1,354,860 research outputs found

    Influence of components of tumour microenvironment on the response of HCT-116 colorectal cancer to the ruthenium-based drug NAMI-A

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    Solid tumours are constituted of tumour cells, healthy cells recruited from the host tissues and soluble factors released by both these cell types. The present investigation examines the capacity of co-cultures between the HCEC colon epithelial cells and the HCT-116 colorectal cancer cells (mimicking the primary site of tumour growth) and between IHH hepatocytes and the HCT-116 colorectal cancer cells (metastatic site) to influence the effects of NAMI-A (imidazolium trans-imidazoledimethylsulphoxidetetrachloro ruthenate) on the tumour cells themselves. The growth of HCT-116 cells is significantly influenced when the cancer cells are sown on a monolayer of HCEC. The release of soluble factors by the healthy cells promotes, in HCT-116 colorectal cancer cells, the transcription of genes involved in growth, invasion and migration. NAMI-A is not cytotoxic to HCT-116 cells grown on plastics or co-cultured with HCEC or IHH cells, and maintains its ability to control the cell pseudo-metastatic ability, mimicked by the migration in the scratch test. The effects of NAMI-A on HCT-116 migration are supported by its inhibition of the transcription of the ABL-2, ATF-3 and RND-1 genes. In conclusion the study highlights the need of test systems more complex than a single cancer cell culture to study an anticancer drug in vitro and reinforces the hypothesis that NAMI-A targets the ability of the cancer cell to interact with the tumour microenvironment and with the signals that support its metastatic ability

    Chambery

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    This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete. Visit this record in UMA's new catalogue at: https://archives.library.unimelb.edu.au/nodes/view/301689318931 Sub-item: [2005.0036.00220] "Chambery

    Chambery

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    This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete. Visit this record in UMA's new catalogue at: https://archives.library.unimelb.edu.au/nodes/view/301690318932 Sub-item: [2005.0036.00221] "Chambery

    Chambery

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    This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete. Visit this record in UMA's new catalogue at: https://archives.library.unimelb.edu.au/nodes/view/301686318928 Sub-item: [2005.0036.00217] "Chambery

    Copper(I)-Catalyzed Azide-Alkyne Cycloadditions in Ionic Liquids under Amine-Free Conditions

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    Copper(I) iodide catalyzed cycloadditions of various combinations of structurally diverse organic azides and terminal alkynes were carried out in a commercially available, polyoxygenated ionic liquid (AMMOENG 100 (TM)) without addition of free amine. Unlike the previously tested ionic liquids, this solvent led exclusively to the 1,4-disubstituted triazole regioisomer

    Free-radical hydrothiolation of glycals: a thiol-ene-based synthesis of S-disaccharides

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    A method for the synthesis of a new family of 1-deoxy S-disaccharides has been established via free-radical hydrothiolation of glycals by sugar thiols (thiol-ene coupling). The photoinduced coupling between four tri-O-acetyl-D-glycals and three different sugar thiols reveals that the reaction efficiency and stereoselectivity are highly dependent on the stereochemistry of the OAc groups at C3 and C4 of the glycal. (C) 2011 Elsevier Ltd. All rights reserved

    Single and dual glycoside clustering around calix[4]arene scaffolds via click Thiol-ene coupling and azide-alkyne cycloaddition

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    We present the first synthesis of calix[4]arene-based S-glycoclusters via photoinduced multiple thiol-ene coupling of tetra- and octa-allyl calix[4]arenes with peracetylated glucosyl thiol (67-88% yields). Moreover we describe the dual clustering at the upper and lower rim of a calix[4]arene with two different sugars (galactose and glucose) via sequential copper(i)-catalyzed azide-alkyne cycloaddition and photoinduced thiol-ene coupling. © 2009 The Royal Society of Chemistry

    Structural analysis of toxic volkensin, a type 2 ribosome inactivating protein from Adenia volkensii Harm (kilyambiti plant): Molecular modeling and surface analysis by computational methods and limited proteolysis

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    Volkensin, isolated from Adenia volkensii, is one of the most toxic type 2 ribosome-inactivating protein (RIP), exerting its biological function by inhibiting protein synthesis. Despite the high sequence identity with type 2 RIPs, including ricin, volkensin shows interesting peculiar properties. In this work a computational model building of volkensin was performed. The volkensin electrostatic potential charge distribution, the hydrophobic profile and the surface topology analyses were also carried out to aid the understanding of structure-function relationships of this potent toxin. Volkensin surface topology was probed by applying a limited proteolysis approach with the aim to gain insights into volkensin conformational features. (C) 2009 Elsevier B.V. All rights reserved

    Primary structure and glycan moiety characterization of PD-Ss, type 1 ribosome-inactivating proteins from Phytolacca dioica L. seeds, by precursor ion discovery on a Q-TOF mass spectrometer

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    Seeds from Phytolacca dioica L. contain at least three N-glycosylated PD-Ss, type 1 ribosome-inactivating proteins (RIPs), which were separated and purified to homogeneity by conventional chromatographic techniques. ESI-Q-TOF mass spectrometry provided the accurate Mr of native PD-S1 and PD-S3 (30957.1 and 29785.1, respectively) and the major form PD-S2 (30753.8). As the amino acid sequence of PD-S2 was already known, its disulfide pairing was determined and found to be Cys34-Cys262 and Cys88-Cys110. Further structural characterization of PD-S1 and PD-S3 (N-terminal sequence determination up to residue 30, amino acid analysis and tryptic peptide mapping) showed that the three PD-Ss shared the entire protein sequence. To explain the different chromatographic behaviour, their glycosylation patterns were characterized by a fast and sensitive mass spectrometry-based approach, applying a precursor ion discovery mode on a Q-TOF mass spectrometer. A standard plant paucidomannosidic N-glycosylation pattern [Hex3, HexNAc2, deoxyhexose1, pentose1] was found for PD-S1 and PD-S2 on Asn120. Furthermore, a glycosylation site carrying only a HexNAc residue was identified on Asn112 in PD-S1 and PD-S3. Finally, considering the two disulfide bridges and the glycan moieties, the experimental Mr values were in agreement with the mass values calculated from the primary structure. The complete characterization of PD-Ss shows the high potential of mass spectrometry to rapidly characterize proteins, widespread in eukaryotes, differing only in their glycosylation motifs. © 2008 Elsevier Ltd. All rights reserved
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