Chromosomal control of wheat gliadin protein epitopes: analysis with specific monoclonal antibodies

1991 ◽  
Vol 82 (1) ◽  
pp. 44-53 ◽  
Author(s):  
J. H. Skerritt ◽  
O. Martinuzzi ◽  
E. V. Metakovsky
Keyword(s):  
Monoclonal Antibodies ◽  
Wheat Gliadin ◽  
Gliadin Protein

Curcumin Resuscitate Gliadin Induced Oxidative Damage And Altered Cellular Responses In Human Intestinal Cells Via Cross-Talk Between The Transcription Factor Nrf-2 And Multifunctional Protein APE1

2021 ◽  
Author(s):  
Kunj Bihari Gupta ◽  
Anil Kumar Mantha ◽  
Monisha Dhiman
Keyword(s):  
Oxidative Stress ◽  
Dna Repair ◽  
Nitrosative Stress ◽  
Mitochondrial Ros ◽  
Hct 116 ◽  
Wheat Gliadin ◽  
Pre Treatment ◽  
Gliadin Protein ◽  
Ht 29

Abstract An imbalance between the production of oxygen and nitrogen free radicals and their degradation by the antioxidant system are the major causative factors for the wheat intolerance diseases. In the present study, we have examined the wheat gliadin protein-induced oxidative and nitrosative stress and downstream responses in the human intestinal cell lines viz. HCT-116 and HT-29. The role of phytochemical curcumin was investigated to alleviate the gliadin associated cellular damages. The focus of the study was to identify the role of key DNA repair enzyme apurinic/apyrimidinic endonuclease 1 (APE1) in gliadin protein-induced toxicity in the intestine, which may be crucial for establishing the gut-associated diseases. Reactive oxygen species (ROS); reactive nitrogen species (RNS); mitochondrial ROS; mitochondrial trans-membrane potential; protein carbonylation; lipid peroxidation; and the oxidized DNA base damage was estimated in HCT-116 and HT-29 cells after 24 h treatment of 160 µg/ml of gliadin, 10 µM of curcumin and its combination. In addition, the transcriptional expression and enzymatic activities of antioxidants (SOD; Catalase; and GSH) were measured in the in these cells. Furthermore, the cross-talk between the nuclear factor erythroid 2-related factor-2 (Nrf-2) and the multifunctional enzyme APE1 was analyzed by the immunofluorescent based imaging and co-immunoprecipitation assays. The endonuclease activity of APE1 and the DNA-protein interaction of NRF-2 with ARE was analyzed by using electrophoretic mobility shift assay (EMSA) with the nuclear lysates of HCT-116 and HT-29 cells. Results suggest that 3 h pre-treatment of curcumin followed by the treatment of gliadin protein for 24 h time protect the HCT-116 and HT-29 cells via (1) decreasing the ROS, RNS, oxidative stress, mitochondrial ROS, recuperate mitochondrial trans-membrane potential; (2) reestablishing the cellular antioxidant defence systems; (3) enhancing the DNA-repair via APE1 and which further activates the ARE elements via activation of Nrf-2. In conclusion, wheat gliadin induces the oxidative/nitrosative stress, mitochondrial damage and damages the cellular biomolecules; hence is associated with the disease pathogenesis and tissue damage in wheat intolerance diseases. The gliadin induced stress and its consequences are significantly reduced by the pre-treatment of curcumin via DNA repair pathways and oxidative stress which is evident through the interaction between two essential proteins of these pathways APE1 and Nrf-2 hence suggesting the role of curcumin based management of wheat intolerance diseases like celiac disease.

Monoclonal Antibodies to Measure Wheat Gliadin in Gluten-Free Foods

1986 ◽  
Vol 71 (s15) ◽  
pp. 69P-69P
Author(s):  
A.R. Freedman ◽  
G. Galfre ◽  
P.J. Ciclitira
Keyword(s):  
Monoclonal Antibodies ◽  
Gluten Free ◽  
Wheat Gliadin

Ultrastructural analysis of unique glycoconjugates in the rat olfactory system

1992 ◽  
Vol 50 (1) ◽  
pp. 890-891
Author(s):  
James E. Crandall ◽  
Linda C. Hassinger ◽  
Gerald A. Schwarting
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Monoclonal Antibodies ◽  
Olfactory System ◽  
Olfactory Bulbs ◽  
Temporal And Spatial Patterns ◽  
Carbohydrate Epitopes ◽  
Olfactory Systems ◽  
Temporal And Spatial ◽  
Cell Surface Glycoconjugates

Cell surface glycoconjugates are considered to play important roles in cell-cell interactions in the developing central nervous system. We have previously described a group of monoclonal antibodies that recognize defined carbohydrate epitopes and reveal unique temporal and spatial patterns of immunoreactivity in the developing main and accessory olfactory systems in rats. Antibody CC2 reacts with complex α-galactosyl and α-fucosyl glycoproteins and glycolipids. Antibody CC1 reacts with terminal N-acetyl galactosamine residues of globoside-like glycolipids. Antibody 1B2 reacts with β-galactosyl glycolipids and glycoproteins. Our light microscopic data suggest that these antigens may be located on the surfaces of axons of the vomeronasal and olfactory nerves as well as on some of their target neurons in the main and accessory olfactory bulbs.

Structural and Chemical Studies of Pathological Fibers in Human Neurofibrillary Degeneration

1985 ◽  
Vol 43 ◽  
pp. 726-729
Author(s):  
K.S. Kosik ◽  
L.K. Duffy ◽  
S. Bakalis ◽  
C. Abraham ◽  
D.J. Selkoe
Keyword(s):  
Monoclonal Antibodies ◽  
Alzheimer Disease ◽  
Human Brain ◽  
Neurofibrillary Tangles ◽  
Morphological Analysis ◽  
High Specificity ◽  
Cytoskeletal Proteins ◽  
Neuritic Plaque ◽  
Protein Chemistry ◽  
Chemical Studies

The major structural lesions of the human brain during aging and in Alzheimer disease (AD) are the neurofibrillary tangles (NFT) and the senile (neuritic) plaque. Although these fibrous alterations have been recognized by light microscopists for almost a century, detailed biochemical and morphological analysis of the lesions has been undertaken only recently. Because the intraneuronal deposits in the NFT and the plaque neurites and the extraneuronal amyloid cores of the plaques have a filamentous ultrastructure, the neuronal cytoskeleton has played a prominent role in most pathogenetic hypotheses.The approach of our laboratory toward elucidating the origin of plaques and tangles in AD has been two-fold: the use of analytical protein chemistry to purify and then characterize the pathological fibers comprising the tangles and plaques, and the use of certain monoclonal antibodies to neuronal cytoskeletal proteins that, despite high specificity, cross-react with NFT and thus implicate epitopes of these proteins as constituents of the tangles.

Use of immunoblotting and monoclonal antibodies to evaluate the residual antigenic activity of milk protein hydrolysed formulae

1996 ◽  
Vol 26 (10) ◽  
pp. 1182-1187 ◽  
Author(s):  
P. RESTANI ◽  
A. PLEBANI ◽  
T. VELONA ◽  
G. CAVAGNI ◽  
A. G. UGAZIO ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Milk Protein ◽  
Antigenic Activity
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