scholarly journals Kiwifruit defense protein, kiwellin (Act d 5) percutaneously sensitizes mouse models through the epidermal application of crude kiwifruit extract

2021 ◽  
Author(s):  
Tatsuya Moriyama ◽  
Serina Kinugasa ◽  
Shota Hidaka ◽  
Serina Tanaka ◽  
Eri Izumi ◽  
...  
Keyword(s):  
Sodium Dodecyl ◽  
Specific Ige ◽  
Amino Acid Sequences ◽  
The Body ◽  
Enzyme Linked Immunosorbent Assay ◽  
Related Protein ◽  
Crude Extracts ◽  
Pathogenesis Related Protein ◽  
Defense Protein ◽  
Related Proteins

Background: Kiwifruit is a popular fruit consumed worldwide and is also used as a cosmetic ingredient. However, it is known to cause allergic reactions in humans. Recent studies have suggested an association between food allergy and food allergens entering the body via the skin. However, percutaneously sensitizing kiwifruit allergens have not been identified in human studies or in animal models. Objective: This study aimed to identify kiwifruit proteins that percutaneously sensitized mice through the epidermal application of crude extracts from green and gold kiwifruit on the dorsal skin, and serum IgE and IgG1 levels were used as sensitization markers. Design: BALB/c mice were back-shaved and their skin was exposed to crude extracts from green and gold kiwifruit that contained sodium dodecyl sulfate. Specific IgE and IgG1 antibodies generated and secreted in response to antigens were measured using enzyme-linked immunosorbent assay or immunoblotting. Results: Skin exposure to kiwifruit extract induced an increase in the levels of kiwifruit-specific IgE and IgG1, which are helper T cell 2-related allergenic antibodies in mice. These antibodies reacted with 18, 23, and 24 kDa proteins found in both green and gold kiwifruits. Thus, three percutaneously sensitizing allergens were identified and purified. Their amino acid sequences partially matched with that of kiwellin (Act d 5). Discussion and conclusion: Kiwellin has been identified as a plant defense-related protein. Interestingly, many plant allergens are biodefense-related proteins belonging to the pathogenesis-related protein family. Kiwellin, which was discovered to be a transdermal sensitizing antigen, might also be categorized as a biodefense-related protein. This study is the first to identify kiwellin (Act d 5) as a percutaneously sensitizing kiwifruit allergen in a mouse model.

scholarly journals Thaumatin-Like Protein (Pru av 2) Is a Cherry Allergen That Triggers Percutaneous Sensitization in Mice

Foods ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 134
Author(s):  
Eri Izumi ◽  
Shota Hidaka ◽  
Ayako Hiroi ◽  
Serina Kinugasa ◽  
Erika Yano ◽  
...  
Keyword(s):  
Sodium Dodecyl ◽  
Specific Ige ◽  
The Body ◽  
Food Allergies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Allergenic Food ◽  
Food Allergens ◽  
Skin Exposure ◽  
First Time ◽  
Major Cherry Allergen

Numerous recent studies have suggested that food allergens enter the skin and predispose individuals to food allergies through the production of IgE antibodies in the body. Cherries are a popular fruit eaten worldwide. However, cherries are an allergenic food and percutaneous sensitization with cherry allergens through the perioral region may occur while ingesting cherries. The identity of the cherry protein that triggers percutaneous sensitization in humans or animal models remains unknown. In this study, the backs of BALB/c mice were shaved and crude cherry extracts containing sodium dodecyl sulfate were applied to the skin. Thereafter, the cherry-specific IgE and IgG1 antibodies generated and secreted in response to the epidermal application were measured using an enzyme-linked immunosorbent assay or immunoblotting. Skin exposure to cherry extracts elevated cherry-specific IgG1 levels. Application of fractionated and purified cherry proteins (antigen candidates for percutaneous sensitization) that bound to the IgG1 antibodies led to the identification of a thaumatin-like protein (Pru av 2). This molecule is known as the major cherry allergen that affects humans. In conclusion, our study identified Pru av 2 as a cherry allergen that triggers percutaneous sensitization in mice for the first time.

scholarly journals Granulins: the structure and function of an emerging family of growth factors

1998 ◽  
Vol 158 (2) ◽  
pp. 145-151 ◽  
Author(s):  
A Bateman ◽  
HP Bennett
Keyword(s):  
Cell Growth ◽  
Biological Activities ◽  
Three Dimensional ◽  
Mesenchymal Cells ◽  
Amino Acid Sequences ◽  
The Body ◽  
Egf Receptors ◽  
Haematopoietic Cells ◽  
And Function ◽  
Related Proteins

The granulin/epithelin motif defines a family of structurally unique proteins, of great evolutionary antiquity, which have been implicated as regulators of cell growth. Recurrent in granulin research are the surprising parallels between the granulin and EGF systems. Both are cysteinerich peptides of approximately 6 kDa that can modify cell growth. They show similar, but not identical, biological activities, although granulin/epithelin peptides do not bind EGF receptors; the three-dimensional folds of granulin and EGF are partially superimposible; and the precursors for mammalian granulin/epithelins and EGF are both organized as multiple repeats of conserved cysteine modules. Given the dissimilarity between amino acid sequences of members of the granulin/epithelin family and EGF-related peptides, the parallelism between the two systems probably represents convergent evolution towards related solutions to common biological problems. The granulin/epithelin precursor gene is expressed throughout the body, but its expression is predominantly in epithelial and haematopoietic cells. There is a great deal of versatility in the means by which cells process and handle the granulin/epithelin precursor. In some instances, the precursor is secreted intact (Zhou et al. 1993), and in others it is stored in a vesicular organelle, such as the sperm acrosome (Baba et al. 1993a). It may be processed into small 6-kDa peptides, which, in the neutrophil, can also be stored in vesicles (Bateman et al. 1990, Couto et al. 1992). The 6-kDa peptide forms, the intact precursor, and related proteins such as TGFe, regulate the growth of epithelial and mesenchymal cells. Epithelial cells express putative receptors for granulin/epithelin peptides and TGFe (Culouscou et al. 1993, Parnell et al. 1995). Thus, although much remains to be clarified, granulin/epithelin polypeptides and related proteins are emerging as widely distributed potential autocrine and paracrine growth modulating factors for epithelial and mesenchymal cells.

scholarly journals Antibody produced against isolated Rh(D) polypeptide reacts with other Rh-related antigens

Blood ◽  
1988 ◽  
Vol 72 (5) ◽  
pp. 1622-1626
Author(s):  
K Suyama ◽  
J Goldstein
Keyword(s):  
Gel Electrophoresis ◽  
High Titer ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rabbit Antibody ◽  
Immune Precipitation ◽  
D Cells ◽  
D Antigen ◽  
Related Proteins

Rh(D) antigen-containing polypeptide was prepared by immune precipitation of intact cDE/cDE erythrocytes by using a high-titer preparation of polyclonal anti-D. when isolated Rh(D) polypeptide was administered to rabbits, antibody was produced that was unresponsive toward Rh-positive and -negative cells but reacted strongly with the immunogen in enzyme-linked immunosorbent assay-type immunobinding and Western blot immunostaining assays. Rabbit antibody also immunostains isolated Rh(c) polypeptide as well as the Rh antigen-containing components of sodium dodecyl sulfate-polyacrylamide gel electrophoresis- separated membrane proteins from Rh(D)-positive (cDE/cDE,CDe/CDe), Rh(D)-negative (cde/cde,Cde/Cde), and -D-/-D- cells. It does not react with any membrane protein from Rh-null regulator type cells, thus indicating a specificity for Rh-related proteins. We have also been able to demonstrate that polyclonal and monoclonal anti-D preparations that do not immunostain isolated Rh(D) polypeptide will react with it in our immunobinding assay.

scholarly journals Fertility-LightGBM: A fertility-related protein prediction model by multi-information fusion and light gradient boosting machine

2020 ◽  
Author(s):  
Lingling Yue ◽  
Minghui Wang ◽  
Xinhua Yang ◽  
Yu Han ◽  
Lili Song ◽  
...  
Keyword(s):  
Prediction Model ◽  
Amino Acid Sequences ◽  
Training Dataset ◽  
Gradient Boosting ◽  
Sequence Information ◽  
Related Protein ◽  
Light Gradient ◽  
Protein Prediction ◽  
Gradient Boosting Machine ◽  
Related Proteins

ABSTRACTThe identification of fertility-related proteins plays an essential part in understanding the embryogenesis of germ cell development. Since the traditional experimental methods are expensive and time-consuming to identify fertility-related proteins, the purposes of predicting protein functions from amino acid sequences appeared. In this paper, we propose a fertility-related protein prediction model. Firstly, the model combines protein physicochemical property information, evolutionary information and sequence information to construct the initial feature space ‘ALL’. Then, the least absolute shrinkage and selection operator (LASSO) is used to remove redundant features. Finally, light gradient boosting machine (LightGBM) is used as a classifier to predict. The 5-fold cross-validation accuracy of the training dataset is 88.5%, and the independent accuracy of the training dataset is 91.5%. The results show that our model is more competitive for the prediction of fertility-related proteins, which is helpful for the study of fertility diseases and related drug targets.

scholarly journals TechLab and Alexon Giardia Enzyme-Linked Immunosorbent Assay Kits Detect Cyst Wall Protein 1

1999 ◽  
Vol 37 (3) ◽  
pp. 611-614 ◽  
Author(s):  
James H. Boone ◽  
Tracy D. Wilkins ◽  
Theodore E. Nash ◽  
Jill E. Brandon ◽  
Elizabeth A. Macias ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cyst Wall ◽  
Fluorescent Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amino Acid Sequences ◽  
Enzyme Linked Immunosorbent Assay ◽  
Stool Specimens ◽  
Human Stool ◽  
Immunofluorescence Antibody

A Giardia lamblia antigen detected by the TechLabGiardia Test (TechLab, Inc., Blacksburg, Va.) and the Alexon ProSpecT Giardia microplate assay (Alexon, Inc., Sunnyvale, Calif.) was purified by immunoaffinity chromatography from supernatant fluids of encystment cultures. Two major proteins (M r 22,000 and 26,000) were observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Coomassie staining that did not resemble the GSA65 antigen reportedly detected by the Alexon test. These proteins reacted intensely with the monoclonal antibodies used in both commercial enzyme-linked immunosorbent assays (ELISAs). Both proteins had identical N-terminal amino acid sequences and were identified as cyst wall protein 1 (CWP1). The 26-kDa form appeared early during encystment followed by the appearance of the 22-kDa form. Recombinant CWP1 (M r 26,000) was strongly positive in both commercial tests. CWP1 was stable in human stool specimens, resistant to degradation by proteases andN- and O-glycanases, and unaffected by oxidation with sodium periodate. Two minor proteins withM rs of 32,000 and 39,000 were detected in CWP1 preparations by using a sensitive fluorescent protein stain. Both were identified as CWP2, and neither reacted with the monoclonal antibodies from the commercial tests. We analyzed 535 stool specimens for CWP1 by using both commercial ELISAs and resolved discrepant results by using routine ova and parasite examination (O&P) and on immunofluorescence antibody assay. The presence of CWP1 correlated well between both ELISAs (98.7% correlation). Our results demonstrate that both commercial ELISAs detect CWP1, which is a useful diagnostic marker because it is highly stable, is secreted in large amounts by encysting trophozoites, and correlates well with O&P.

scholarly journals Two Caenorhabditis elegans calponin-related proteins have overlapping functions to maintain cytoskeletal integrity and are essential for reproduction

2020 ◽  
Author(s):  
Shoichiro Ono ◽  
Kanako Ono
Keyword(s):  
Caenorhabditis Elegans ◽  
Actin Filaments ◽  
Body Wall ◽  
The Body ◽  
Body Wall Muscle ◽  
Related Protein ◽  
Somatic Gonad ◽  
Related Proteins

AbstractMulticellular organisms have multiple genes encoding calponins and calponin-related proteins, and some of these are known to regulate actin cytoskeletal dynamics and contractility. However, functional similarities and differences among these proteins are largely unknown. In the nematode Caenorhabditis elegans, UNC-87 is a calponin-related protein with seven calponin-like (CLIK) motifs and is required for maintenance of contractile apparatuses in muscle cells. Here, we report that CLIK-1, another calponin-related protein that also contains seven CLIK motifs, has an overlapping function with UNC-87 to maintain actin cytoskeletal integrity in vivo and has both common and different actin-regulatory activities in vitro. CLIK-1 is predominantly expressed in the body wall muscle and somatic gonad, where UNC-87 is also expressed. unc-87 mutation causes cytoskeletal defects in the body wall muscle and somatic gonad, whereas clik-1 depletion alone causes no detectable phenotypes. However, simultaneous depletion of clik-1 and unc-87 caused sterility due to ovulation failure by severely affecting the contractile actin networks in the myoepithelial sheath of the somatic gonad. In vitro, UNC-87 bundles actin filaments. However, CLIK-1 binds to actin filaments without bundling them and is antagonistic to UNC-87 in filament bundling. UNC-87 and CLIK-1 share common functions to inhibit cofilin binding and allow tropomyosin binding to actin filaments, suggesting that both proteins stabilize actin filaments. Thus, partially redundant functions of UNC-87 and CLIK-1 in ovulation is likely mediated by their common actin-regulatory activities, but their distinct activities in actin bundling suggest that they also have different biological functions.

scholarly journals High Methionine Diet-Induced Alzheimer’s Disease like Symptoms Are Accompanied by 5-Methylcytosine Elevated Levels in the Brain

2021 ◽  
Vol 2021 ◽  
pp. 1-16
Author(s):  
Tingting Pi ◽  
Shenjiao Wei ◽  
Yongxuan Jiang ◽  
Jing-Shan Shi
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Food Intake ◽  
Amyloid Β ◽  
The Body ◽  
Morris Water Maze Test ◽  
Enzyme Linked Immunosorbent Assay ◽  
Ability Test ◽  
Maze Test ◽  
Related Proteins

Background. Excessive or insufficient intake of methionine (Met) causes neuronal dysfunction, neurodegeneration, cerebrovascular dysfunction, vascular leakage, and short-term memory loss, which result in the occurrence of Alzheimer’s disease- (AD-) like symptoms. Objective. To determine the relationship between high methionine diets (HMD) induced AD-like symptoms and 5-methylcytosine (5-mC) level. Methods. C57BL/6J mice were randomly divided into two groups: the control group (Maintain diets) and the model group (2% HMD). Mice were fed with 2% HMD for 9 weeks. Animals were weighed and food intake was recorded weekly. Open field test, nesting ability test, Y maze test, new object recognition test, and Morris water maze test were used to detect the motor, learning, and memory ability. Hematoxylin-eosin (HE) staining was used to observe the damage of cells in hippocampus and cortex. Immunofluorescence (IF) staining was used to detect the expression and distribution of amyloid-β 1-40 (Aβ1-40), amyloid-β 1-42 (Aβ1-42), and 5-methylcytosine (5-mC) in hippocampus and cortex. Western blotting (WB) was used to determine the expression of Aβ and DNA methyltransferases- (DNMTs-) related proteins in the cortex. Enzyme-linked immunosorbent assay (ELISA) was performed to detect homocysteine (Hcy) level (ELISA). Results. Feeding of HMD decreased the body weight and food intake of mice. Behavioral testing revealed that HMD caused learning, memory, and motor ability impairment in the mice. HE staining results showed that HMD feeding caused damage of hippocampal and cortical neurons, along with disordered cell arrangement, and loss of neurons. Furthermore, HMD increased the contents of Aβ1-40, Aβ1-42, and 5-mC in the hippocampus and cortex. WB results showed that HMD increased the expression of Aβ production-related proteins, such as amyloid precursor protein (APP) and beta-secretase 1 (BACE1), and decreased the expression of Aβ metabolism-related protein in the cortex, including insulin-degrading enzyme (IDE) and neprilysin (NEP). Additionally, the decreased expression of DNA methyltransferase1 (DNMT1) was observed in HMD-treated mice, but there was no significant change of DNMT3a level. ELISA results showed that HMD increased the levels of Hcy in serum. Conclusion. Our result suggested that the HMD can cause neurotoxicity, leading to AD-like symptoms in mice, which may be related to 5-mC elevated.

scholarly journals Albiflorin attenuates inflammation and apoptosis by upregulating AMPK-mediated expression of CDX2 in a mouse model of ulcerative colitis

2020 ◽  
Vol 19 (5) ◽  
pp. 995-999
Author(s):  
Xiaoping Xu ◽  
Haiyan Liu ◽  
Yuan Pan ◽  
Zhaohui Lui ◽  
Dong Chen ◽  
...  
Keyword(s):  
Ulcerative Colitis ◽  
Body Weight ◽  
Inflammatory Cytokines ◽  
Mucosal Damage ◽  
The Body ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mice Model ◽  
Ameliorative Effect ◽  
Related Proteins ◽  
Hematoxylin Eosin

Purpose: To investigate the mechanism underlying the ameliorative effect of albiflorin (AF) on ulcerative colitis (UC) in dextran sulphate sodium (DSS)-induced mice model. Method: Female C57BL/6 mice were administered DSS to establish a mice model of UC. After one week, the mice received AF, and the body weight and length of colon were measured. The histopathological features of colon tissues treated with hematoxylin-eosin (H & E) stain were examinedby microscopy. Expression of inflammatory cytokines and apoptosis-related proteins were determined using enzyme-linked immunosorbent assay (ELISA) and western blotting. Results: The relative abundance of goblet cells and crypts of mice were significantly reduced in DSSinduced UC mice model; furthermore, focal ulcers and mucosal damage were apparent. Moreover, treatment with DSS decreased body weight and colon length, downregulated Bcl-2 and AMPK pathwayrelated proteins, increased inflammatory cytokines levels, and upregulated Bax and cleaved caspase-3. In contrast, treatment with AF completely ameliorated DSS-induced effects. Conclusion: AF treatment attenuated DSS-induced inflammation response and apoptosis via AMPK pathway and modulation of CDX2 expression in UC mice model. Keyword: Albiflorin, Ulcerative colitis, AMPK, CDX2, Apoptosis

scholarly journals Current Overview of Allergens of Plant Pathogenesis Related Protein Families

2014 ◽  
Vol 2014 ◽  
pp. 1-19 ◽  
Author(s):  
Mau Sinha ◽  
Rashmi Prabha Singh ◽  
Gajraj Singh Kushwaha ◽  
Naseer Iqbal ◽  
Avinash Singh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cross Reactivity ◽  
Amino Acid Sequences ◽  
Pr Proteins ◽  
Antigenic Determinants ◽  
Related Protein ◽  
Protein Families ◽  
Pathogenesis Related Protein ◽  
Pathogenesis Related ◽  
Plant Pathogenesis

Pathogenesis related (PR) proteins are one of the major sources of plant derived allergens. These proteins are induced by the plants as a defense response system in stress conditions like microbial and insect infections, wounding, exposure to harsh chemicals, and atmospheric conditions. However, some plant tissues that are more exposed to environmental conditions like UV irradiation and insect or fungal attacks express these proteins constitutively. These proteins are mostly resistant to proteases and most of them show considerable stability at low pH. Many of these plant pathogenesis related proteins are found to act as food allergens, latex allergens, and pollen allergens. Proteins having similar amino acid sequences among the members of PR proteins may be responsible for cross-reactivity among allergens from diverse plants. This review analyzes the different pathogenesis related protein families that have been reported as allergens. Proteins of these families have been characterized in regard to their biological functions, amino acid sequence, and cross-reactivity. The three-dimensional structures of some of these allergens have also been evaluated to elucidate the antigenic determinants of these molecules and to explain the cross-reactivity among the various allergens.

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