat during the next 90 minutes (plasma membrane, 4.76 +/- 0.67; endosomes, 7.23 +/- 2.02), while the labeling density of smooth vesicles and tubules and of lysosomes rises (smooth vesicles and tubules, 5.56 +/- 0.94; lysosomes, 7.76 +/- 1.56). The Golgi apparatus-complex, which is unlabeled at 30 minutes, is weakly labeled at 2 hours (1.26 +/- 0.28). The fact that the lysosomes are already labeled at 30 minutes while the Golgi apparatus-complex is unlabeled at that time indicates that the transport of wheat germ agglutinin to the Golgi apparatus-complex is a relatively late phenomenon, and suggests that the bulk of the wheat germ agglutinin destined for lysosomes does not pass through the Golgi apparatus-complex.

Animals↗

PubMed1991

Localization of wheat germ agglutinin and antibody binding sites on the plasma membranes of sea urchin sperm heads as revealed by label-fracture and fracture-flip.

Freeze-fracture electron microscopy reveals that intramembrane particles are concentrated in a band encircling the posterior portion of the acrosome of Strongylocentrotus purpuratus sperm. Two colloidal gold labeling methods, label-fracture and replica-staining fracture-flip, were employed to show that the plant lectin wheat germ agglutinin, which recognizes a 210 kDa sperm surface glycoprotein, binds to this localized band of intramembrane particles. Monoclonal antibody J18/2, which also recognizes the 210 kDa surface glycoprotein, shows this localized binding in approximately 20% of the sperm observed in this study. The majority of sperm displayed a uniform distribution of receptor sites for monoclonal antibody J18/2. Since wheat germ agglutinin and monoclonal antibody J18/2 are known to agglutinate Strongylocentrotus purpuratus sperm but not sperm of another sea urchin, Lytechinus pictus, similar determinations were made for the latter species. Lytechinus pictus sperm are not labeled with wheat germ agglutinin and are only sparsely labeled with monoclonal antibody J18/2. The acrosomal localizations of wheat germ agglutinin and monoclonal antibody J18/2 receptors in Strongylocentrotus purpuratus sperm are consistent with the involvement of the 210 kDa surface glycoprotein in an egg jelly-induced sperm acrosome reaction. Low-temperature post-embed labeling of thin sections with wheat germ agglutinin and monoclonal antibody J18/2 show concentrations of label within the acrosomal vesicle of Strongylocentrotus purpuratus sperm, suggesting the presence of an intracellular storage site for the 210 kDa glycoprotein.

Animals↗

PubMed2025

Hyperspectral imaging of grains uncovers the genetic architecture of nitrogen response of development in bread wheat.

UNLABELLED: Unraveling the genetic architecture of nitrogen response of development is critical for improving wheat productivity while reducing nitrogen inputs. In this study, hyperspectral imaging (HSI) was applied to wheat grains obtained from nitrogen-deficient and normal conditions, combined with genome-wide association studies (GWAS), to investigate the nitrogen response of development in a diverse wheat panel. The 1,792 i-traits were acquired via hyperspectral imaging system, which reflect detailed phenotypic assessments of wheat development, capturing subtle variations in nitrogen response. A total of 3,556 significant loci and 3,648 candidate genes were identified. Key candidate genes involved in nitrogen uptake and utilization were identified by integrating agronomic traits with i-traits, including TaARE1-7A, TaPTR9-7B, TaNAR2.1, and Rht-B1. This approach underscores the potential of combining HSI on grains with GWAS to dissect complex traits like nitrogen response, offering valuable genetic insights for breeding nitrogen-efficient wheat varieties and enhancing sustainability in crop production. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s11032-025-01609-6.

Bread wheat↗

PubMed1984

Agglutinating activity of gliadin-derived peptides from bread wheat: implications for coeliac disease pathogenesis.

The PT-digest of bread wheat gliadin was very active in agglutinating undifferentiated human K562(S) cells. This activity was quantitatively, but not qualitatively, similar to that of Con A or WGA. Moreover, Con A-induced cell agglutination was inhibited by mannan and mannose, WGA-induced agglutination by NAG only, and cell agglutination induced by bread wheat gliadin peptides was inhibited by each of these three saccharides. Not only was mannan the most active saccharide in preventing cell agglutination induced by bread wheat gliadin peptides, but it was also able to dissociate agglutinated cells. As compared to the PT- digest of whole bread wheat gliadin, the digest obtained from purified A-gliadin was tenfold more active. The PT-digest of durum wheat gliadin did not show any agglutinating activity.

Agglutination Tests↗

PubMed1981

The effects of wheat germ agglutinin on the adipocyte insulin receptor.

Treatment of rat adipocytes with wheat germ agglutinin markedly enhances insulin binding by increasing the affinity of the insulin receptor. The structure of adipocyte receptor following wheat germ agglutinin treatment was studied by column chromatography and polyacrylamide gel electrophoresis to determine if aggregates of the insulin receptor are present. Solubilization of the receptor by Triton X-100 and passage of this material over Sepharose 6B revealed two insulin binding activities: a major peak which had a Strokes radius of 87 A and a minor peak with a Strokes radius of 47 A. Wheat germ agglutinin treatment produced an increase in the binding activity of both peaks, but their molecular weights did not change. In addition, 125I-labeled insulin was covalently attached to the adipocyte insulin binding sites by a cross-linking reagent. Column chromatography of the insulin-receptor complex again indicated the presence of two species with Strokes radii of 87 A and 47 A. Heterogeneity in these complexes was also demonstrated by polyacrylamide gel electrophoresis in the presence of Triton X-100. Ferguson plots indicated that the peak of radioactivity had a molecular radius of 60 A, a size found both in the presence and absence of wheat germ treatment of adipocytes. These findings suggest that the increase in receptor affinity produced by wheat germ agglutinin treatment is not caused by the formation of receptor clusters. Instead, it appears that a simple interaction between the plant lectin and the receptor is sufficient to induce the changes in the insulin binding properties of adipocytes.

Adipose Tissue↗

PubMed1982

Effects of N-acetylglucosamine and platelet inhibitors on the synergistic interaction of platelets and aggregating agents in the presence of wheat germ agglutinin.

Low concentrations of wheat germ agglutinin (4 micrograms/ml) have been shown to act synergistically to induce platelet aggregation with epinephrine, collagen, arachidonate and ionophore A23187. Aggregation ceased on the addition of the haptenic sugar N-acetylglucosamine at any time following the onset of aggregation with these agonists and a small degree of disaggregation was observed during the reversible first wave with the biphasic aggregating agents epinephrine and ADP. Cyclooxygenase inhibitors such as indomethacin and aspirin blocked the second wave of aggregation with the biphasic aggregating agents epinephrine and ADP but a synergistic response continued to be shown with the first wave in the presence of these inhibitors. Release of [14C]serotonin and the mobilization of [3H]arachidonate by epinephrine and collagen were markedly stimulated in the presence of wheat germ agglutinin but there was no increase of either radiolabel in the case of ADP. Platelet shape change, but not aggregation, occurred with low levels of wheat germ agglutinin and the synergistic response with ADP, collagen or ionophore A23187 occurred without further shape change. Wheat germ agglutinin did not affect the basal or stimulated levels of cyclic AMP. The membrane fluidity of platelets was not affected by the lectin or by thrombin as shown by the lack of change in fluorescence polarization with diphenylhexatriene. It is suggested that the binding of wheat germ agglutinin to the platelet surface induces platelet activation by mechanisms similar to those of other agonists and that it may affect the distribution of membrane-bound Ca2+ by a reversible perturbation of the platelet membrane.

Acetylglucosamine↗

PubMed1986

Isolated erythroglycans have a high-affinity interaction with wheat germ agglutinin but are poorly accessible in situ.

The sugar and cell specificities of wheat germ agglutinin have been studied extensively. In particular, it is well established that wheat germ agglutinin will interact with highly sialylated glycoconjugates of the type carried by the erythrocyte glycoprotein, glycophorin (Adair, W.L. and Kornfeld, S. (1974) J. Biol. Chem. 249, 4696-4704). We have found that polylactosamines isolated from adult and fetal erythrocytes can have a high-affinity interaction with immobilized wheat germ agglutinin. In fact, this interaction is much stronger than the sialic acid-dependent interaction. Using flow microfluorimetry in conjunction with various serological and enzymatic pretreatments, we have measured the extent to which polylactosamines contribute to wheat germ agglutinin binding. We have found that most of the neuraminidase-resistant receptors on erythrocytes are polylactosamine in nature. However, this residual binding of wheat germ agglutinin to neuraminidase-treated erythrocytes is of much lower apparent affinity than the sialic acid-dependent interaction. The lower reactivity of polylactosamines at the erythrocyte surface suggests that these large glycans are actually poorly accessible.

Adult↗

PubMed1986

Characteristics of two wheat germ agglutinin-resistant variants of B16 mouse melanoma cells with reduced tumorigenicity.

Two variants of B16 mouse melanoma cells, selected for their resistance to toxic levels of wheat germ agglutinin isolectin 1 (WGA-1) in serum-free medium, showed by chromosome analysis that they are still mouse cell-lines, continue to produce melanin, and are less tumorigenic in mice than the parent B16 cells. The variants showed a marked decrease in cell agglutination with the wheat germ lectin and a slight increase in cell agglutination with concanavalin A. The binding of 125I-labeled wheat germ agglutinin to the two variant lines was likewise decreased over a 10(3)-fold range of lectin concentrations. Terminal sialyl residues were critical in WGA-1 binding to the wild-type cells. The binding data indicated a decrease in high-affinity binding as well as a decrease in the total number of binding sites in the variants. Polyacrylamide gel electrophoresis, followed by affinity staining with 125I-wheat germ agglutinin, showed alterations in the wheat germ agglutinin-binding glycoproteins in the variants compared to those of the parent cell line. However, lactoperoxidase-catalyzed iodination revealed a similar cell-surface protein pattern among the three cell lines. Radioactive glycoproteins secreted or shed by the three cell lines grown in the presence of [3H]glucosamine in serum-free medium were fractionated on the basis of their interaction with WGA-Sepharose (2 mg/mL). The WGA-bound glycoproteins from the two variants had molecular weights of 92,000, 56,000, and 42,000. None of these components was detected in the parent cell-line. A major WGA-binding glycoprotein, which accounted for 37% of the total [3H]glucosamine incorporated, was isolated from the spent medium of the parent mouse melanoma cell-line. This glycoprotein was apparently absent in the WGA-1-resistant variants.

Agglutination Tests↗

PubMed1989

Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography.

We recently found that many RNA polymerase II transcription factors are modified with N-acetylglucosamine residues. These sugar moieties confer upon transcription factors an ability to bind the lectin wheat germ agglutinin. We have taken advantage of this interaction to devise a purification procedure for the "GC-box" binding transcription factor Sp1. Crude nuclear extracts are first subjected to wheat germ agglutinin affinity chromatography and then subjected to sequence-specific DNA affinity chromatography. The Sp1 protein purified by this procedure is at least 95% pure, and the overall recovery is greater than 80%. In addition to yielding larger quantities of Sp1 than conventional schemes, the new purification procedure is also simpler and more rapid. We show that wheat germ agglutinin affinity chromatography can also be used to purify the glycosylated forms of the CCAAT-binding transcription factor. Thus, wheat germ agglutinin affinity chromatography may aid the purification of other transcription factors that bear N-acetylglucosamine residues. Furthermore, the ability to separate glycosylated forms of transcription factors from their unglycosylated counterparts by wheat germ agglutinin affinity chromatography should facilitate investigations into the role of N-acetylglucosamine residues in the functioning of transcription factor proteins.

Acetylglucosamine↗