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  1. Article: Extracellular Vesicles and Cell Pathways Involved in Cancer Chemoresistance.

    Console, Lara / Scalise, Mariafrancesca

    Life (Basel, Switzerland)

    2022  Volume 12, Issue 5

    Abstract: Chemoresistance is a pharmacological condition that allows transformed cells to maintain their proliferative phenotype in the presence of administered anticancer drugs. Recently, extracellular vesicles, including exosomes, have been identified as ... ...

    Abstract Chemoresistance is a pharmacological condition that allows transformed cells to maintain their proliferative phenotype in the presence of administered anticancer drugs. Recently, extracellular vesicles, including exosomes, have been identified as additional players responsible for the chemoresistance of cancer cells. These are nanovesicles that are released by almost all cell types in both physiological and pathological conditions and contain proteins and nucleic acids as molecular cargo. Extracellular vesicles released in the bloodstream reach recipient cells and confer them novel metabolic properties. Exosomes can foster chemoresistance by promoting prosurvival and antiapoptotic pathways, affecting cancer stem cells and immunotherapies, and stimulating drug efflux. In this context, a crucial role is played by membrane transporters belonging to ABC, SLC, and P-type pump families. These proteins are fundamental in cell metabolism and drug transport in either physiological or pathological conditions. In this review, different roles of extracellular vesicles in drug resistance of cancer cells will be explored.
    Language English
    Publishing date 2022-04-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2662250-6
    ISSN 2075-1729
    ISSN 2075-1729
    DOI 10.3390/life12050618
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Extracellular Vesicles and Cell Pathways Involved in Cancer Chemoresistance

    Lara Console / Mariafrancesca Scalise

    Life, Vol 12, Iss 618, p

    2022  Volume 618

    Abstract: Chemoresistance is a pharmacological condition that allows transformed cells to maintain their proliferative phenotype in the presence of administered anticancer drugs. Recently, extracellular vesicles, including exosomes, have been identified as ... ...

    Abstract Chemoresistance is a pharmacological condition that allows transformed cells to maintain their proliferative phenotype in the presence of administered anticancer drugs. Recently, extracellular vesicles, including exosomes, have been identified as additional players responsible for the chemoresistance of cancer cells. These are nanovesicles that are released by almost all cell types in both physiological and pathological conditions and contain proteins and nucleic acids as molecular cargo. Extracellular vesicles released in the bloodstream reach recipient cells and confer them novel metabolic properties. Exosomes can foster chemoresistance by promoting prosurvival and antiapoptotic pathways, affecting cancer stem cells and immunotherapies, and stimulating drug efflux. In this context, a crucial role is played by membrane transporters belonging to ABC, SLC, and P-type pump families. These proteins are fundamental in cell metabolism and drug transport in either physiological or pathological conditions. In this review, different roles of extracellular vesicles in drug resistance of cancer cells will be explored.
    Keywords exosomes ; cancer ; membrane transporters ; SLC ; ABC ; chemoresistance ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2022-04-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Editorial: Transport of Nutrients, Metabolites and Ions linked to Bioenergetics: Relevance to Human Pathology, Volume II.

    Scalise, Mariafrancesca / Koprowski, Piotr / Indiveri, Cesare

    Frontiers in molecular biosciences

    2022  Volume 9, Page(s) 957599

    Language English
    Publishing date 2022-08-17
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2022.957599
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Inflammation and Organic Cation Transporters Novel (OCTNs).

    Pochini, Lorena / Galluccio, Michele / Console, Lara / Scalise, Mariafrancesca / Eberini, Ivano / Indiveri, Cesare

    Biomolecules

    2024  Volume 14, Issue 4

    Abstract: Inflammation is a physiological condition characterized by a complex interplay between different cells handled by metabolites and specific inflammatory-related molecules. In some pathological situations, inflammation persists underlying and worsening the ...

    Abstract Inflammation is a physiological condition characterized by a complex interplay between different cells handled by metabolites and specific inflammatory-related molecules. In some pathological situations, inflammation persists underlying and worsening the pathological state. Over the years, two membrane transporters namely OCTN1 (SLC22A4) and OCTN2 (SLC22A5) have been shown to play specific roles in inflammation. These transporters form the OCTN subfamily within the larger SLC22 family. The link between these proteins and inflammation has been proposed based on their link to some chronic inflammatory diseases such as asthma, Crohn's disease (CD), and rheumatoid arthritis (RA). Moreover, the two transporters show the ability to mediate the transport of several compounds including carnitine, carnitine derivatives, acetylcholine, ergothioneine, and gut microbiota by-products, which have been specifically associated with inflammation for their anti- or proinflammatory action. Therefore, the absorption and distribution of these molecules rely on the presence of OCTN1 and OCTN2, whose expression is modulated by inflammatory cytokines and transcription factors typically activated by inflammation. In the present review, we wish to provide a state of the art on OCTN1 and OCTN2 transport function and regulation in relationships with inflammation and inflammatory diseases focusing on the metabolic signature collected in different body districts and gene polymorphisms related to inflammatory diseases.
    MeSH term(s) Humans ; Inflammation/metabolism ; Solute Carrier Family 22 Member 5/metabolism ; Solute Carrier Family 22 Member 5/genetics ; Animals ; Organic Cation Transport Proteins/metabolism ; Organic Cation Transport Proteins/genetics ; Ergothioneine/metabolism ; Crohn Disease/metabolism ; Crohn Disease/genetics ; Crohn Disease/pathology ; Arthritis, Rheumatoid/metabolism ; Arthritis, Rheumatoid/genetics ; Gastrointestinal Microbiome ; Carnitine/metabolism ; Asthma/metabolism ; Asthma/genetics ; Acetylcholine/metabolism ; Symporters
    Chemical Substances Solute Carrier Family 22 Member 5 ; SLC22A4 protein, human ; SLC22A5 protein, human ; Organic Cation Transport Proteins ; Ergothioneine (BDZ3DQM98W) ; Carnitine (S7UI8SM58A) ; Acetylcholine (N9YNS0M02X) ; Symporters
    Language English
    Publishing date 2024-03-25
    Publishing country Switzerland
    Document type Journal Article ; Review ; 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/biom14040392
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Editorial

    Mariafrancesca Scalise / Piotr Koprowski / Cesare Indiveri

    Frontiers in Molecular Biosciences, Vol

    Transport of Nutrients, Metabolites and Ions linked to Bioenergetics: Relevance to Human Pathology, Volume II

    2022  Volume 9

    Keywords membrane transport ; pathology ; human health ; channels ; cell biology ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-08-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Inhibition of the Mitochondrial Carnitine/Acylcarnitine Carrier by Itaconate through Irreversible Binding to Cysteine 136: Possible Pathophysiological Implications.

    Giangregorio, Nicola / Tonazzi, Annamaria / Console, Lara / Scalise, Mariafrancesca / Indiveri, Cesare

    Biomolecules

    2023  Volume 13, Issue 6

    Abstract: Background: The carnitine/acylcarnitine carrier (CAC) represents the route of delivering acyl moieties to the mitochondrial matrix for accomplishing the fatty acid β-oxidation. The CAC has a couple of Cys residues (C136 and C155) most reactive toward ... ...

    Abstract Background: The carnitine/acylcarnitine carrier (CAC) represents the route of delivering acyl moieties to the mitochondrial matrix for accomplishing the fatty acid β-oxidation. The CAC has a couple of Cys residues (C136 and C155) most reactive toward ROS and redox signaling compounds such as GSH, NO, and H
    Methods: the modulatory effects of itaconate on the transport activity of the native and recombinant CAC were tested using the proteoliposome experimental model together with site-directed mutagenesis and computational analysis.
    Results: Itaconate reacts with the CAC causing irreversible inhibition. Dose-response experiment performed with the native and recombinant protein showed IC
    MeSH term(s) Humans ; Carnitine/metabolism ; Cysteine/metabolism ; HeLa Cells/drug effects ; Membrane Transport Proteins/drug effects ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Membrane Transport Modulators/pharmacology
    Chemical Substances acylcarnitine ; Carnitine (S7UI8SM58A) ; Cysteine (K848JZ4886) ; itaconic acid (Q4516562YH) ; Membrane Transport Proteins ; SLC25A20 protein, human (EC 2.3.1.) ; Membrane Transport Modulators
    Language English
    Publishing date 2023-06-15
    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/biom13060993
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Editorial: Transport of Nutrients, Metabolites and Ions Linked to Bioenergetics: Relevance to Human Pathology.

    Scalise, Mariafrancesca / Koprowski, Piotr / Indiveri, Cesare

    Frontiers in molecular biosciences

    2021  Volume 8, Page(s) 770797

    Language English
    Publishing date 2021-09-27
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2021.770797
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Amino Acids Transport and Metabolism 2.0

    Mariafrancesca Scalise / Cesare Indiveri

    International Journal of Molecular Sciences, Vol 21, Iss 4, p

    2020  Volume 1212

    Abstract: This editorial aims to summarize the 19 scientific papers that contributed to this Special Issue. ...

    Abstract This editorial aims to summarize the 19 scientific papers that contributed to this Special Issue.
    Keywords n/a ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Amino Acids Transport and Metabolism 2.0.

    Scalise, Mariafrancesca / Indiveri, Cesare

    International journal of molecular sciences

    2020  Volume 21, Issue 4

    Abstract: This editorial aims to summarize the 19 scientific papers that contributed to this Special Issue. ...

    Abstract This editorial aims to summarize the 19 scientific papers that contributed to this Special Issue.
    MeSH term(s) Adaptor Proteins, Signal Transducing ; Amino Acids/metabolism ; Biological Transport/physiology ; Cationic Amino Acid Transporter 1/metabolism ; Glutamate Plasma Membrane Transport Proteins/metabolism ; Humans ; Large Neutral Amino Acid-Transporter 1 ; Proteins
    Chemical Substances Adaptor Proteins, Signal Transducing ; Amino Acids ; Cationic Amino Acid Transporter 1 ; Glutamate Plasma Membrane Transport Proteins ; LAT2 protein, human ; Large Neutral Amino Acid-Transporter 1 ; Proteins ; SLC7A1 protein, human ; SLC7A5 protein, human
    Language English
    Publishing date 2020-02-12
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms21041212
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Repurposing Nimesulide, a Potent Inhibitor of the B0AT1 Subunit of the SARS-CoV-2 Receptor, as a Therapeutic Adjuvant of COVID-19.

    Scalise, Mariafrancesca / Indiveri, Cesare

    SLAS discovery : advancing life sciences R & D

    2020  Volume 25, Issue 10, Page(s) 1171–1173

    Abstract: The global pandemic caused by the SARS-CoV-2 infection is a health emergency that needs to be addressed immediately. The international scientific community, following World Health Organization (WHO) indications, launched different trials for testing ... ...

    Abstract The global pandemic caused by the SARS-CoV-2 infection is a health emergency that needs to be addressed immediately. The international scientific community, following World Health Organization (WHO) indications, launched different trials for testing drugs putatively able to block the SARS-CoV-2 infection or treat the COVID-19 disease symptoms. In parallel, studies devoted to a better understanding of SARS-CoV-2 biology are in the course for designing an effective vaccine. One of the human membrane proteins known to be docked by the virus is angiotensin-converting enzyme 2 (ACE2), proposed to be responsible for viral entry in target cells. Recently, the 3D structure of ACE2 has been obtained, showing its physical interaction with B0AT1 (SLC6A19), a plasma membrane transporter involved in the trafficking of amino acids in cells. The receptor targeted by SARS-CoV-2 is a supercomplex formed by a dimer of ACE2-B0AT1, in which ACE2 binds the viral protein and B0AT1 stabilizes the heterodimer. As a serendipity occurrence, nimesulide was shown to abolish the transport function of B0AT1. Here we suggest including nimesulide in the list of drugs to be tested for the identification of co-adjuvants in the treatment of COVID-19.
    MeSH term(s) Amino Acid Transport Systems, Neutral/chemistry ; Amino Acid Transport Systems, Neutral/metabolism ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; Drug Repositioning ; Host-Pathogen Interactions/drug effects ; Humans ; SARS-CoV-2/pathogenicity ; Serine Endopeptidases/metabolism ; Sulfonamides/pharmacology
    Chemical Substances Amino Acid Transport Systems, Neutral ; Antiviral Agents ; SLC6A19 protein, human ; Sulfonamides ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-) ; nimesulide (V4TKW1454M)
    Keywords covid19
    Language English
    Publishing date 2020-06-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2885123-7
    ISSN 2472-5560 ; 2472-5552
    ISSN (online) 2472-5560
    ISSN 2472-5552
    DOI 10.1177/2472555220934421
    Database MEDical Literature Analysis and Retrieval System OnLINE

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