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  1. Article: Claudin tight junction proteins: novel aspects in paracellular transport.

    Will, Constanze / Fromm, Michael / Müller, Dominik

    Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis

    2008  Volume 28, Issue 6, Page(s) 577–584

    Abstract: Claudins are essential components of the intercellular tight junction and major determinants of paracellular solute fluxes across epithelia and endothelia. Many members of this family display a distinct charge or size specificity, whereas others render ... ...

    Abstract Claudins are essential components of the intercellular tight junction and major determinants of paracellular solute fluxes across epithelia and endothelia. Many members of this family display a distinct charge or size specificity, whereas others render the epithelium impermeable to transport. Due to intercellular localization, claudin-mediated transport processes are passive and driven by an electrochemical gradient. In epithelial tissues, claudins exhibit a temporal-spatial expression pattern corresponding with regional and local solute transport profiles. Whereas paracellular transport mechanisms in organs such as intestine and kidney have been extensively investigated, little is known about the molecular mechanisms determining solute transport in the peritoneum, and thus the determinants of peritoneal dialysis. Given the ubiquitous expression of claudins in endothelia and epithelia, it is predictable that claudins also contribute to pore formation and determination in the peritoneum, and that they are involved in solute flux. Therefore, we review the basic characteristics of claudin family members and their function as exemplified in renal tubular transport and give an outlook to what extent claudin family members might be of importance for solute reabsorption across the peritoneal membrane.
    MeSH term(s) Absorption ; Animals ; Claudin-1 ; Dialysis Solutions/metabolism ; Epithelium/metabolism ; Humans ; Kidney Tubules/physiology ; Loop of Henle/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/physiology ; Peritoneal Dialysis ; Peritoneum/metabolism ; Tight Junctions/physiology
    Chemical Substances CLDN1 protein, human ; Claudin-1 ; Dialysis Solutions ; Membrane Proteins
    Language English
    Publishing date 2008-10-27
    Publishing country United States
    Document type Comment ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 645010-6
    ISSN 0896-8608
    ISSN 0896-8608
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: HPV typing and CGH analysis for the differentiation of primary and metastatic squamous cell carcinomas of the aerodigestive tract.

    Will, Constanze / Schewe, Christiane / Schluns, Karsten / Petersen, Iver

    Cellular oncology : the official journal of the International Society for Cellular Oncology

    2001  Volume 28, Issue 3, Page(s) 97–105

    Abstract: Human papilloma virus (HPV) typing and Comparative Genomic Hybridisation (CGH) analysis can be used in the classification of multiple tumours of the aerodigestive tract for the differentiation between secondary malignancy versus metastasis. We present 3 ... ...

    Abstract Human papilloma virus (HPV) typing and Comparative Genomic Hybridisation (CGH) analysis can be used in the classification of multiple tumours of the aerodigestive tract for the differentiation between secondary malignancy versus metastasis. We present 3 exemplary cases of patients with multiple squamous cell carcinomas, localised within the head and neck region, cervical lymph node and the lung. In two patients, HPV typing identified HPV type 16 in the tonsillar carcinomas and the corresponding cervical lymph node and lung carcinoma indicating that the latter were metastatic spreads. In case 1, CGH confirmed the clonal relationship. Case two showed a peculiar syncytial growth pattern with lymphocytic infiltration which may constitute a potential morphological marker for HPV infection. In case three, a vallecular carcinoma was HPV negative while a lung cancer was positive for HPV type 6 indicating two independent primary tumours. Our case triplet illustrates the variability of HPV infection in squamous cell cancer of the aerodigestive tract and power as well as limitations of morphology, HPV typing and tumour genetics in the classification of multiple tumours.
    MeSH term(s) Carcinoma, Squamous Cell/genetics ; Carcinoma, Squamous Cell/pathology ; Carcinoma, Squamous Cell/virology ; DNA, Viral/analysis ; DNA, Viral/genetics ; Female ; Genome, Human/genetics ; Head and Neck Neoplasms/genetics ; Head and Neck Neoplasms/pathology ; Head and Neck Neoplasms/virology ; Human papillomavirus 16/genetics ; Human papillomavirus 6/genetics ; Humans ; Lung Neoplasms/genetics ; Lung Neoplasms/secondary ; Lung Neoplasms/virology ; Male ; Middle Aged ; Nucleic Acid Hybridization/methods ; Papillomaviridae/classification ; Papillomaviridae/genetics ; Papillomavirus Infections/genetics ; Papillomavirus Infections/pathology ; Papillomavirus Infections/virology ; Tonsillar Neoplasms/genetics ; Tonsillar Neoplasms/pathology ; Tonsillar Neoplasms/virology
    Chemical Substances DNA, Viral
    Language English
    Publishing date 2001-01-10
    Publishing country Netherlands
    Document type Case Reports ; Comparative Study ; Journal Article
    ZDB-ID 2157351-7
    ISSN 1875-8606 ; 1570-5870
    ISSN (online) 1875-8606
    ISSN 1570-5870
    DOI 10.1155/2006/619539
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  3. Book ; Online ; Thesis: Generierung und Charakterisierung Claudin 16 und Claudin 10 defizienter Mäuse

    Will, Constanze [Verfasser] / Tzschentke, Barbara [Akademischer Betreuer] / Müller, Dominik [Akademischer Betreuer] / Fromm, Michael [Akademischer Betreuer]

    2011  

    Author's details Constanze Will. Gutachter: Barbara Tzschentke ; Dominik Müller ; Michael Fromm
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Publisher Humboldt Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I
    Publishing place Berlin
    Document type Book ; Online ; Thesis
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  4. Article ; Online: Deletion of claudin-10 (Cldn10) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis.

    Breiderhoff, Tilman / Himmerkus, Nina / Stuiver, Marchel / Mutig, Kerim / Will, Constanze / Meij, Iwan C / Bachmann, Sebastian / Bleich, Markus / Willnow, Thomas E / Müller, Dominik

    Proceedings of the National Academy of Sciences of the United States of America

    2012  Volume 109, Issue 35, Page(s) 14241–14246

    Abstract: In the kidney, tight junction proteins contribute to segment specific selectivity and permeability of paracellular ion transport. In the thick ascending limb (TAL) of Henle's loop, chloride is reabsorbed transcellularly, whereas sodium reabsorption takes ...

    Abstract In the kidney, tight junction proteins contribute to segment specific selectivity and permeability of paracellular ion transport. In the thick ascending limb (TAL) of Henle's loop, chloride is reabsorbed transcellularly, whereas sodium reabsorption takes transcellular and paracellular routes. TAL salt transport maintains the concentrating ability of the kidney and generates a transepithelial voltage that drives the reabsorption of calcium and magnesium. Thus, functionality of TAL ion transport depends strongly on the properties of the paracellular pathway. To elucidate the role of the tight junction protein claudin-10 in TAL function, we generated mice with a deletion of Cldn10 in this segment. We show that claudin-10 determines paracellular sodium permeability, and that its loss leads to hypermagnesemia and nephrocalcinosis. In isolated perfused TAL tubules of claudin-10-deficient mice, paracellular permeability of sodium is decreased, and the relative permeability of calcium and magnesium is increased. Moreover, furosemide-inhibitable transepithelial voltage is increased, leading to a shift from paracellular sodium transport to paracellular hyperabsorption of calcium and magnesium. These data identify claudin-10 as a key factor in control of cation selectivity and transport in the TAL, and deficiency in this pathway as a cause of nephrocalcinosis.
    MeSH term(s) Animals ; Biological Transport/genetics ; Biological Transport/physiology ; Calcium/metabolism ; Claudins/genetics ; Claudins/metabolism ; Drinking/physiology ; Embryonic Stem Cells/physiology ; Gene Deletion ; Homeostasis/genetics ; Homeostasis/physiology ; Loop of Henle/metabolism ; Magnesium/blood ; Metabolic Diseases/genetics ; Metabolic Diseases/metabolism ; Metabolic Diseases/physiopathology ; Mice ; Mice, Knockout ; Nephrocalcinosis/genetics ; Nephrocalcinosis/metabolism ; Nephrocalcinosis/physiopathology ; Phenotype ; Sodium/metabolism ; Water Deprivation/physiology
    Chemical Substances Claudins ; claudin 10 ; Sodium (9NEZ333N27) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2012-08-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1203834109
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  5. Article ; Online: Targeted deletion of murine Cldn16 identifies extra- and intrarenal compensatory mechanisms of Ca2+ and Mg2+ wasting.

    Will, Constanze / Breiderhoff, Tilman / Thumfart, Julia / Stuiver, Marchel / Kopplin, Kathrin / Sommer, Kerstin / Günzel, Dorothee / Querfeld, Uwe / Meij, Iwan C / Shan, Qixian / Bleich, Markus / Willnow, Thomas E / Müller, Dominik

    American journal of physiology. Renal physiology

    2010  Volume 298, Issue 5, Page(s) F1152–61

    Abstract: Claudin-16 (CLDN16) is critical for renal paracellular epithelial transport of Ca(2+) and Mg(2+) in the thick ascending loop of Henle. To gain novel insights into the role of CLDN16 in renal Ca(2+) and Mg(2+) homeostasis and the pathological mechanisms ... ...

    Abstract Claudin-16 (CLDN16) is critical for renal paracellular epithelial transport of Ca(2+) and Mg(2+) in the thick ascending loop of Henle. To gain novel insights into the role of CLDN16 in renal Ca(2+) and Mg(2+) homeostasis and the pathological mechanisms underlying a human disease associated with CLDN16 dysfunction [familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC), OMIM 248250], we generated a mouse model of CLDN16 deficiency. Similar to patients, CLDN16-deficient mice displayed hypercalciuria and hypomagnesemia. Contrary to FHHNC patients, nephrocalcinosis was absent in our model, indicating the existence of compensatory pathways in ion handling in this model. In line with the renal loss of Ca(2+), compensatory mechanisms like parathyroid hormone and 1,25(OH)(2)D(3) were significantly elevated. Also, gene expression profiling revealed transcriptional upregulation of several Ca(2+) and Mg(2+) transport systems including Trpv5, Trpm6, and calbindin-D9k. Induced gene expression was also seen for the transcripts of two putative Mg(2+) transport proteins, Cnnm2 and Atp13a4. Moreover, urinary pH was significantly lower when compared with wild-type mice. Taken together, our findings demonstrate that loss of CLDN16 activity leads to specific alterations in Ca(2+) and Mg(2+) homeostasis and that CLDN16-deficient mice represent a useful model to further elucidate pathways involved in renal Ca(2+) and Mg(2+) handling.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Animals ; Biological Transport/physiology ; Calcium/metabolism ; Cation Transport Proteins/metabolism ; Claudins/deficiency ; Claudins/genetics ; Claudins/metabolism ; Disease Models, Animal ; Gene Deletion ; Homeostasis/physiology ; Hypercalciuria/metabolism ; Hypercalciuria/physiopathology ; Magnesium/metabolism ; Membrane Transport Proteins ; Mice ; Mice, Knockout ; Nephrocalcinosis/metabolism ; Nephrocalcinosis/physiopathology ; Renal Tubular Transport, Inborn Errors/metabolism ; Renal Tubular Transport, Inborn Errors/physiopathology ; Signal Transduction/physiology
    Chemical Substances Cation Transport Proteins ; Claudins ; Cnnm2 protein, mouse ; Membrane Transport Proteins ; claudin 16 ; Adenosine Triphosphatases (EC 3.6.1.-) ; ATP13A4 protein, mouse (EC 3.6.1.3) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2010-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 603837-2
    ISSN 1522-1466 ; 0363-6127
    ISSN (online) 1522-1466
    ISSN 0363-6127
    DOI 10.1152/ajprenal.00499.2009
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  6. Article ; Online: CNNM2, encoding a basolateral protein required for renal Mg2+ handling, is mutated in dominant hypomagnesemia.

    Stuiver, Marchel / Lainez, Sergio / Will, Constanze / Terryn, Sara / Günzel, Dorothee / Debaix, Huguette / Sommer, Kerstin / Kopplin, Kathrin / Thumfart, Julia / Kampik, Nicole B / Querfeld, Uwe / Willnow, Thomas E / Němec, Vladimír / Wagner, Carsten A / Hoenderop, Joost G / Devuyst, Olivier / Knoers, Nine V A M / Bindels, René J / Meij, Iwan C /
    Müller, Dominik

    American journal of human genetics

    2011  Volume 88, Issue 3, Page(s) 333–343

    Abstract: Familial hypomagnesemia is a rare human disorder caused by renal or intestinal magnesium (Mg(2+)) wasting, which may lead to symptoms of Mg(2+) depletion such as tetany, seizures, and cardiac arrhythmias. Our knowledge of the physiology of Mg(2+) (re) ... ...

    Abstract Familial hypomagnesemia is a rare human disorder caused by renal or intestinal magnesium (Mg(2+)) wasting, which may lead to symptoms of Mg(2+) depletion such as tetany, seizures, and cardiac arrhythmias. Our knowledge of the physiology of Mg(2+) (re)absorption, particularly the luminal uptake of Mg(2+) along the nephron, has benefitted from positional cloning approaches in families with Mg(2+) reabsorption disorders; however, basolateral Mg(2+) transport and its regulation are still poorly understood. Here, by using a candidate screening approach, we identified CNNM2 as a gene involved in renal Mg(2+) handling in patients of two unrelated families with unexplained dominant hypomagnesemia. In the kidney, CNNM2 was predominantly found along the basolateral membrane of distal tubular segments involved in Mg(2+) reabsorption. The basolateral localization of endogenous and recombinant CNNM2 was confirmed in epithelial kidney cell lines. Electrophysiological analysis showed that CNNM2 mediated Mg(2+)-sensitive Na(+) currents that were significantly diminished in mutant protein and were blocked by increased extracellular Mg(2+) concentrations. Our data support the findings of a recent genome-wide association study showing the CNNM2 locus to be associated with serum Mg(2+) concentrations. The mutations found in CNNM2, its observed sensitivity to extracellular Mg(2+), and its basolateral localization signify a critical role for CNNM2 in epithelial Mg(2+) transport.
    MeSH term(s) Amino Acid Sequence ; Amino Acid Substitution/genetics ; Animals ; Base Sequence ; Cation Transport Proteins/chemistry ; Cation Transport Proteins/genetics ; Cyclins/chemistry ; Cyclins/genetics ; Electrophysiological Phenomena/drug effects ; Female ; Genes, Dominant/genetics ; HEK293 Cells ; Humans ; Immunohistochemistry ; Kidney/drug effects ; Kidney/metabolism ; Kidney/pathology ; Magnesium/metabolism ; Magnesium/pharmacology ; Magnesium Deficiency/genetics ; Magnesium Deficiency/pathology ; Male ; Mice ; Molecular Sequence Data ; Mutation/genetics ; Nephrons/drug effects ; Nephrons/metabolism ; Nephrons/pathology ; Pedigree ; Up-Regulation/drug effects
    Chemical Substances CNNM2 protein, human ; Cation Transport Proteins ; Cyclins ; Magnesium (I38ZP9992A)
    Language English
    Publishing date 2011-03-17
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 219384-x
    ISSN 1537-6605 ; 0002-9297
    ISSN (online) 1537-6605
    ISSN 0002-9297
    DOI 10.1016/j.ajhg.2011.02.005
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  7. Article: Deletion of claudin-10 (Cldn10) in the thick ascending limb impairs paracellular sodium permeability and leads to hypermagnesemia and nephrocalcinosis

    Breiderhoff, Tilman / Himmerkus, Nina / Stuiver, Marchel / Mutig, Kerim / Will, Constanze / Meij, Iwan C. / Bachmann, Sebastian / Bleich, Markus / Willnow, Thomas E. / Müller, Dominik

    Proceedings of the National Academy of Sciences of the United States of America

    Volume v. 109,, Issue no. 3

    Abstract: In the kidney, tight junction proteins contribute to segment specific selectivity and permeability of paracellular ion transport. In the thick ascending limb (TAL) of Henle's loop, chloride is reabsorbed transcellularly, whereas sodium reabsorption takes ...

    Abstract In the kidney, tight junction proteins contribute to segment specific selectivity and permeability of paracellular ion transport. In the thick ascending limb (TAL) of Henle's loop, chloride is reabsorbed transcellularly, whereas sodium reabsorption takes transcellular and paracellular routes. TAL salt transport maintains the concentrating ability of the kidney and generates a transepithelial voltage that drives the reabsorption of calcium and magnesium. Thus, functionality of TAL ion transport depends strongly on the properties of the paracellular pathway. To elucidate the role of the tight junction protein claudin-10 in TAL function, we generated mice with a deletion of Cldn10 in this segment. We show that claudin-10 determines paracellular sodium permeability, and that its loss leads to hypermagnesemia and nephrocalcinosis. In isolated perfused TAL tubules of claudin-10–deficient mice, paracellular permeability of sodium is decreased, and the relative permeability of calcium and magnesium is increased. Moreover, furosemide-inhibitable transepithelial voltage is increased, leading to a shift from paracellular sodium transport to paracellular hyperabsorption of calcium and magnesium. These data identify claudin-10 as a key factor in control of cation selectivity and transport in the TAL, and deficiency in this pathway as a cause of nephrocalcinosis.
    Keywords mice ; calcium ; absorption ; nephrocalcinosis ; magnesium ; kidneys ; tight junctions ; sodium ; proteins ; permeability
    Language English
    Document type Article
    ISSN 0027-8424
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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