1.The Role of Barrier Dysfunction and Change of Claudin Expression in Inflammatory Bowel Disease.
Gut and Liver 2015;9(6):699-700
No abstract available.
Animals
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Apoptosis/*physiology
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Claudins/*metabolism
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Colitis/*physiopathology
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Intestinal Mucosa/*physiopathology
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Mannose-Binding Lectin/*immunology
2.Structure and immunomodulation activity of a novel mannose binding lectin from housefly pupae.
Chunling WANG ; Yan XIA ; Shijiao ZHANG ; Lirui WANG ; Xiaohong CAO
Chinese Journal of Biotechnology 2013;29(5):601-611
We purified a novel mannose binding lectin form Musca domestica pupae by affinity chromatography on Con A-Sepharose 4B and DEAE weak anion-exchange chromatography. By SDS-PAGE, MBL-1 yielded a single band with the molecular weight of 24 kDa. It was a glycoprotein detected by periodic acid-schiffs staining reaction, with 97.36% protein and 2.1% oligosaccharide. Meanwhile, the results of beta-elimination reaction, infrared spectroscopy, atomic force microscopy and protein sequencing instrument show that MBL-1 was an ellipsoidal-shaped monomer with 60-100 nm in diameter. N-glycoside bond linked oligosaccharide chain and the N-terminal blocked peptide chain. Further study suggested that MBL-1 promote the proliferation of macrophage in a concentration-dependent manner. The scanning electron microscope analysis shows that MBL-1 promoted the activation of macrophages. These results show that MBL-1 purified from Musca domestica pupae possesses immune regulation effect, serving a reference basis to develop natural immune-modulator.
Animals
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Glycoproteins
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analysis
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Houseflies
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chemistry
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Immunomodulation
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immunology
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physiology
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Macrophages
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immunology
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Mannose-Binding Lectin
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chemistry
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physiology
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Oligosaccharides
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analysis
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Pupa
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chemistry
3.Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry.
Kristelle S BROWN ; Michael J KEOGH ; Ania M OWSIANKA ; Richard ADAIR ; Arvind H PATEL ; James N ARNOLD ; Jonathan K BALL ; Robert B SIM ; Alexander W TARR ; Timothy P HICKLING
Protein & Cell 2010;1(7):664-674
Mannan-binding lectin (MBL) is a soluble innate immune protein that binds to glycosylated targets. MBL acts as an opsonin and activates complement, contributing to the destruction and clearance of infecting microorganisms. Hepatitis C virus (HCV) encodes two envelope glycoproteins E1 and E2, expressed as non-covalent E1/E2 heterodimers in the viral envelope. E1 and E2 are potential ligands for MBL. Here we describe an analysis of the interaction between HCV and MBL using recombinant soluble E2 ectodomain fragment, the full-length E1/E2 heterodimer, expressed in vitro, and assess the effect of this interaction on virus entry. A binding assay using antibody capture of full length E1/E2 heterodimers was used to demonstrate calcium dependent, saturating binding of MBL to HCV glycoproteins. Competition with various saccharides further confirmed that the interaction was via the lectin domain of MBL. MBL binds to E1/E2 representing a broad range of virus genotypes. MBL was shown to neutralize the entry into Huh-7 cells of HCV pseudoparticles (HCVpp) bearing E1/E2 from a wide range of genotypes. HCVpp were neutralized to varying degrees. MBL was also shown to neutralize an authentic cell culture infectious virus, strain JFH-1 (HCVcc). Furthermore, binding of MBL to E1/E2 was able to activate the complement system via MBL-associated serine protease 2. In conclusion, MBL interacts directly with HCV glycoproteins, which are present on the surface of the virion, resulting in neutralization of HCV particles.
Binding, Competitive
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Glycosylation
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Hepacivirus
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genetics
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pathogenicity
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physiology
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Humans
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Mannose-Binding Lectin
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metabolism
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Mannose-Binding Protein-Associated Serine Proteases
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metabolism
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Monosaccharides
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metabolism
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Protein Binding
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Protein Multimerization
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Tumor Cells, Cultured
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Viral Envelope Proteins
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metabolism
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Virion
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pathogenicity
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physiology
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Virus Internalization
4.Roles of pattern recognition receptors in diabetic nephropathy.
Zhi-Feng ZHOU ; Lei JIANG ; Qing ZHAO ; Yu WANG ; Jing ZHOU ; Qin-Kai CHEN ; Jin-Lei LV
Journal of Zhejiang University. Science. B 2020;21(3):192-203
Diabetic nephropathy (DN) is currently the most common complication of diabetes. It is considered to be one of the leading causes of end-stage renal disease (ESRD) and affects many diabetic patients. The pathogenesis of DN is extremely complex and has not yet been clarified; however, in recent years, increasing evidence has shown the important role of innate immunity in DN pathogenesis. Pattern recognition receptors (PRRs) are important components of the innate immune system and have a significant impact on the occurrence and development of DN. In this review, we classify PRRs into secretory, endocytic, and signal transduction PRRs according to the relationship between the PRRs and subcellular compartments. PRRs can recognize related pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs), thus triggering a series of inflammatory responses, promoting renal fibrosis, and finally causing renal impairment. In this review, we describe the proposed role of each type of PRRs in the development and progression of DN.
Alarmins/physiology*
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C-Reactive Protein/physiology*
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Diabetic Nephropathies/etiology*
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Endocytosis
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Humans
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Immunity, Innate
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Mannose-Binding Lectin/physiology*
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Pathogen-Associated Molecular Pattern Molecules
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Receptors, Pattern Recognition/physiology*
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Serum Amyloid P-Component/physiology*
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Signal Transduction
5.Changes in the Expression and Distribution of Claudins, Increased Epithelial Apoptosis, and a Mannan-Binding Lectin-Associated Immune Response Lead to Barrier Dysfunction in Dextran Sodium Sulfate-Induced Rat Colitis.
Bosi YUAN ; Shuping ZHOU ; Youke LU ; Jiong LIU ; Xinxin JIN ; Haijun WAN ; Fangyu WANG
Gut and Liver 2015;9(6):734-740
BACKGROUND/AIMS: This animal study aimed to define the underlying cellular mechanisms of intestinal barrier dysfunction. METHODS: Rats were fed 4% with dextran sodium sulfate (DSS) to induce experimental colitis. We analyzed the sugars in 24-hour urine output by high pressure liquid chromatography. The expression of claudins, mannan-binding lectin (MBL), and MBL-associated serine proteases 2 (MASP-2) were detected in the colonic mucosa by immunohistochemistry; and apoptotic cells in the colonic epithelium were detected by the terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick-end labeling method assay. RESULTS: The lactulose and sucralose excretion levels in the urine of rats with DSS-induced colitis were significantly higher than those in the control rats. Mannitol excretion was lower and lactulose/mannitol ratios and sucralose/mannitol ratios were significantly increased compared with those in the control group (p<0.05). Compared with the controls, the expression of sealing claudins (claudin 3, claudin 5, and claudin 8) was significantly decreased, but that of claudin 1 was increased. The expression of pore-forming claudin 2 was upregulated and claudin 7 was downregulated in DSS-induced colitis. The epithelial apoptotic ratio was 2.8%+/-1.2% in controls and was significantly increased to 7.2%+/-1.2% in DSS-induced colitis. The expression of MBL and MASP-2 in the intestinal mucosa showed intense staining in controls, whereas there was weak staining in the rats with colitis. CONCLUSIONS: There was increased intestinal permeability in DSS-induced colitis. Changes in the expression and distribution of claudins, increased epithelial apoptosis, and the MASP-2-induced immune response impaired the intestinal epithelium and contributed to high intestinal permeability.
Animals
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Apoptosis/*physiology
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Claudins/*metabolism
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Colitis/chemically induced/immunology/*physiopathology
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Colon/immunology/physiopathology
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Dextran Sulfate
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Intestinal Mucosa/*physiopathology
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Lactulose/metabolism
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Mannitol/metabolism
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Mannose-Binding Lectin/*immunology
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Permeability
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Rats
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Rats, Sprague-Dawley
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Sucrose/analogs & derivatives/metabolism
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Up-Regulation