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griffonia simplicifolia/kanker
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Lectin microarray technology identifies specific lectins related to lymph node metastasis of advanced gastric cancer.
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BACKGROUND
Although various molecular profiling technologies have the potential to predict specific tumor phenotypes, the comprehensive profiling of lectin-bound glycans in human cancer tissues has not yet been achieved.
METHODS
We examined 242 advanced gastric cancer (AGC) patients without or with
Inhibition of Ehrlich ascites tumor cell growth by Griffonia simplicifolia I lectin in vivo.
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Griffonia (Bandeiraea) simplicifolia I (GS I) seeds contain a family of alpha-D-galactopyranosyl-binding isolectins which strongly agglutinate Ehrlich ascites tumor cells due to the presence of this determinant sugar on their cell surface glycoproteins. Administration of GS I lectin (100
Glycopeptides from murine teratocarcinoma cells: structure of the determinants recognised by Griffonia simplicifolia agglutinin I and by sera from patients with ovarian germ cell tumors.
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High-molecular-weight glycopeptides synthesised by teratocarcinoma OTT6050 bear the binding site for Griffonia simplicifolia agglutinin I and are recognised by antibodies in the sera of patients with ovarian germ cell tumors. Digestion of the glycopeptides with endo-beta-D-galactosidase C abolished
The concurrent expression of Griffonia simplicifolia-IB4 binding and tumor necrosis factor-alpha differs between alveolar and peritoneal macrophages.
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As a corollary to their anatomic location, alveolar macrophages (AM) have a lower threshold for generating some physiologic functions than peritoneal macrophages (PM). In this study, we examined both of these populations for their ability to bind the lectin Griffonia simplicifolia-IB4 (GSIB4) and to
Immunocytochemical identification of myoepithelial cells in normal and neoplastic rat mammary glands with the lectins Griffonia simplicifolia-1 and pokeweed mitogen.
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Peroxidase-conjugated Griffonia simplicifolia-1 (GS-1) and pokeweed mitogen (PWM) histochemically stain only the myoepithelial cells and not the epithelial or fibroblastic cells of rat mammary glands preserved in methacarn or glutaraldehyde and embedded in paraffin. This pattern of staining occurs
Use of lectin histochemistry in pancreatic cancer.
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Lectin peroxidase histochemical analysis was carried out on pancreatic tissue from patients with pancreatic carcinoma and chronic pancreatitis and from subjects with normal pancreas to find a tumour specific pattern of lectin binding that would aid histological and cytological diagnosis. There were
Lectin staining of neoplastic and normal background colorectal mucosa in nonpolyposis and polyposis patients.
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A lectin histochemistry approach was adopted for comparative assessment of a colon cancer risk. Binding of Ulex europaeus agglutinin-I (UEA-I), peanut agglutinin (PNA), Griffonia simplicifolia agglutinin-II (GSA-II), and Dolichos biflorus agglutinin (DBA) was investigated in tumor and background
Appearance of Ulex europaeus agglutinin-1 and Griffonia simplicifolia agglutinin-1 binding sites on cancer cells in sigmo-rectal polyps.
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Ninety-three polypectomized cases from the sigmo-rectal region were examined by lectin histochemistry. On the apical surface, the UEA-1 binding sites were positive in 24/29 carcinomas and in 25/62 adenomas; while the GSA-1 binding sites were positive in 16/29 carcinomas and in 0/62 adenomas. In 2
Cause and effect between concentration-dependent tissue damage and temporary cell proliferation in rat stomach mucosa by NaCl, a stomach tumor promoter.
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This study was designed to test whether concentration or dose of NaCl was responsible for the initial tissue damage (after 1 min) and resulting temporary cell proliferation at 17 h in stomach mucosa of male F344 rats after gastric intubation of 0.65, 1.3, 2.6 and 3.7 M NaCl. Histological damage was
Formalin-fixed macrophages bind tumor targets similarly to viable macrophages.
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Macrophages (MPs) fixed with 1% formalin in PBS bound targets similarly to viable MPs. Like binding between viable MPs and tumor cells, the process was temperature and calcium dependent. Fixed MPs discriminated targets similarly to viable MPs. Targets not bound by viable MPs were not bound by fixed
Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing alpha-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell alpha(1,3)-galactosyltransferase.
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The ability of Ehrlich tumor cell alpha(1,3)-galactosyltransferase to catalyze the incorporation of alpha-D-Gal residues into a specific branch of bi-, tri-, and tetraantennary oligosaccharides has been investigated by acetolysis followed by gel filtration of the fragments on Bio-Gel P-4. Taking
A new test to measure homotypic aggregation of human tumour cells.
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A method is described for quantitative measurements of homotypic aggregation by sequential passaging of cells through several gauze nets with different mesh width. This method allows rapid and simple determination of the size distribution of the formed aggregates with little cost. Time course and
Histochemical study of lectin binding in neoplastic and non-neoplastic urothelium.
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A histochemical study of lectin binding was performed to assess staining with lectins and, therefore, the expression of complex carbohydrates in human neoplastic urothelium. Forty-seven patients with transitional cell carcinoma of the bladder and six controls were studied. Cryostat sections were
Isolation and characterization of a family of alpha-D-galactosyl-containing glycopeptides from Ehrlich ascites tumor cells.
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A family of glycopeptides that contain nonreducing terminal alpha-D-galactosyl residues has been isolated from Pronase digests of delipidated Ehrlich ascites tumor cells. The glycopeptides, which comprise 17.2% of the total plasma membrane hexose, have an average molecular weight of 7500 and are
Increased galectin-3 expression in gastric cancer: correlations with histopathological subtypes, galactosylated antigens and tumor cell proliferation.
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Galectin-3 represents an endogenous galactoside-binding lectin which may be involved in tumor cell adhesion and proliferation. In order to evaluate its biological significance in human gastric cancer, we investigated its expression in the stomach of a large series of patients (n = 193) by
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