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Article: Comparison of the Efficacy and Prognostic Factors of Endoscopic Submucosal Dissection with Different Procedures for Colorectal Neuroendocrine Tumors.

Qiu, Minxia / Kong, Cancan / Chen, Wenmei / Mao, Wei

Alternative therapies in health and medicine

2024

Abstract: Objective: To compare the clinical efficacy, prognostic factors, and survival impact of endoscopic submucosal dissection (ESD) versus endoscopic submucosal resection (ESR) in patients with colorectal neuroendocrine tumors (NETs).: Methods: This ... ...

Abstract	Objective: To compare the clinical efficacy, prognostic factors, and survival impact of endoscopic submucosal dissection (ESD) versus endoscopic submucosal resection (ESR) in patients with colorectal neuroendocrine tumors (NETs). Methods: This retrospective study analyzed 118 patients with colorectal NETs treated from January 2012 to December 2020. Patients were divided into the ESD group (n=59) and the ESR group (n=59) based on the surgical treatment method. We assessed the surgical efficacy, long-term survival, and factors influencing tumor recurrence using logistic regression analysis with clear criteria for group division. Results: En bloc resection, complete histological resection rates, and postoperative complications did not significantly differ between groups (P > .05). In the 33 patients with recurrence, those with tumor diameter < 10 mm, tumor grade G1, and negative resection margins were significantly fewer (P < .05). Logistic regression identified tumor diameter, grade, and resection margin status as significant predictors of recurrence (P < .05). There was no significant difference in distant metastasis, survival rates, and mortality between the groups (P > .05). Conclusions: ESD and ESR offer high clinical efficacy in treating colorectal NETs without significantly impacting prognosis or long-term survival. ESD, however, may be more suited for larger tumors due to its precise tissue removal capability. Future research should explore the long-term outcomes over 3 and 5 years to further validate these findings.
Language	English
Publishing date	2024-05-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	1225073-9
ISSN	1078-6791
ISSN	1078-6791
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Article ; Online: Structure and allergenicity of α-lactalbumin: effects of ultrasonic prior to glycation and subsequent phosphorylation

Chen, Wenmei / Chen, Qiongzhen / Zhou, Houze / Shao, Yanhong / Wang, Yang / Liu, Jun / Tu, Zongcai

Food Science and Human Wellness. 2023 May, v. 12, no. 3 p.825-831

2023

Abstract: Bovine α-lactalbumin (BLA) induced severe cow's milk allergy. In this study, a novel strategy combining ultrasonication, performed before glycation, and phosphorylation was proposed to reduce BLA allergenicity. Result showed that IgE- and IgG-binding ... ...

Abstract	Bovine α-lactalbumin (BLA) induced severe cow's milk allergy. In this study, a novel strategy combining ultrasonication, performed before glycation, and phosphorylation was proposed to reduce BLA allergenicity. Result showed that IgE- and IgG-binding capacities and the release rates of histamine and interleukin-6 from RBL-2H3 were reduced. Moreover, intrinsic fluorescence intensity and surface hydrophobicity were decreased, whereas glycated sites (R10, N44, K79, K108, N102 and K114) and phosphorylated sites (Y36 and S112) of BLA were increased. Minimum allergenicity was detected during BLA treatment after ultrasonic prior to glycation and subsequent phosphorylation because of considerable increase in glycated and phosphorylated sites. Therefore, the decrease in allergenicity of BLA, the effect correlated well with the shielding effect of glycated sites combined with phosphorylated sites and the conformational changes. This study provides important theoretical foundations for improving and using the ultrasonic technology combined with protein modification in allergenic protein processing.
Keywords	allergenicity ; allergens ; cattle ; fluorescence ; food science ; glycation ; histamine ; humans ; hydrophobicity ; interleukin-6 ; milk ; milk allergy ; phosphorylation ; ultrasonic treatment ; ultrasonics ; Bovine α-lactalbumin ; Ultrasonic ; Protein modification
Language	English
Dates of publication	2023-05
Size	p. 825-831.
Publishing place	Elsevier B.V.
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	2712869-6
ISSN	2213-4530
ISSN	2213-4530
DOI	10.1016/j.fshw.2022.09.021
Database	NAL-Catalogue (AGRICOLA)

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Article: Ultrasound Improved the Non-Covalent Interaction of β-Lactoglobulin with Luteolin: Regulating Human Intestinal Microbiota and Conformational Epitopes Reduced Allergy Risks.

Wang, Titi / Chen, Wenmei / Shao, Yanhong / Liu, Jun / Tu, Zongcai

Foods (Basel, Switzerland)

2022 Volume 11, Issue 7

Abstract: The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the ... ...

Abstract	The present study aims to investigate the effects of ultrasound on the non-covalent interaction of β-lactoglobulin (β-LG) and luteolin (LUT) and to investigate the relationship between allergenicity and human intestinal microbiota. After treatment, the conformational structures of β-LG were changed, which reflected by the decrease in α-helix content, intrinsic fluorescence intensity and surface hydrophobicity, whereas the β-sheet content increased. Molecular docking studies revealed the non-covalent interaction of β-LG and LUT by hydrogen bond, van der Walls bond and hydrophobic bond. β-LG-LUT complex treated by ultrasound has a lower IgG/IgE binding ability and inhibits the allergic reaction of KU812 cells, depending on the changes in the conformational epitopes of β-LG. Meanwhile, the β-LG-LUT complex affected the composition of human intestinal microbiota, such as the relative abundance of
Language	English
Publishing date	2022-03-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704223-6
ISSN	2304-8158
ISSN	2304-8158
DOI	10.3390/foods11070988
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Article ; Online: Gut Microbiome-Serum Metabolism Revealed the Allergenicity of Ferulic Acid Combined with Glucose-Modified β-Lactoglobulin.

Wang, Yang / Zhang, Kai / Chen, Wen-Mei / Mao, Ji-Hua / Wang, Xu-Mei / Shao, Yan-Hong / Tu, Zong-Cai / Liu, Jun

Journal of agricultural and food chemistry

2024 Volume 72, Issue 20, Page(s) 11746–11758

Abstract: A novel strategy combining ferulic acid and glucose was proposed to reduce β-lactoglobulin (BLG) allergenicity and investigate whether the reduction in allergenicity was associated with gut microbiome and serum metabolism. As a result, the multistructure ...

Abstract	A novel strategy combining ferulic acid and glucose was proposed to reduce β-lactoglobulin (BLG) allergenicity and investigate whether the reduction in allergenicity was associated with gut microbiome and serum metabolism. As a result, the multistructure of BLG changed, and the modified BLG decreased significantly the contents of IgE, IgG, IgG
MeSH term(s)	Coumaric Acids/metabolism ; Coumaric Acids/chemistry ; Gastrointestinal Microbiome ; Animals ; Lactoglobulins/immunology ; Lactoglobulins/chemistry ; Lactoglobulins/metabolism ; Mice ; Humans ; Allergens/immunology ; Allergens/chemistry ; Allergens/metabolism ; Glucose/metabolism ; Female ; Bacteria/immunology ; Bacteria/metabolism ; Bacteria/classification ; Bacteria/genetics ; Mice, Inbred BALB C ; Immunoglobulin E/immunology ; Immunoglobulin E/blood ; Fatty Acids, Volatile/metabolism ; Cattle ; Immunoglobulin G/immunology ; Immunoglobulin G/blood ; Milk Hypersensitivity/immunology
Chemical Substances	ferulic acid
Language	English
Publishing date	2024-05-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.4c01545
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Article: Simulated in vitro digestion of α-lactalbumin modified by phosphorylation: Detection of digestive products and allergenicity

Chen, Wen-mei / Shao, Yan-hong / Wang, Zhi / Liu, Jun / Tu, Zong-cai

Food chemistry. 2022 Mar. 15, v. 372

2022

Abstract: The effects of phosphorylation on the allergenicity of bovine α-lactalbumin (BLA) and digestive products were studied in vitro digestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA. ... ...

Abstract	The effects of phosphorylation on the allergenicity of bovine α-lactalbumin (BLA) and digestive products were studied in vitro digestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA. In vivo and in vitro assessment of allergenicity showed that phosphorylation prior to digestion significantly decreased the IgE/IgG binding capacity and allergic response in KU812 cells, and reduced the levels of IgG, IgE, IL-4 and histamine, with an increase in IFN-γ levels in mouse serum, depending on the changes in BLA structures, producing numerous small peptides. There were four phosphorylated sites (S22, T29, S47 and S70) in the high molecular weight components of phosphorylated BLA after digestion. These phosphorylated sites could mask the linear epitopes of digestive products, resulting in reduced allergic activity. Phosphorylation prior to digestion of dairy products can reduce the risk of anaphylaxis in patients with milk allergy to some extent.
Keywords	allergenicity ; anaphylaxis ; blood serum ; cattle ; digestion ; epitopes ; food chemistry ; histamine ; interleukin-4 ; mice ; milk allergy ; molecular weight ; phosphorylation ; risk reduction
Language	English
Dates of publication	2022-0315
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	243123-3
ISSN	1873-7072 ; 0308-8146
ISSN (online)	1873-7072
ISSN	0308-8146
DOI	10.1016/j.foodchem.2021.131308
Database	NAL-Catalogue (AGRICOLA)

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Article: Bovine β-Lactoglobulin Covalent Modification by Flavonoids: Effect on the Allergenicity and Human Intestinal Microbiota

Liu, Jun / Wang, Yang / Tu, Zong-cai / Chen, Wen-mei / Yuan, Tao

Journal of agricultural and food chemistry. 2021 June 09, v. 69, no. 24

2021

Abstract: The present study aims to investigate the structure of covalent conjugates of bovine β-lactoglobulin (BLG) and flavonoids (luteolin, myricetin, and hyperoside), and their effect on the allergenicity and human intestinal microbiota. Covalent modification ... ...

Abstract	The present study aims to investigate the structure of covalent conjugates of bovine β-lactoglobulin (BLG) and flavonoids (luteolin, myricetin, and hyperoside), and their effect on the allergenicity and human intestinal microbiota. Covalent modification of amino acids in BLG by flavonoids was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and o-phthaldialdehyde assay. The secondary and conformational structures of BLG were changed by the covalent modification, which were determined by the circular dichroism, Fourier transform infrared spectroscopy, fluorescence spectroscopy, and UV spectroscopy. The enzyme-linked immunosorbent assay (ELISA) and cell experiments indicated that BLG covalent conjugates could reduce IgE/IgG binding capacities and suppress the allergy reactivity of RBL-2H3 cells, suggesting that the covalent modification modulated the balance of T cells. Meanwhile, covalent modification of BLG with these flavonoids can alter the diversity of human intestinal microbiota and the community abundance at phylum, family, and genus levels. The results revealed that covalent modification of BLG with flavonoids alters human intestinal microbiota, might result in the reduction of allergenicity, which could provide information for confirming the relationship between food allergy and the intestinal microbial ecosystem.
Keywords	Fourier transform infrared spectroscopy ; allergenicity ; cattle ; circular dichroism spectroscopy ; enzyme-linked immunosorbent assay ; fluorescence emission spectroscopy ; food allergies ; food chemistry ; humans ; intestinal microorganisms ; luteolin ; myricetin ; polyacrylamide gel electrophoresis ; sodium dodecyl sulfate ; ultraviolet-visible spectroscopy
Language	English
Dates of publication	2021-0609
Size	p. 6820-6828.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.1c02482
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Simulated in vitro digestion of α-lactalbumin modified by phosphorylation: Detection of digestive products and allergenicity.

Chen, Wen-Mei / Shao, Yan-Hong / Wang, Zhi / Liu, Jun / Tu, Zong-Cai

Food chemistry

2021 Volume 372, Page(s) 131308

Abstract	The effects of phosphorylation on the allergenicity of bovine α-lactalbumin (BLA) and digestive products were studied in vitro digestion. Two components with different molecular weight and conformation were obtained from natural and phosphorylated BLA. In vivo and in vitro assessment of allergenicity showed that phosphorylation prior to digestion significantly decreased the IgE/IgG binding capacity and allergic response in KU812 cells, and reduced the levels of IgG, IgE, IL-4 and histamine, with an increase in IFN-γ levels in mouse serum, depending on the changes in BLA structures, producing numerous small peptides. There were four phosphorylated sites (S22, T29, S47 and S70) in the high molecular weight components of phosphorylated BLA after digestion. These phosphorylated sites could mask the linear epitopes of digestive products, resulting in reduced allergic activity. Phosphorylation prior to digestion of dairy products can reduce the risk of anaphylaxis in patients with milk allergy to some extent.
MeSH term(s)	Allergens ; Animals ; Cattle ; Digestion ; Immunoglobulin E ; Lactalbumin ; Mice ; Phosphorylation
Chemical Substances	Allergens ; Immunoglobulin E (37341-29-0) ; Lactalbumin (9013-90-5)
Language	English
Publishing date	2021-10-05
Publishing country	England
Document type	Journal Article
ZDB-ID	243123-3
ISSN	1873-7072 ; 0308-8146
ISSN (online)	1873-7072
ISSN	0308-8146
DOI	10.1016/j.foodchem.2021.131308
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Bovine β-Lactoglobulin Covalent Modification by Flavonoids: Effect on the Allergenicity and Human Intestinal Microbiota.

Liu, Jun / Wang, Yang / Tu, Zong-Cai / Chen, Wen-Mei / Yuan, Tao

Journal of agricultural and food chemistry

2021 Volume 69, Issue 24, Page(s) 6820–6828

Abstract	The present study aims to investigate the structure of covalent conjugates of bovine β-lactoglobulin (BLG) and flavonoids (luteolin, myricetin, and hyperoside), and their effect on the allergenicity and human intestinal microbiota. Covalent modification of amino acids in BLG by flavonoids was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and
MeSH term(s)	Allergens ; Animals ; Cattle ; Ecosystem ; Flavonoids ; Gastrointestinal Microbiome ; Humans ; Lactoglobulins
Chemical Substances	Allergens ; Flavonoids ; Lactoglobulins
Language	English
Publishing date	2021-06-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	241619-0
ISSN	1520-5118 ; 0021-8561
ISSN (online)	1520-5118
ISSN	0021-8561
DOI	10.1021/acs.jafc.1c02482
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Article ; Online: Expression of B Cell-Specific Moloney Murine Leukemia Virus Integration Site 1 (BMI-1) and WW Domain-Containing Oxidoreductase (WWOX) in Liver Cancer Tissue and Normal Liver Tissue.

Yu, Jun / Hu, Minlan / Chen, Wenmei / Wen, Zirong

Medical science monitor : international medical journal of experimental and clinical research

2018 Volume 24, Page(s) 6673–6679

Abstract: BACKGROUND The aim of this study was to compare the expression levels of mRNA of the B cell-specific Moloney murine leukemia virus integration site 1 (BMI-1) and the WW domain-containing oxidoreductase (WWOX) genes and their protein products in tissues ... ...

Abstract	BACKGROUND The aim of this study was to compare the expression levels of mRNA of the B cell-specific Moloney murine leukemia virus integration site 1 (BMI-1) and the WW domain-containing oxidoreductase (WWOX) genes and their protein products in tissues from patients with liver cancer with normal liver tissues from patients without liver cancer. MATERIAL AND METHODS The liver cancer group (N=56) included patients with available tissue samples of histologically confirmed liver cancer. The control group (N=24) included histologically confirmed normal liver tissue samples. Immunofluorescence staining and Western blot were used to detect and compare protein expression of Bmi-1 and WWOX in liver tissues in the liver cancer group and the control group. Reverse transcription-polymerase chain reaction (RT-PCR) was used to detect and compare mRNA expression of BMI-1 and WWOX in liver tissues in the liver cancer group and the control group. Expression levels of the protein and mRNA levels and the clinicopathological features including patient prognosis in liver cancer were evaluated statistically using analysis of variance (ANOVA). RESULTS There were significant differences in the expression levels of protein and mRNA of BMI-1 and WWOX between the liver cancer group and the control group. BMI-1 mRNA and protein expression were significantly increased, and WWOX mRNA and protein expression were significantly reduced in liver cancer tissue, compared with normal liver tissue (p<0.05). CONCLUSIONS In liver cancer tissue compared with normal liver, the expression of BMI-1 and WWOX mRNA and their protein products were upregulated and down-regulated, respectively.
MeSH term(s)	Adult ; Aged ; Carcinoma, Hepatocellular/genetics ; China ; Female ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Liver/cytology ; Liver/metabolism ; Liver Neoplasms/genetics ; Liver Neoplasms/metabolism ; Male ; Middle Aged ; Moloney murine leukemia virus ; Oxidoreductases ; Polycomb Repressive Complex 1/genetics ; Polycomb Repressive Complex 1/metabolism ; Prognosis ; RNA, Messenger ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; WW Domain-Containing Oxidoreductase/genetics ; WW Domain-Containing Oxidoreductase/metabolism ; WW Domains
Chemical Substances	BMI1 protein, human ; RNA, Messenger ; Tumor Suppressor Proteins ; Oxidoreductases (EC 1.-) ; WW Domain-Containing Oxidoreductase (EC 1.1.1.-) ; WWOX protein, human (EC 1.1.1.-) ; Polycomb Repressive Complex 1 (EC 2.3.2.27)
Language	English
Publishing date	2018-09-22
Publishing country	United States
Document type	Journal Article
ZDB-ID	1439041-3
ISSN	1643-3750 ; 1234-1010
ISSN (online)	1643-3750
ISSN	1234-1010
DOI	10.12659/MSM.909675
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Article: The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation

Liu, Jun / Chen, Wen-mei / Shao, Yan-hong / Zhang, Jia-li / Tu, Zong-cai

Food chemistry. 2020 Apr. 25, v. 310

2020

Abstract: Bovine α-lactalbumin (α-Lac) allergy is a common health problem. This study assesses the allergenic reactivity and the structural properties of α-Lac after protein modification (glycation, phosphorylation and acetylation) by ELISA, cells experiment and ... ...

Abstract	Bovine α-lactalbumin (α-Lac) allergy is a common health problem. This study assesses the allergenic reactivity and the structural properties of α-Lac after protein modification (glycation, phosphorylation and acetylation) by ELISA, cells experiment and high-resolution mass spectrometry. Three modified methods significantly reduced the IgE/IgG-binding capacity, and the release of histamine and interleukin-6, and changed the conformational structure of α-Lac. α-Lac was glycated at K13, K16, K94, K98, and K108, phosphorylated at Y18, S22, Y103, and S112, and acetylated at K13, T33, S34, T38, S47, K62, S69, S70, K108, and K114, respectively, leading to masking the linear epitopes of α-Lac. Therefore, the decrease of allergenic reactivity of α-Lac induced by glycation, phosphorylation and acetylation depends upon not only the shielding effect of their modified sites, but also the change of conformational structure. This study confirmed that protein modification was a promising method for decreasing the allergenic reactivity of allergic proteins.
Keywords	acetylation ; allergenicity ; cattle ; enzyme-linked immunosorbent assay ; epitopes ; glycation ; histamine ; hypersensitivity ; immunoglobulin E ; interleukin-6 ; lactalbumin ; mass spectrometry ; phosphorylation
Language	English
Dates of publication	2020-0425
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	243123-3
ISSN	1873-7072 ; 0308-8146
ISSN (online)	1873-7072
ISSN	0308-8146
DOI	10.1016/j.foodchem.2019.125853
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