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  1. Article ; Online: MPDU1 regulates CEACAM1 and cell adhesion in vitro and in vivo.

    Bennett, Daniel C / Cazet, Aurelie / Charest, Jon / Contessa, Joseph N

    Glycoconjugate journal

    2018  Volume 35, Issue 3, Page(s) 265–274

    Abstract: N-linked glycosylation (NLG) is a co-translational modification that is essential for the folding, stability, and trafficking of transmembrane (TM) and secretory glycoproteins. Efficient NLG requires the stepwise synthesis and en bloc transfer of a 14- ... ...

    Abstract N-linked glycosylation (NLG) is a co-translational modification that is essential for the folding, stability, and trafficking of transmembrane (TM) and secretory glycoproteins. Efficient NLG requires the stepwise synthesis and en bloc transfer of a 14-sugar carbohydrate known as a lipid-linked oligosaccharide (LLO). The genetics of LLO biosynthesis have been established in yeast and Chinese hamster systems, but human models of LLO biosynthesis are lacking. In this study we report that Kato III human gastric cancer cells represent a model of deficient LLO synthesis, possessing a homozygous deletion of the LLO biosynthesis factor, MPDU1. Kato III cells lacking MPDU1 have all the hallmarks of a glycosylation-deficient cell line, including altered sensitivity to lectins and the formation of truncated LLOs. Analysis of transcription using an expression microarray and protein levels using a proteome antibody array reveal changes in the expression of several membrane proteins, including the metalloprotease ADAM-15 and the cell adhesion molecule CEACAM1. Surprisingly, the restoration of MPDU1 expression in Kato III cells demonstrated a clear phenotype of increased cell-cell adhesion, a finding that was confirmed in vivo through analysis of tumor xenografts. These experiments also confirmed that protein levels of CEACAM-1, which functions in cell adhesion, is dependent on LLO biosynthesis in vivo. Kato III cells and the MPDU1-rescued Kato IIIM cells therefore provide a novel model to examine the consequences of defective LLO biosynthesis both in vitro and in vivo.
    MeSH term(s) Antigens, CD/biosynthesis ; Antigens, CD/genetics ; Cell Adhesion/genetics ; Cell Adhesion Molecules/biosynthesis ; Cell Adhesion Molecules/genetics ; Cell Line, Tumor ; Gene Expression Regulation ; Glycolipids/biosynthesis ; Glycolipids/genetics ; Glycosylation ; Humans
    Chemical Substances Antigens, CD ; CD66 antigens ; Cell Adhesion Molecules ; Glycolipids
    Language English
    Publishing date 2018-04-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 283770-5
    ISSN 1573-4986 ; 0282-0080
    ISSN (online) 1573-4986
    ISSN 0282-0080
    DOI 10.1007/s10719-018-9819-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Tumor Biomechanics Alters Metastatic Dissemination of Triple Negative Breast Cancer via Rewiring Fatty Acid Metabolism.

    Filipe, Elysse C / Velayuthar, Sipiththa / Philp, Ashleigh / Nobis, Max / Latham, Sharissa L / Parker, Amelia L / Murphy, Kendelle J / Wyllie, Kaitlin / Major, Gretel S / Contreras, Osvaldo / Mok, Ellie T Y / Enriquez, Ronaldo F / McGowan, Suzanne / Feher, Kristen / Quek, Lake-Ee / Hancock, Sarah E / Yam, Michelle / Tran, Emmi / Setargew, Yordanos F I /
    Skhinas, Joanna N / Chitty, Jessica L / Phimmachanh, Monica / Han, Jeremy Z R / Cadell, Antonia L / Papanicolaou, Michael / Mahmodi, Hadi / Kiedik, Beata / Junankar, Simon / Ross, Samuel E / Lam, Natasha / Coulson, Rhiannon / Yang, Jessica / Zaratzian, Anaiis / Da Silva, Andrew M / Tayao, Michael / Chin, Ian L / Cazet, Aurélie / Kansara, Maya / Segara, Davendra / Parker, Andrew / Hoy, Andrew J / Harvey, Richard P / Bogdanovic, Ozren / Timpson, Paul / Croucher, David R / Lim, Elgene / Swarbrick, Alexander / Holst, Jeff / Turner, Nigel / Choi, Yu Suk / Kabakova, Irina V / Philp, Andrew / Cox, Thomas R

    Advanced science (Weinheim, Baden-Wurttemberg, Germany)

    2024  , Page(s) e2307963

    Abstract: In recent decades, the role of tumor biomechanics on cancer cell behavior at the primary site has been increasingly appreciated. However, the effect of primary tumor biomechanics on the latter stages of the metastatic cascade, such as metastatic seeding ... ...

    Abstract In recent decades, the role of tumor biomechanics on cancer cell behavior at the primary site has been increasingly appreciated. However, the effect of primary tumor biomechanics on the latter stages of the metastatic cascade, such as metastatic seeding of secondary sites and outgrowth remains underappreciated. This work sought to address this in the context of triple negative breast cancer (TNBC), a cancer type known to aggressively disseminate at all stages of disease progression. Using mechanically tuneable model systems, mimicking the range of stiffness's typically found within breast tumors, it is found that, contrary to expectations, cancer cells exposed to softer microenvironments are more able to colonize secondary tissues. It is shown that heightened cell survival is driven by enhanced metabolism of fatty acids within TNBC cells exposed to softer microenvironments. It is demonstrated that uncoupling cellular mechanosensing through integrin β1 blocking antibody effectively causes stiff primed TNBC cells to behave like their soft counterparts, both in vitro and in vivo. This work is the first to show that softer tumor microenvironments may be contributing to changes in disease outcome by imprinting on TNBC cells a greater metabolic flexibility and conferring discrete cell survival advantages.
    Language English
    Publishing date 2024-04-11
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2808093-2
    ISSN 2198-3844 ; 2198-3844
    ISSN (online) 2198-3844
    ISSN 2198-3844
    DOI 10.1002/advs.202307963
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Targeting the Id1-Kif11 Axis in Triple-Negative Breast Cancer Using Combination Therapy.

    Thankamony, Archana P / Murali, Reshma / Karthikeyan, Nitheesh / Varghese, Binitha Anu / Teo, Wee S / McFarland, Andrea / Roden, Daniel L / Holliday, Holly / Konrad, Christina Valbirk / Cazet, Aurelie / Dodson, Eoin / Yang, Jessica / Baker, Laura A / George, Jason T / Levine, Herbert / Jolly, Mohit Kumar / Swarbrick, Alexander / Nair, Radhika

    Biomolecules

    2020  Volume 10, Issue 9

    Abstract: The basic helix-loop-helix (bHLH) transcription factors inhibitor of differentiation 1 ( ...

    Abstract The basic helix-loop-helix (bHLH) transcription factors inhibitor of differentiation 1 (
    MeSH term(s) Animals ; Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Aurora Kinase A/antagonists & inhibitors ; Aurora Kinase A/genetics ; Aurora Kinase A/metabolism ; Benzamides/pharmacology ; Cell Cycle/genetics ; Cell Line, Tumor ; Cell Self Renewal/drug effects ; Female ; Gene Expression Regulation, Neoplastic ; Gene Knockdown Techniques ; Humans ; Inhibitor of Differentiation Protein 1/genetics ; Inhibitor of Differentiation Protein 1/metabolism ; Kinesin/antagonists & inhibitors ; Kinesin/genetics ; Kinesin/metabolism ; Mice ; Neoplastic Stem Cells/drug effects ; Paclitaxel/pharmacology ; Quinazolines/pharmacology ; Triple Negative Breast Neoplasms/drug therapy ; Triple Negative Breast Neoplasms/genetics ; Triple Negative Breast Neoplasms/metabolism
    Chemical Substances Benzamides ; ID1 protein, human ; Idb1 protein, mouse ; Inhibitor of Differentiation Protein 1 ; KIF11 protein, human ; Quinazolines ; ispinesib (BKT5F9C2NI) ; Aurka protein, mouse (EC 2.7.11.1) ; Aurora Kinase A (EC 2.7.11.1) ; Kif11 protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4) ; Paclitaxel (P88XT4IS4D)
    Language English
    Publishing date 2020-09-08
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom10091295
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Mannose phosphate isomerase regulates fibroblast growth factor receptor family signaling and glioma radiosensitivity.

    Cazet, Aurélie / Charest, Jonathan / Bennett, Daniel C / Sambrooks, Cecilia Lopez / Contessa, Joseph N

    PloS one

    2014  Volume 9, Issue 10, Page(s) e110345

    Abstract: Asparagine-linked glycosylation is an endoplasmic reticulum co- and post-translational modification that enables the transit and function of receptor tyrosine kinase (RTK) glycoproteins. To gain insight into the regulatory role of glycosylation enzymes ... ...

    Abstract Asparagine-linked glycosylation is an endoplasmic reticulum co- and post-translational modification that enables the transit and function of receptor tyrosine kinase (RTK) glycoproteins. To gain insight into the regulatory role of glycosylation enzymes on RTK function, we investigated shRNA and siRNA knockdown of mannose phosphate isomerase (MPI), an enzyme required for mature glycan precursor biosynthesis. Loss of MPI activity reduced phosphorylation of FGFR family receptors in U-251 and SKMG-3 malignant glioma cell lines and also resulted in significant decreases in FRS2, Akt, and MAPK signaling. However, MPI knockdown did not affect ligand-induced activation or signaling of EGFR or MET RTKs, suggesting that FGFRs are more susceptible to MPI inhibition. The reductions in FGFR signaling were not caused by loss of FGF ligands or receptors, but instead were caused by interference with receptor dimerization. Investigations into the cellular consequences of MPI knockdown showed that cellular programs driven by FGFR signaling, and integral to the clinical progression of malignant glioma, were impaired. In addition to a blockade of cellular migration, MPI knockdown also significantly reduced glioma cell clonogenic survival following ionizing radiation. Therefore our results suggest that targeted inhibition of enzymes required for cell surface receptor glycosylation can be manipulated to produce discrete and limited consequences for critical client glycoproteins expressed by tumor cells. Furthermore, this work identifies MPI as a potential enzymatic target for disrupting cell surface receptor-dependent survival signaling and as a novel approach for therapeutic radiosensitization.
    MeSH term(s) Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Movement/genetics ; Cell Proliferation ; Gene Knockdown Techniques ; Glioma/genetics ; Glioma/metabolism ; Glioma/radiotherapy ; Humans ; Mannose-6-Phosphate Isomerase/genetics ; Mannose-6-Phosphate Isomerase/metabolism ; Protein Multimerization ; Protein Transport ; RNA, Small Interfering ; Radiation Tolerance/genetics ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, Fibroblast Growth Factor, Type 2/chemistry ; Receptor, Fibroblast Growth Factor, Type 2/genetics ; Receptor, Fibroblast Growth Factor, Type 2/metabolism ; Receptors, Fibroblast Growth Factor/chemistry ; Receptors, Fibroblast Growth Factor/genetics ; Receptors, Fibroblast Growth Factor/metabolism ; Signal Transduction
    Chemical Substances RNA, Small Interfering ; Receptors, Fibroblast Growth Factor ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Receptor, Fibroblast Growth Factor, Type 2 (EC 2.7.10.1) ; Mannose-6-Phosphate Isomerase (EC 5.3.1.8)
    Language English
    Publishing date 2014-10-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0110345
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Tumour-associated carbohydrate antigens in breast cancer.

    Cazet, Aurélie / Julien, Sylvain / Bobowski, Marie / Burchell, Joy / Delannoy, Philippe

    Breast cancer research : BCR

    2010  Volume 12, Issue 3, Page(s) 204

    Abstract: Glycosylation changes that occur in cancer often lead to the expression of tumour-associated carbohydrate antigens. In breast cancer, these antigens are usually associated with a poor prognosis and a reduced overall survival. Cellular models have shown ... ...

    Abstract Glycosylation changes that occur in cancer often lead to the expression of tumour-associated carbohydrate antigens. In breast cancer, these antigens are usually associated with a poor prognosis and a reduced overall survival. Cellular models have shown the implication of these antigens in cell adhesion, migration, proliferation and tumour growth. The present review summarizes our current knowledge of glycosylation changes (structures, biosynthesis and occurrence) in breast cancer cell lines and primary tumours, and the consequences on disease progression and aggressiveness. The therapeutic strategies attempted to target tumour-associated carbohydrate antigens in breast cancer are also discussed.
    MeSH term(s) Antigens, Tumor-Associated, Carbohydrate/metabolism ; Breast Neoplasms/metabolism ; Female ; Humans ; Prognosis
    Chemical Substances Antigens, Tumor-Associated, Carbohydrate
    Language English
    Publishing date 2010-06-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2015059-3
    ISSN 1465-542X ; 1465-5411
    ISSN (online) 1465-542X
    ISSN 1465-5411
    DOI 10.1186/bcr2577
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The Hedgehog signalling pathway in breast development, carcinogenesis and cancer therapy.

    Hui, Mun / Cazet, Aurélie / Nair, Radhika / Watkins, D Neil / O'Toole, Sandra A / Swarbrick, Alexander

    Breast cancer research : BCR

    2013  Volume 15, Issue 2, Page(s) 203

    Abstract: Despite the progress achieved in breast cancer screening and therapeutic innovations, the basal-like subtype of breast cancer (BLBC) still represents a particular clinical challenge. In order to make an impact on survival in this type of aggressive ... ...

    Abstract Despite the progress achieved in breast cancer screening and therapeutic innovations, the basal-like subtype of breast cancer (BLBC) still represents a particular clinical challenge. In order to make an impact on survival in this type of aggressive breast cancer, new targeted therapeutic agents are urgently needed. Aberrant activation of the Hedgehog (Hh) signalling pathway has been unambiguously tied to cancer development and progression in a variety of solid malignancies, and the recent approval of vismodegib, an orally bioavailable small-molecule inhibitor of Smoothened, validates Hh signalling as a valuable therapeutic target. A number of recent publications have highlighted a role for Hh signalling in breast cancer models and clinical specimens. Interestingly, Hh ligand overexpression is associated with the BLBC phenotype and a poor outcome in terms of metastasis and breast cancer-related death. In this review, we provide a comprehensive overview of the canonical Hh signalling pathway in mammals, highlight its roles in mammary gland development and breast carcinogenesis and discuss its potential therapeutic value in BLBC.
    MeSH term(s) Antineoplastic Agents/therapeutic use ; Breast Neoplasms/drug therapy ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Transformation, Neoplastic/drug effects ; Cell Transformation, Neoplastic/metabolism ; Cell Transformation, Neoplastic/pathology ; Female ; Hedgehog Proteins/metabolism ; Humans ; Molecular Targeted Therapy ; Signal Transduction/drug effects
    Chemical Substances Antineoplastic Agents ; Hedgehog Proteins
    Language English
    Publishing date 2013-03-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2015059-3
    ISSN 1465-542X ; 1465-5411
    ISSN (online) 1465-542X
    ISSN 1465-5411
    DOI 10.1186/bcr3401
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Mannose phosphate isomerase regulates fibroblast growth factor receptor family signaling and glioma radiosensitivity.

    Aurélie Cazet / Jonathan Charest / Daniel C Bennett / Cecilia Lopez Sambrooks / Joseph N Contessa

    PLoS ONE, Vol 9, Iss 10, p e

    2014  Volume 110345

    Abstract: Asparagine-linked glycosylation is an endoplasmic reticulum co- and post-translational modification that enables the transit and function of receptor tyrosine kinase (RTK) glycoproteins. To gain insight into the regulatory role of glycosylation enzymes ... ...

    Abstract Asparagine-linked glycosylation is an endoplasmic reticulum co- and post-translational modification that enables the transit and function of receptor tyrosine kinase (RTK) glycoproteins. To gain insight into the regulatory role of glycosylation enzymes on RTK function, we investigated shRNA and siRNA knockdown of mannose phosphate isomerase (MPI), an enzyme required for mature glycan precursor biosynthesis. Loss of MPI activity reduced phosphorylation of FGFR family receptors in U-251 and SKMG-3 malignant glioma cell lines and also resulted in significant decreases in FRS2, Akt, and MAPK signaling. However, MPI knockdown did not affect ligand-induced activation or signaling of EGFR or MET RTKs, suggesting that FGFRs are more susceptible to MPI inhibition. The reductions in FGFR signaling were not caused by loss of FGF ligands or receptors, but instead were caused by interference with receptor dimerization. Investigations into the cellular consequences of MPI knockdown showed that cellular programs driven by FGFR signaling, and integral to the clinical progression of malignant glioma, were impaired. In addition to a blockade of cellular migration, MPI knockdown also significantly reduced glioma cell clonogenic survival following ionizing radiation. Therefore our results suggest that targeted inhibition of enzymes required for cell surface receptor glycosylation can be manipulated to produce discrete and limited consequences for critical client glycoproteins expressed by tumor cells. Furthermore, this work identifies MPI as a potential enzymatic target for disrupting cell surface receptor-dependent survival signaling and as a novel approach for therapeutic radiosensitization.
    Keywords Medicine ; R ; Science ; Q
    Subject code 572
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Carbohydrate-to-carbohydrate interactions between α2,3-linked sialic acids on α2 integrin subunits and asialo-GM1 underlie the bone metastatic behaviour of LNCAP-derivative C4-2B prostate cancer cells.

    Van Slambrouck, Séverine / Groux-Degroote, Sophie / Krzewinski-Recchi, Marie-Ange / Cazet, Aurélie / Delannoy, Philippe / Steelant, Wim F A

    Bioscience reports

    2014  Volume 34, Issue 5

    Abstract: Complex interplays among proteins, lipids and carbohydrates can alter the phenotype and are suggested to have a crucial role in tumour metastasis. Our previous studies indicated that a complex of the GSLs (glycosphingolipids), AsGM1 (asialo-GM1), which ... ...

    Abstract Complex interplays among proteins, lipids and carbohydrates can alter the phenotype and are suggested to have a crucial role in tumour metastasis. Our previous studies indicated that a complex of the GSLs (glycosphingolipids), AsGM1 (asialo-GM1), which lacks α2,3-linked sialic acid, and α2β1 integrin receptors is responsible for the metastatic behaviour of C4-2B prostate cancer cells. Herein, we identified and addressed the functional significance of changes in sialylation during prostate cancer progression. We observed an increase in α2,3-linked sialic acid residues on α2 subunits of α2β1 integrin receptors, correlating with increased gene expression of α2,3-STs (sialyltransferases), particularly ST3GAL3. Cell surface α2,3-sialylation of α2 subunits was required for the integrin α2β1-dependent cell adhesion to collagen type I and the same α2,3-linked sialic acid residues on the integrin receptor were responsible for the interaction with the carbohydrate moiety of AsGM1, explaining the complex formation between AsGM1 and α2β1 integrin receptors. These results provide novel insights into the role of sialic acids in the organization and function of important membrane components in invasion and metastatic processes.
    MeSH term(s) Bone Neoplasms/genetics ; Bone Neoplasms/metabolism ; Bone Neoplasms/pathology ; Bone Neoplasms/secondary ; Cell Line, Tumor ; G(M1) Ganglioside/genetics ; G(M1) Ganglioside/metabolism ; Humans ; Integrin alpha2/genetics ; Integrin alpha2/metabolism ; Male ; Neoplasm Metastasis ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/metabolism ; Prostatic Neoplasms/pathology ; Sialic Acids/genetics ; Sialic Acids/metabolism
    Chemical Substances Integrin alpha2 ; Sialic Acids ; G(M1) Ganglioside (37758-47-7) ; asialo GM1 ganglioside (71012-19-6)
    Language English
    Publishing date 2014-09-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 764946-0
    ISSN 1573-4935 ; 0144-8463
    ISSN (online) 1573-4935
    ISSN 0144-8463
    DOI 10.1042/BSR20140096
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Cryopreservation of human cancers conserves tumour heterogeneity for single-cell multi-omics analysis.

    Wu, Sunny Z / Roden, Daniel L / Al-Eryani, Ghamdan / Bartonicek, Nenad / Harvey, Kate / Cazet, Aurélie S / Chan, Chia-Ling / Junankar, Simon / Hui, Mun N / Millar, Ewan A / Beretov, Julia / Horvath, Lisa / Joshua, Anthony M / Stricker, Phillip / Wilmott, James S / Quek, Camelia / Long, Georgina V / Scolyer, Richard A / Yeung, Bertrand Z /
    Segara, Davendra / Mak, Cindy / Warrier, Sanjay / Powell, Joseph E / O'Toole, Sandra / Lim, Elgene / Swarbrick, Alexander

    Genome medicine

    2021  Volume 13, Issue 1, Page(s) 81

    Abstract: Background: High throughput single-cell RNA sequencing (scRNA-Seq) has emerged as a powerful tool for exploring cellular heterogeneity among complex human cancers. scRNA-Seq studies using fresh human surgical tissue are logistically difficult, preclude ... ...

    Abstract Background: High throughput single-cell RNA sequencing (scRNA-Seq) has emerged as a powerful tool for exploring cellular heterogeneity among complex human cancers. scRNA-Seq studies using fresh human surgical tissue are logistically difficult, preclude histopathological triage of samples, and limit the ability to perform batch processing. This hindrance can often introduce technical biases when integrating patient datasets and increase experimental costs. Although tissue preservation methods have been previously explored to address such issues, it is yet to be examined on complex human tissues, such as solid cancers and on high throughput scRNA-Seq platforms.
    Methods: Using the Chromium 10X platform, we sequenced a total of ~ 120,000 cells from fresh and cryopreserved replicates across three primary breast cancers, two primary prostate cancers and a cutaneous melanoma. We performed detailed analyses between cells from each condition to assess the effects of cryopreservation on cellular heterogeneity, cell quality, clustering and the identification of gene ontologies. In addition, we performed single-cell immunophenotyping using CITE-Seq on a single breast cancer sample cryopreserved as solid tissue fragments.
    Results: Tumour heterogeneity identified from fresh tissues was largely conserved in cryopreserved replicates. We show that sequencing of single cells prepared from cryopreserved tissue fragments or from cryopreserved cell suspensions is comparable to sequenced cells prepared from fresh tissue, with cryopreserved cell suspensions displaying higher correlations with fresh tissue in gene expression. We showed that cryopreservation had minimal impacts on the results of downstream analyses such as biological pathway enrichment. For some tumours, cryopreservation modestly increased cell stress signatures compared to freshly analysed tissue. Further, we demonstrate the advantage of cryopreserving whole-cells for detecting cell-surface proteins using CITE-Seq, which is impossible using other preservation methods such as single nuclei-sequencing.
    Conclusions: We show that the viable cryopreservation of human cancers provides high-quality single-cells for multi-omics analysis. Our study guides new experimental designs for tissue biobanking for future clinical single-cell RNA sequencing studies.
    MeSH term(s) Biological Specimen Banks ; Biomarkers, Tumor ; Cryopreservation/methods ; Cryopreservation/standards ; Gene Expression Profiling/methods ; Gene Expression Regulation ; Genomics/methods ; High-Throughput Nucleotide Sequencing ; Humans ; Immunophenotyping ; Neoplasms/diagnosis ; Neoplasms/etiology ; Organ Specificity/genetics ; Sequence Analysis, RNA/methods ; Signal Transduction ; Single-Cell Analysis/methods
    Chemical Substances Biomarkers, Tumor
    Language English
    Publishing date 2021-05-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2484394-5
    ISSN 1756-994X ; 1756-994X
    ISSN (online) 1756-994X
    ISSN 1756-994X
    DOI 10.1186/s13073-021-00885-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Copper-free click chemistry for highly luminescent quantum dot conjugates: application to in vivo metabolic imaging.

    Bernardin, Aude / Cazet, Aurélie / Guyon, Laurent / Delannoy, Philippe / Vinet, Françoise / Bonnaffé, David / Texier, Isabelle

    Bioconjugate chemistry

    2010  Volume 21, Issue 4, Page(s) 583–588

    Abstract: Quantum dots (QD) are inorganic nanocrystals with outstanding optical properties, specially suited for biological imaging applications. Their attachment to biomolecules in mild aqueous conditions for the design of bioconjugates is therefore highly ... ...

    Abstract Quantum dots (QD) are inorganic nanocrystals with outstanding optical properties, specially suited for biological imaging applications. Their attachment to biomolecules in mild aqueous conditions for the design of bioconjugates is therefore highly desirable. 1,3-dipolar [3 + 2] cycloaddition between azides and terminal alkynes ("click chemistry") could represent an attractive QD functionalization method. Unfortunately, the use of the popular Cu(I)-catalyzed version of this reaction is not applicable for achieving this goal, since the presence of copper dramatically alters the luminescence properties of QD dispersions. We demonstrate here that copper-free click chemistry, between strained cyclooctyne functionalized QD and azido-biomolecules, leads to highly luminescent conjugates. In addition, we show that QD-cyclooctyne can be used at previously unreported low concentration (250 nM) for imaging the incorporation of azido-modified sialic acid in cell membrane glycoproteins.
    MeSH term(s) Alkynes/chemistry ; Animals ; Azides/chemistry ; Azides/metabolism ; CHO Cells ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Copper/chemistry ; Cricetinae ; Cricetulus ; Luminescence ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/metabolism ; Molecular Imaging/methods ; N-Acetylneuraminic Acid/chemistry ; N-Acetylneuraminic Acid/metabolism ; Quantum Dots
    Chemical Substances Alkynes ; Azides ; Membrane Glycoproteins ; Copper (789U1901C5) ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2010-04-21
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1024041-x
    ISSN 1520-4812 ; 1043-1802
    ISSN (online) 1520-4812
    ISSN 1043-1802
    DOI 10.1021/bc900564w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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