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Search Results: 1 - 10 of 38149 matches for " Lin Zhongxiang "
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Synthesis and NMR Spectral Studies of the 7-C60-Adduct of N,N-(Tetrachlorophthaloyl) Dehydroabietylamine
Zhi Zhou,Zhongxiang Lin
Molecules , 2012, DOI: 10.3390/molecules17044209
Abstract: The 7-C60-adduct of N,N-(tetrachlorophthaloyl)dehydroabietylamine was synthesized for the first time and characterized by IR, UV-vis, mass and NMR spectral studies. The 1H-NMR and 13C-NMR resonance signals of the new compound are unambiguously assigned by using homo- and heteronuclear 2D NMR spectroscopic techniques such as COSY, ROESY, HSQC and HMBC. The C1 symmetric structure with 6,6-junction of compound was determined.
Cell adhesion receptors and cancer
Zhongxiang Lin,Wenjun Zhang
Chinese Science Bulletin , 1999, DOI: 10.1007/BF02885533
Abstract: Cell-to-cell and cell-to-extracellular matrix (ECM) interactions in the functions of cell adhesion and signal transduction are important in global control of cell phenotypes and cell behavior and are crucial for maintenance of homeostasis and structural/functional stabilization of tissues and organs. Cell adhesion receptors are recognized as the molecular basis of cell adhesion. Cadherin and integrin are widely expressed adhesion receptors in most tissues. They are transmembrane glycoproteins which, through their cytoplasmic domain, bind to many proteins at the inner surface of cell membrane to form molecule-linkage complexes and then connect with the cytoskeleton. Through cell adhesion receptors a network functioning as cell adhesion and signal transduction is organized between tissue cells and cellECM. In this regard cell adhesion receptors play an important role in regulation of morphogenesis, cellcell recognition, cell migration, cell sorting and the determination of cell’s fate in development. They mediate cell functions and their fault expression is intimately correlated with development of disorders like cancer. Several isoforms of lntegrin were found to have tumor suppressor effect. Some components in the molecule-linkage of focal contact are actin-binding proteins as well as substrates of kinase in the lntegrin initiated signal pathway to play a role as signal transducer. Some of these molecules exhibited tumor suppressor effect too. Decreased expression of E-Cadherin has been demonstrated in many epithelium originated carcinomas. Cadherin associated membrane adhesion plaque molecule β-Catenin is also involved in the oncogene Wnt signal pathway. Both E-Cadherin and β-Catenin were proved respectively with tumor suppressor effect against invasiveness and metastasis. That Cadherin is important for the posttranslationally functional expression of Connexin has been supported by evidence from developmental biology and cancer cell differentiation studies to suggest that some sort of interrelation feedback control exists between the two signal pathways.
Choice for host-specific high-adhesive Lactobacillus strains  [PDF]
Xueyan Lin, Zhonghua Wang, Zhongxiang Niu, Hongjie Liu, Yun Wang
Advances in Bioscience and Biotechnology (ABB) , 2012, DOI: 10.4236/abb.2012.32022
Abstract: Adhesive ability was tested in seven Lactobacillus solated from the chicken digestive tract after cultivation with CaCo-2 cells (intestinal epithelial cells), MDCK (dog kidney) cells and CEF (chicken embryo fiber) cells. We noted the following important observations regarding the adhesive ability between different Lactobacillus strains and three cell types: the adhesive interaction between the SDnB7, SDnE1 and SDnA3 lactobacillus strains and CaCo-2cells was greater compared to controls, the adhesive effect between SDnB1 and CEF cells was also greater than controls and Lactobacillus showed only minimal adherence to MDCK cells. Incubation time also affected Lactobacillus adherence to CaCo-2cells: adhesive ability was optimal at 37°C when incubated for 2 days and this was confirmed by a local increase in the concentration of Lactobacillus around CaCo-2 cells when incubated for 24 h as opposed to 3 h. Adherence ability in lactobacillus was also tested at various concentrations (108, 107, 106, 105 and 104 ). The number of Lactobacillus that adhered around the cells was significantly increased in the treatment with 108 bacterial cells. Transmission electron microscopy revealed that the cellularity of the junction between CaCo-2cells and Lactobacillus was not compromised. Transmission electron microscopy also revealed that the thalli fabric structure remained intact.
The nature of adhesion factors which lie on the surfaces of Lactobacillus adhering to cells  [PDF]
Xueyan Lin, Zhonghua Wang, Zhongxiang Niu, Jun Peng, Yun Wang
Advances in Bioscience and Biotechnology (ABB) , 2012, DOI: 10.4236/abb.2012.32023
Abstract: Lactobacillus adheres to intestinal epithelial cells and yeast fungus cells with the aid of adhesion factors expressed on its cell surface. To identify adhesion factors nature on the surface of Lactobacillus, an adhesion experiment was carried out by pre-treating the Lactobacillus supernatant with different concentrations of bovine serum albumin, trypsin and 100°C for 10min. Additionally, intestinal epithelial cells were treated with sodium iodate, trypsin and sugar inhibition tests to characterize the receptors in Lactobacillus that interact with intestinal epithelial cells. It was demonstrated that Lactobacillus adhesion ability was decreased (P < 0.01) after treating the supernatant with different concentrations of bovine serum albumin, trypsin and 100°C for 10 min respectively. The adhesion factor on the surface of Lactobacillus cells was identified as a D-mannose glycoprotein. This observation was confirmed after treating intestinal epithelial cells with sodium iodate and trypsin, and sugar inhibition tests. Wild type Lactobacillus can agglutinate yeast fungus cells but after being exposured to mannose, agglutination to yeast fungus cells is lost or reduced. Results from this study we also got that inactivated and live bacteria that similarly adhere to intestinal epithelial cells.
Cell adhesion receptors and cancer

Zhongxiang Lin,Wenjun Zhang,

科学通报(英文版) , 1999,
Abstract: Cell-to-cell and cell-to-extracellular matrix (ECM) interactions in the functions of cell adhesion and signal transduction are important in global control of cell phenotypes and cell behavior and are crucial for maintenance of homeostasis and structural/functional stabilization of tissues and organs. Cell adhesion receptors are recognized as the molecular basis of cell adhesion. Cadherin and integrin are widely expressed adhesion receptors in most tissues. They are transmembrane glycoproteins which, through their cytoplasmic domain, bind to many proteins at the inner surface of cell membrane to form molecule-linkage complexes and then connect with the cytoskeleton. Through cell adhesion receptors a network functioning as cell adhesion and signal transduction is organized between tissue cells and cellECM. In this regard cell adhesion receptors play an important role in regulation of morphogenesis, cellcell recognition, cell migration, cell sorting and the determination of cell’s fate in development. They mediate cell functions and their fault expression is intimately correlated with development of disorders like cancer. Several isoforms of lntegrin were found to have tumor suppressor effect. Some components in the molecule-linkage of focal contact are actin-binding proteins as well as substrates of kinase in the lntegrin initiated signal pathway to play a role as signal transducer. Some of these molecules exhibited tumor suppressor effect too. Decreased expression of E-Cadherin has been demonstrated in many epithelium originated carcinomas. Cadherin associated membrane adhesion plaque molecule β-Catenin is also involved in the oncogene Wnt signal pathway. Both E-Cadherin and β-Catenin were proved respectively with tumor suppressor effect against invasiveness and metastasis. That Cadherin is important for the posttranslationally functional expression of Connexin has been supported by evidence from developmental biology and cancer cell differentiation studies to suggest that some sort of interrelation feedback control exists between the two signal pathways.
Cell surface clustering of Cadherin adhesion complex induced by antibody coated beads
Wenjun Zhang,Zhongxiang Lin,Ying Hu
Chinese Science Bulletin , 2000, DOI: 10.1007/BF02898898
Abstract: Cadherin receptors mediate cell-cell adhesion, signal transduction and assembly of cytoskeletons. How a single transmembrane molecule Cadherin can be involved in multiple functions through modulating its binding activities with many membrane adhesion molecules and cytoskeletal components is an unanswered question which can be elucidated by clues from bead experiments. Human lung cells expressing N-Cadherin were examined. After co-incubation with anti-N-Cadherin monoclonal antibody coated beads, cell surface clustering of N-Cadherin was induced. Immunofluorescent detection demonstrated that in addition to Cadherin, β-Catenin, α-Catenin, α-Actinin and Actin fluorescence also aggregated respectively at the membrane site of bead attachment. Myosin heavy chain (MHC), another major component of Actin cytoskeleton, did not aggregate at the membrane site of bead attachment. Adhesion unrelated protein Con A and polylysine conjugated beads did not induce the clustering of adhesion molecules. It is indicated that the Cadherin/Catenins/α-Actinin/Actin complex is formed at Cadherin mediated cell adherens junction; occupancy and cell surface clustering of Cadherin is crucial for the formation of Cadherin adhesion protein complexes.
Alteration of cadherin isoform expression and inhibition of gap junctions in stomach carcinoma cells
Li Jinping,Zhang Zhiqian,Ning Tao,Ke Yang,Lin Zhongxiang
Chinese Science Bulletin , 2001, DOI: 10.1007/BF02901134
Abstract: To explore cell malignant phenotype correlated changes of cell surface adhesion molecules and cell-cell communication in carcinogenesis, human stomach transformed and cancer cell lines were investigated. Expressions of E-cadherin, N-cadherin, α-catenin, β-catenin as well as gap junction (GJ) protein Cx32 were studied by utilization of immunoblotting, immunocytochemical and fluorescent dye transfer methods. Mammalian normal stomach mucosal cells expressed E-cadherin but not N-cadherin. E-cadherin immunofluorescence was detected at cell membranous adherens junctions (AJ) where colocalization with immunofluorescent staining of inner surface adhesion plaque proteins αand β-catenins was observed. The existence of E-cadherin/ catenin (α-, β-) protein complexes as AJ was suggested. In transformed and stomach cancer cells E-cadherin was inhibited, instead, N-cadherin was expressed and localized at membranous AJ where co-staining with α-and β-catenin fluorescence was observed. Formation of N-cadherin/catenin (α-, β-) protein complex at AJs of transformed and cancer cells was suggested. The above observations were further supported by immunoblotting results. Normal stomach muscosal and transformed cells expressed Cx32 at membranous GJ and were competent of gap junction communication (GJIC). In stomach cancer cells, Cx32 was inhibited and GJIC was defective. The results suggested that changes of signal pathways mediated by both cell adhesion and cell communication systems are associated intracellular events of stomach carcinogenesis. The alteration of cadherin isoform from E-to N-cadherin in transformed and stomach cancer cells is the first report.
The expression of N-cadherin /catenins /actin complex in human lung normal and carcinoma cells
Wenjun Zhang,Zhongxiang Lin,Zhiqian Zhang,Ying Hu
Chinese Science Bulletin , 1998, DOI: 10.1007/BF02898958
Abstract: The difference between human normal and carcinoma lung cells was studied with regard to the protein expression level and localization of the cadherin/catenin/actin complex. Results demonstrated that nod lung cell RF expressed high levels of N-cadherin. β-catenin, α-catenin. These 3 proteins were colocalized at AJs and their submembrane adhesion plaques where they link the Rho-phalloidin-positive actin stress fibers, indicating the existence of N-cadherin/catenin/actin complexes at the AJs Aberrant expression of AJ proteins and the actin cytoskelecton in carcinoma PG cells was observed: (1) inhibition of N-cadherin and to a degree of inhibition of α-catenin protein expression; (2) varied protein modification of β-catenin in cytoplasm soluble fraction and altered distribution of immunofluorescence: majorly in the cytoplasm and minorly on the membrane; (3) disassembly of actin stress fibers and formation of actin bodies in the cytoplasm. The data suggest that inhibited expression of AJ proteins is correlated with the disruption of the AJ complexes and the actin cytoskeleton in carcinoma PG cells, and responsible for its metastasis behaviors.
Expression of gap junctions and inhibition of cell growth in communication-defected cells after transfection with gap junction gene Cx43 cDNA
Zhiqian Zhang,Zhongxiang Lin,Naiqin Wang,Yaling Han
Chinese Science Bulletin , 1997, DOI: 10.1007/BF02884236
Abstract:
Correlation between expression of cadherin and gap junctional communication in human lung carcinoma cells
Wenjun Zhang,Zhiqian Zhang,Zhongxiang Lin,Naiqin Wang,Ying Hu
Science China Life Sciences , 1998, DOI: 10.1007/BF02882743
Abstract: The correlation between expression of ca2+-dependent cell adhesion molecule, cadherin, and gap junctional intercellular communication (GJIC) in human lung carcinoma PG cell line and connexin43 (Cx43) cDNA transfected PG cell clones was investigated. Results from immunoblotting and immunofluorescent staining revealed that cultured normal human lung cells (RF) expressed N-cadherin. However, the expression level of Kcadherin in PG cells was very low in comparison with normal RF cells. The Cx43 transfected PG clones exhibited comparable levels of Cx43 protein, but varied in the level of N-cadherin expression and in the function of GJIC as measured by scrape-loading and dye transfer (SLDT) method. Positive correlation between N-cadherin and GJIC was demonstrated. Thein vitro andin uivo, growth examination results suggest that N-cadherin mediated cell-cell adhesions and Cx43 functional expression, the GJIC, may work coordinately with each other in regulation of cell growth and differentiation. Deficiency in both GJIC and cell adhesion may be crucial for cell transformation.
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