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glycosidase/brustkrebs
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Seite 1 von 31 Ergebnisse
[Glycosidases of mammals: association of activities and changes of levels in some disorders].
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beta-Galactosidase and associated activities (beta-glucosidase and beta-fucosidase) have been studied in rabbit and bovine liver and rabbit spleen. The physico-chemical (optimal pH, pI, MW) and kinetical (Km, Vmax, Ki) properties were determined for all the activities. Two enzyme forms were
Serum beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer.
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The specific activities of several glycosidases (beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase) were determined in human sera from a control group to 10 normal subjects and in four groups, each of 10 patients,
Comparing the immunogenicity of glycosidase-directed resiquimod prodrugs mediated by cancer cell metabolism
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We have recently developed an enzyme-directed immunostimulant (EDI) prodrug motif, which is metabolized to active immunostimulant by cancer cells and, following drug efflux, activates nearby immune cells, resulting in immunogenicity. In this study, we synthesized several EDI prodrugs featuring an
Structures of the oligosaccharide chains of two forms of alpha 1-acid glycoprotein purified from liver metastases of lung, colon, and breast tumors.
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Two forms of alpha 1-acid glycoprotein with common immunological determinants and almost identical amino acid compositions but different amounts of carbohydrate were isolated from liver metastases of primary colon, lung, and breast tumors by extraction with perchloric acid, gel filtration on
Breast cancer invasion is mediated by beta-N-acetylglucosaminidase (beta-NAG) and associated with a dysregulation in the secretory pathway of cancer cells.
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The extracellular matrix is enriched with carbohydrate polymers that mask the protein backbone. This study aims to test the hypothesis that for successful cancer cell invasion the cells must secrete glycosidases to reveal the protein backbone, and then the action of proteases provides the physical
Characterization of a novel amphiregulin-related molecule in 12-O-tetradecanoylphorbol-13-acetate-treated breast cancer cells.
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Amphiregulin (AR) can be induced at the mRNA level by 17-beta-estradiol (E2) or the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA). This study compares the effects of TPA and E2 on the regulation of processing of AR isoforms and on subcellular localization in human MCF-7
Alterations in human breast cancer adhesion-motility in response to changes in cell surface glycoproteins displaying alpha-L-fucose moieties.
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Glycosylation of proteins plays multiple roles in cell-cell and cell-matrix interactions. Fucose is a monosaccharide associated with glycosylation events and is known to be over-expressed in many malignant tumors. By using alpha-L-fucosidase (alpha-L-fase), a glycosidase that specifically removes
Cell surface associated alpha-L-fucose moieties modulate human breast cancer neoplastic progression.
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Glycosylation drives critical processes important for mammalian cell-cell and cell-matrix interactions. Alpha-L-fucose (alpha-L-f) is a key monosaccharide component of oligosaccharides that has been found to be overexpressed during tumor progression. Modification of cell surface fucosylation, we
Cytotoxic effects, carbonic anhydrase isoenzymes, α-glycosidase and acetylcholinesterase inhibitory properties, and molecular docking studies of heteroatom-containing sulfonyl hydrazone derivatives
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Today, interest in studies on the search for new drugs to be used in diseases such as cancer, cardiovascular diseases, neurodegenerative diseases and diabetes, as well as prevention of microbial inflammation is increasing day by day. Emerging biological and pharmacological effects of sulfonyl
Tumor Suppressor Activity of Klotho in Breast Cancer Is Revealed by Structure-Function Analysis.
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Klotho is a transmembrane protein containing two internal repeats, KL1 and KL2, both displaying significant homology to members of the β-glycosidase family. Klotho is expressed in the kidney, brain, and various endocrine tissues, but can also be cleaved and act as a circulating hormone. Klotho is an
Unique alpha 2, 8-polysialylated glycoproteins in breast cancer and leukemia cells.
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The N-linked oligosaccharides of neural cell adhesion molecule and the rat brain voltage-dependent sodium channel alpha subunit are specifically modified by alpha 2, 8-polysialic acid chains. Until now, this carbohydrate modification has been observed only on these two proteins in mammalian cells.
A study of serum glycosidases in cancer.
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N-Acetyl-beta-glucosaminidase (NAG) and beta-glucuronidase were measured in the serum of 70 patients with breast and digestive-tract neoplasms and in 70 healthy subjects. The mean value of the NAG activity was significantly (P < 0.001) elevated in patients with gastric, liver and pancreas cancer as
Neurotensin receptor-1 inducible palmitoylation is required for efficient receptor-mediated mitogenic-signaling within structured membrane microdomains.
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Neurotensin receptor-1 (NTSR-1) is a G-protein coupled receptor (GPCR) that has been recently identified as a mediator of cancer progression. NTSR-1 and its endogenous ligand, neurotensin (NTS), are co-expressed in several breast cancer cell lines and breast cancer tumor samples. Based on our
Human milk-fat globule membrane derived mucin is a disulfide-linked heteromer.
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The human milk-fat globule membrane (HMFG) contains a number of antigens also expressed on breast tumors. The dominant antigens are a mucin of MW greater than 400,000 and a group of antigens of MW 67,000-70,000. The mucin was separated with monoclonal antibodies against HMFG and a MW 70,000 doublet
Antiproliferative and antimitogenic activities in a peptide from puffball mushroom Calvatia caelata.
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A peptide with a molecular weight of 8 kDa and an N-terminal sequence closely resembling that of ubiquitin was isolated from fruiting bodies of the mosaic puffball mushroom Calvatia caelata. The peptide was purified using a protocol that involved ion-exchange chromatography on DEAE-cellulose,
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