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  1. Book: Organic cation transporters

    Ciarimboli, Giuliano / Gautron, Sophie / Schlatter, Eberhard

    integration of physiology, pathology, and pharmacology

    2016  

    Keywords Molecular biology ; Cytoplasm ; Structural biology ; Cell Membrane ; Genetics
    Language English
    Size XIV, 264 S. : Ill., graph. Darst., 235 mm x 155 mm, 0 g
    Publisher Springer
    Publishing place Cham u.a.
    Publishing country Switzerland
    Document type Book
    HBZ-ID HT018861923
    ISBN 978-3-319-23792-3 ; 978-3-319-23793-0 ; 3-319-23792-6 ; 3-319-23793-4
    Database Catalogue ZB MED Medicine, Health

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  2. Article ; Online: Regulation of Transporters for Organic Cations by High Glucose.

    Steinbüchel, Martin / Menne, Johannes / Schröter, Rita / Neugebauer, Ute / Schlatter, Eberhard / Ciarimboli, Giuliano

    International journal of molecular sciences

    2023  Volume 24, Issue 18

    Abstract: Endogenous positively charged organic substances, including neurotransmitters and cationic uremic toxins, as well as exogenous organic cations such as the anti-diabetic medication metformin, serve as substrates for organic cation transporters (OCTs) and ... ...

    Abstract Endogenous positively charged organic substances, including neurotransmitters and cationic uremic toxins, as well as exogenous organic cations such as the anti-diabetic medication metformin, serve as substrates for organic cation transporters (OCTs) and multidrug and toxin extrusion proteins (MATEs). These proteins facilitate their transport across cell membranes. Vectorial transport through the OCT/MATE axis mediates the hepatic and renal excretion of organic cations, regulating their systemic and local concentrations. Organic cation transporters are part of the remote sensing and signaling system, whose activity can be regulated to cope with changes in the composition of extra- and intracellular fluids. Glucose, as a source of energy, can also function as a crucial signaling molecule, regulating gene expression in various organs and tissues. Its concentration in the blood may fluctuate in specific physiological and pathophysiological conditions. In this work, the regulation of the activity of organic cation transporters was measured by incubating human embryonic kidney cells stably expressing human OCT1 (hOCT1), hOCT2, or hMATE1 with high glucose concentrations (16.7 mM). Incubation with this high glucose concentration for 48 h significantly stimulated the activity of hOCT1, hOCT2, and hMATE1 by increasing their maximal velocity (V
    MeSH term(s) Humans ; Organic Cation Transport Proteins/metabolism ; Organic Cation Transporter 2/genetics ; Metformin/pharmacology ; Metformin/metabolism ; Cations/metabolism ; RNA, Messenger
    Chemical Substances Organic Cation Transport Proteins ; Organic Cation Transporter 2 ; Metformin (9100L32L2N) ; Cations ; RNA, Messenger
    Language English
    Publishing date 2023-09-13
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241814051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells.

    Rose, Ralph / Kemper, Björn / Schwab, Albrecht / Schlatter, Eberhard / Edemir, Bayram

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 11930

    Abstract: Aquaporin-2-4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this also ... ...

    Abstract Aquaporin-2-4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this also applies for renal CD cells. Another fact is that the expression of these AQPs is highly modulated by the external osmolality. Here we analyzed the localization of AQP2-4 in primary cultured renal inner medullary CD (IMCD) cells and how osmolality influences the migration behavior of these cells. The primary IMCD cells showed a collective migration behavior and there were no differences in the migration speed between cells cultivated either at 300 or 600 mosmol/kg. Acute increase from 300 to 600 mosmol/kg led to a marked reduction and vice versa an acute decrease from 600 to 300 mosmol/kg to a marked increase in migration speed. Interestingly, none of the analyzed AQPs were localized at the leading edge. While AQP3 disappeared within the first 2-3 rows of cells, AQP4 was enriched at the rear end. Further analysis indicated that migration induced lysosomal degradation of AQP3. This could be prevented by activation of the protein kinase A, inducing localization of AQP3 and AQP2 at the leading edge and increasing the migration speed.
    MeSH term(s) Animals ; Aquaporin 3/genetics ; Aquaporin 3/metabolism ; Aquaporin 4/genetics ; Aquaporin 4/metabolism ; Bucladesine/pharmacology ; Cell Movement/drug effects ; Cell Movement/physiology ; Cell Shape ; Cells, Cultured ; Kidney Medulla/cytology ; Kidney Tubules, Collecting/cytology ; Kidney Tubules, Collecting/drug effects ; Kidney Tubules, Collecting/metabolism ; Microscopy, Fluorescence/methods ; Osmolar Concentration ; Primary Cell Culture ; Rats ; Sodium-Hydrogen Exchanger 1/metabolism ; beta Catenin/metabolism
    Chemical Substances Aquaporin 4 ; Sodium-Hydrogen Exchanger 1 ; beta Catenin ; Aquaporin 3 (158801-98-0) ; Bucladesine (63X7MBT2LQ)
    Language English
    Publishing date 2021-06-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-91369-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book: METABOLISMUS UND EXKRETION VON PEPTIDHORMONEN IN DER NIERE

    Schlatter, Eberhard

    1980  

    Size 83 S.
    Document type Book
    Note HANNOVER, UNIV., FAK. FUER MATHEMATIK U. NATURWISS., DISS., 1981
    HBZ-ID HT002598341
    Database Catalogue ZB MED Medicine, Health

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  5. Article ; Online: Unexpected localization of AQP3 and AQP4 induced by migration of primary cultured IMCD cells

    Ralph Rose / Björn Kemper / Albrecht Schwab / Eberhard Schlatter / Bayram Edemir

    Scientific Reports, Vol 11, Iss 1, Pp 1-

    2021  Volume 12

    Abstract: Abstract Aquaporin-2–4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this ... ...

    Abstract Abstract Aquaporin-2–4 (AQP) are expressed in the principal cells of the renal collecting duct (CD). Beside their role in water transport across membranes, several studies showed that AQPs can influence the migration of cells. It is unknown whether this also applies for renal CD cells. Another fact is that the expression of these AQPs is highly modulated by the external osmolality. Here we analyzed the localization of AQP2–4 in primary cultured renal inner medullary CD (IMCD) cells and how osmolality influences the migration behavior of these cells. The primary IMCD cells showed a collective migration behavior and there were no differences in the migration speed between cells cultivated either at 300 or 600 mosmol/kg. Acute increase from 300 to 600 mosmol/kg led to a marked reduction and vice versa an acute decrease from 600 to 300 mosmol/kg to a marked increase in migration speed. Interestingly, none of the analyzed AQPs were localized at the leading edge. While AQP3 disappeared within the first 2–3 rows of cells, AQP4 was enriched at the rear end. Further analysis indicated that migration induced lysosomal degradation of AQP3. This could be prevented by activation of the protein kinase A, inducing localization of AQP3 and AQP2 at the leading edge and increasing the migration speed.
    Keywords Medicine ; R ; Science ; Q
    Subject code 610
    Language English
    Publishing date 2021-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: Who Wins the Competition: TRPV5 or Calbindin-D28K?

    Schlatter, Eberhard

    Journal of the American Society of Nephrology : JASN

    2006  Volume 17, Issue 11, Page(s) 2954–2956

    MeSH term(s) Animals ; Calbindin 1 ; Calbindins ; Calcium Channels/physiology ; Mice ; S100 Calcium Binding Protein G/physiology ; TRPV Cation Channels/physiology
    Chemical Substances Calb1 protein, mouse ; Calbindin 1 ; Calbindins ; Calcium Channels ; S100 Calcium Binding Protein G ; TRPV Cation Channels ; Trpv5 protein, mouse
    Language English
    Publishing date 2006-11
    Publishing country United States
    Document type Comment ; Editorial
    ZDB-ID 1085942-1
    ISSN 1533-3450 ; 1046-6673
    ISSN (online) 1533-3450
    ISSN 1046-6673
    DOI 10.1681/ASN.2006080935
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Book: Organic cation transporters

    Ciarimboli, Giuliano / Gautron, Sophie / Schlatter, Eberhard

    integration of physiology, pathology, and pharmacology

    2016  

    Author's details Giuliano Ciarimboli, Sophie Gautron, Eberhard Schlatter, editors
    MeSH term(s) Organic Cation Transport Proteins/physiology ; Organic Cation Transport Proteins/pharmacology
    Language English
    Size xv, 264 pages :, illustrations (chiefly color) ;, 25 cm
    Document type Book
    ISBN 9783319237923 ; 3319237926 ; 9783319237930 ; 3319237934
    Database Catalogue of the US National Library of Medicine (NLM)

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  8. Book ; Online ; Thesis: Untersuchungen zur "repaired defect" Hypothese der glomerulären Kapillarwand

    Repp, Viktor [Verfasser] / Schlatter, Eberhard [Akademischer Betreuer]

    2016  

    Author's details Viktor Repp ; Betreuer: Eberhard Schlatter
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language German
    Publisher Universitäts- und Landesbibliothek Münster
    Publishing place Münster
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  9. Article ; Online: Expression of xenobiotic transporters in the human renal proximal tubule cell line RPTEC/TERT1.

    Aschauer, Lydia / Carta, Giada / Vogelsang, Nadine / Schlatter, Eberhard / Jennings, Paul

    Toxicology in vitro : an international journal published in association with BIBRA

    2014  Volume 30, Issue 1 Pt A, Page(s) 95–105

    Abstract: The kidney is a major target for drug-induced injury, primarily due the fact that it transports a wide variety of chemical entities into and out of the tubular lumen. Here, we investigated the expression of the main xenobiotic transporters in the human ... ...

    Abstract The kidney is a major target for drug-induced injury, primarily due the fact that it transports a wide variety of chemical entities into and out of the tubular lumen. Here, we investigated the expression of the main xenobiotic transporters in the human renal proximal tubule cell line RPTEC/TERT1 at an mRNA and/or protein level. RPTEC/TERT1 cells expressed OCT2, OCT3, OCTN2, MATE1, MATE2, OAT1, OAT3 and OAT4. The functionality of the OCTs was demonstrated by directional transport of the fluorescent dye 4-Di-1-ASP. In addition, P-glycoprotein activity in RPTEC/TERT1 cells was verified by fluorescent dye retention in presence of various P-glycoprotein inhibitors. In comparison to proliferating cells, contact inhibited RPTEC/TERT1 cells expressed increased mRNA levels of several ABC transporter family members and were less sensitive to cyclosporine A. We conclude that differentiated RPTEC/TERT1 cells are well suited for utilisation in xenobiotic transport and pharmacokinetic studies.
    MeSH term(s) Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; Gene Expression Regulation/physiology ; Humans ; Kidney Tubules, Proximal/cytology ; Kidney Tubules, Proximal/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
    Chemical Substances Carrier Proteins ; RNA, Messenger
    Language English
    Publishing date 2014-12-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639064-x
    ISSN 1879-3177 ; 0887-2333
    ISSN (online) 1879-3177
    ISSN 0887-2333
    DOI 10.1016/j.tiv.2014.12.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Notch Signaling Activity Determines Uptake and Biological Effect of Imatinib in Systemic Sclerosis Dermal Fibroblasts.

    Harrach, Saliha / Barz, Vivien / Pap, Thomas / Pavenstädt, Hermann / Schlatter, Eberhard / Edemir, Bayram / Distler, Jörg / Ciarimboli, Giuliano / Bertrand, Jessica

    The Journal of investigative dermatology

    2018  Volume 139, Issue 2, Page(s) 439–447

    Abstract: Tyrosine kinase inhibitors have emerged as a therapeutic option for rheumatic diseases such as systemic sclerosis (SSc). Because tyrosine kinases like c-Abl kinase are important for fibroblast activation and fibrosis development in SSc, the c-Abl ... ...

    Abstract Tyrosine kinase inhibitors have emerged as a therapeutic option for rheumatic diseases such as systemic sclerosis (SSc). Because tyrosine kinases like c-Abl kinase are important for fibroblast activation and fibrosis development in SSc, the c-Abl inhibitor imatinib was proposed for SSc treatment. Transporters for organic cations have become increasingly recognized as an important determinant for uptake and efficacy of tyrosine kinase inhibitors. Therefore, we investigated the role of organic cation transporters in the uptake of imatinib. Moreover, the influence of important SSc pathogenetic factors, like PDGF and Notch pathway activation on these uptake processes, has been studied. We showed that organic cation transporters OCT1-3, novel organic cation transporters OCTN1/2, and the multidrug and toxin extrusion protein MATE1 are expressed in healthy dermal and SSc fibroblasts. Decreased expression levels of MATE1 and decreased imatinib uptake were measured in SSc fibroblasts. In small interfering RNA experiments, MATE1 was identified as key transporter for imatinib uptake and biological effect in dermal fibroblasts. Furthermore, PDGF reduced imatinib uptake by decreasing MATE1 expression in SSc fibroblasts, but not in healthy fibroblasts. Blocking the Notch pathway in SSc fibroblasts increased MATE1 transporter expression and imatinib uptake. In conclusion, MATE1-mediated transport governs therapeutic efficacy of imatinib in SSc.
    MeSH term(s) Biopsy ; Cells, Cultured ; Dermis/cytology ; Dermis/metabolism ; Dermis/pathology ; Fibroblasts/metabolism ; Gene Knockdown Techniques ; Humans ; Imatinib Mesylate/pharmacokinetics ; Imatinib Mesylate/therapeutic use ; Organic Cation Transport Proteins/genetics ; Organic Cation Transport Proteins/metabolism ; Platelet-Derived Growth Factor/metabolism ; Primary Cell Culture ; Protein Kinase Inhibitors/pharmacokinetics ; Protein Kinase Inhibitors/therapeutic use ; RNA, Small Interfering/metabolism ; Receptors, Notch/metabolism ; Scleroderma, Systemic/drug therapy ; Scleroderma, Systemic/pathology ; Signal Transduction
    Chemical Substances Organic Cation Transport Proteins ; Platelet-Derived Growth Factor ; Protein Kinase Inhibitors ; RNA, Small Interfering ; Receptors, Notch ; SLC47A1 protein, human ; Imatinib Mesylate (8A1O1M485B)
    Language English
    Publishing date 2018-09-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80136-7
    ISSN 1523-1747 ; 0022-202X
    ISSN (online) 1523-1747
    ISSN 0022-202X
    DOI 10.1016/j.jid.2018.08.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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