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  1. AU="Schreiner, Ryan"
  2. AU=Pltz T
  3. AU="Akhmanova, Anna" AU="Akhmanova, Anna"
  4. AU="Goretsky, Anton"
  5. AU="Cordoza, Makayla L"
  6. AU=Midoux Patrick AU=Midoux Patrick
  7. AU="Mundt, H M"
  8. AU=Tsivitse Susan

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  1. Artikel ; Online: Carbonic Anhydrase Inhibitor Modulation of Intraocular Pressure Is Independent of Soluble Adenylyl Cyclase.

    Wiggins, Shakarr V / Schreiner, Ryan / Ferreira, Jacob / Marmorstein, Alan D / Levin, Lonny R / Buck, Jochen

    Journal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics

    2023  Band 39, Heft 5, Seite(n) 317–323

    Abstract: Purpose: ...

    Abstract Purpose:
    Mesh-Begriff(e) Animals ; Mice ; Intraocular Pressure ; Carbonic Anhydrase Inhibitors ; Adenylyl Cyclases/therapeutic use ; Mice, Inbred C57BL ; Glaucoma/drug therapy
    Chemische Substanzen brinzolamide (9451Z89515) ; Carbonic Anhydrase Inhibitors ; Adenylyl Cyclases (EC 4.6.1.1)
    Sprache Englisch
    Erscheinungsdatum 2023-04-25
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1237021-6
    ISSN 1557-7732 ; 1080-7683
    ISSN (online) 1557-7732
    ISSN 1080-7683
    DOI 10.1089/jop.2022.0180
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Regulation of the apico-basolateral trafficking polarity of the homologous copper-ATPases ATP7A and ATP7B.

    Ruturaj / Mishra, Monalisa / Saha, Soumyendu / Maji, Saptarshi / Rodriguez-Boulan, Enrique / Schreiner, Ryan / Gupta, Arnab

    Journal of cell science

    2023  Band 137, Heft 5

    Abstract: The homologous P-type copper-ATPases (Cu-ATPases) ATP7A and ATP7B are the key regulators of copper homeostasis in mammalian cells. In polarized epithelia, upon copper treatment, ATP7A and ATP7B traffic from the trans-Golgi network (TGN) to basolateral ... ...

    Abstract The homologous P-type copper-ATPases (Cu-ATPases) ATP7A and ATP7B are the key regulators of copper homeostasis in mammalian cells. In polarized epithelia, upon copper treatment, ATP7A and ATP7B traffic from the trans-Golgi network (TGN) to basolateral and apical membranes, respectively. We characterized the sorting pathways of Cu-ATPases between TGN and the plasma membrane and identified the machinery involved. ATP7A and ATP7B reside on distinct domains of TGN in limiting copper conditions, and in high copper, ATP7A traffics to basolateral membrane, whereas ATP7B traverses common recycling, apical sorting and apical recycling endosomes en route to apical membrane. Mass spectrometry identified regulatory partners of ATP7A and ATP7B that include the adaptor protein-1 complex. Upon knocking out pan-AP-1, sorting of both Cu-ATPases is disrupted. ATP7A loses its trafficking polarity and localizes on both apical and basolateral surfaces in high copper. By contrast, ATP7B loses TGN retention but retained its trafficking polarity to the apical domain, which became copper independent. Using isoform-specific knockouts, we found that the AP-1A complex provides directionality and TGN retention for both Cu-ATPases, whereas the AP-1B complex governs copper-independent trafficking of ATP7B solely. Trafficking phenotypes of Wilson disease-causing ATP7B mutants that disrupts putative ATP7B-AP1 interaction further substantiates the role of AP-1 in apical sorting of ATP7B.
    Mesh-Begriff(e) Animals ; Humans ; Adenosine Triphosphatases/metabolism ; Cell Membrane/metabolism ; Copper/metabolism ; Copper-Transporting ATPases/genetics ; Copper-Transporting ATPases/metabolism ; Hepatolenticular Degeneration/genetics ; Mammals/metabolism ; Peptide Fragments/metabolism ; Transcription Factor AP-1/metabolism
    Chemische Substanzen Adenosine Triphosphatases (EC 3.6.1.-) ; ATP7A protein, human (EC 7.2.2.8) ; ATP7A protein, human (2-79) ; Copper (789U1901C5) ; Copper-Transporting ATPases (EC 7.2.2.8) ; Peptide Fragments ; Transcription Factor AP-1 ; ATP7B protein, human (EC 7.2.2.8)
    Sprache Englisch
    Erscheinungsdatum 2023-11-30
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.261258
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel: The mast cell exosome-fibroblast connection: A novel pro-fibrotic pathway.

    Savage, Alexandria / Risquez, Cristobal / Gomi, Kazunori / Schreiner, Ryan / Borczuk, Alain C / Worgall, Stefan / Silver, Randi B

    Frontiers in medicine

    2023  Band 10, Seite(n) 1139397

    Abstract: Introduction: In addition to the traditional activation of resident receptors by release of local mediators, new evidence favors the existence of exosomes in cell-to-cell communication that mediates delivery of specific cargo to modulate recipient cell ... ...

    Abstract Introduction: In addition to the traditional activation of resident receptors by release of local mediators, new evidence favors the existence of exosomes in cell-to-cell communication that mediates delivery of specific cargo to modulate recipient cell function. We report that mast cell exosomes are an additional source of pro-fibrotic substances and constitute a unique pathway for the generation of excess collagen.
    Methods: We use primary human lung fibroblasts (HLFs) to demonstrate the uptake of labeled exosomes isolated from the human mast cell line HMC-1 (MC-EXOs), previously shown to contain protein cargo in common with human mast cell exosomes.
    Results: The MC-EXO uptake by HLF is to the cytosol and increases both proline hydroxylation in HLF lysate and secreted collagen, within 24 h, which is sustained over 72 h, the same time required for transforming growth factor-β (TGF-β) to activate collagen synthesis in the HLFs. Unlike TGF-β, MC-EXO uptake does not induce fibrillar gene activation or invoke the Smad-nuclear transcription pathway. We show that MC-EXO uptake and TGF-β have an additive effect on collagen synthesis in HLF and postulate that MC-EXO uptake by HLFs is a contributing factor to excess collagen synthesis and represents a unique paradigm for understanding fibrosis.
    Discussion: It is known that, in the lungs, mast cells are more activated and increase in number with inflammation, injury and viral infection associated with fibrosis. With the reported increased incidence of post-COVID-pulmonary fibrosis (PCPF), data from patients with severe COVID-19 are presented that show an increase in the mast cell number in lung parenchyma, the site of PCPF. Our findings provide a rationale for targeting multiple fibrogenic pathways in the management of lung fibrosis and the use of mast cell exosomes as a biomarker for the prognostic and diagnostic management of evolving fibrotic lung disease.
    Sprache Englisch
    Erscheinungsdatum 2023-02-23
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2775999-4
    ISSN 2296-858X
    ISSN 2296-858X
    DOI 10.3389/fmed.2023.1139397
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  4. Artikel ; Online: NDUFA4L2 reduces mitochondrial respiration resulting in defective lysosomal trafficking in clear cell renal cell carcinoma.

    Kubala, Jaclyn M / Laursen, Kristian B / Schreiner, Ryan / Williams, Ryan M / van der Mijn, Johannes C / Crowley, Michael J / Mongan, Nigel P / Nanus, David M / Heller, Daniel A / Gudas, Lorraine J

    Cancer biology & therapy

    2023  Band 24, Heft 1, Seite(n) 2170669

    Abstract: In clear cell renal cell carcinoma (ccRCC), activation of hypoxic signaling induces NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4-like 2 (NDUFA4L2) expression. Over 90% of ccRCCs exhibit overexpression of NDUFA4L2, which we previously showed ... ...

    Abstract In clear cell renal cell carcinoma (ccRCC), activation of hypoxic signaling induces NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4-like 2 (NDUFA4L2) expression. Over 90% of ccRCCs exhibit overexpression of NDUFA4L2, which we previously showed contributes to ccRCC proliferation and survival. The function of NDUFA4L2 in ccRCC has not been fully elucidated. NDUFA4L2 was reported to reduce mitochondrial respiration via mitochondrial complex I inhibition. We found that NDUFA4L2 expression in human ccRCC cells increases the extracellular acidification rate, indicative of elevated glycolysis. Conversely, NDUFA4L2 expression in non-cancerous kidney epithelial cells decreases oxygen consumption rate while increasing extracellular acidification rate, suggesting that a Warburg-like effect is induced by NDUFA4L2 alone. We performed mass-spectrometry (MS)-based proteomics of NDUFA4L2 associated complexes. Comparing RCC4-P (parental) ccRCC cells with RCC4 in which NDUFA4L2 is knocked out by CRISPR-Cas9 (RCC4-KO-643), we identified 3,215 proteins enriched in the NDUFA4L2 immunoprecipitates. Among the top-ranking pathways were "Metabolic Reprogramming in Cancer" and "Glycolysis Activation in Cancer (Warburg Effect)." We also show that NDUFA4L2 enhances mitochondrial fragmentation, interacts with lysosomes, and increases mitochondrial-lysosomal associations, as assessed by high-resolution fluorescence microscopy and live cell imaging. We identified 161 lysosomal proteins, including Niemann-Pick Disease Type C Intracellular Cholesterol Transporters 1 and 2 (NPC1, NPC2), that are associated with NDUFA4L2 in RCC4-P cells. RCC4-P cells have larger and decreased numbers of lysosomes relative to RCC4 NDUFA4L2 knockout cells. These findings suggest that NDUFA4L2 regulates mitochondrial-lysosomal associations and potentially lysosomal size and abundance. Consequently, NDUFA4L2 may regulate not only mitochondrial, but also lysosomal functions in ccRCC.
    Mesh-Begriff(e) Humans ; Carcinoma, Renal Cell/genetics ; Electron Transport Complex I/genetics ; Kidney Neoplasms/genetics ; Lysosomes ; Mitochondria
    Chemische Substanzen Electron Transport Complex I (EC 7.1.1.2) ; NDUFA4L2 protein, human
    Sprache Englisch
    Erscheinungsdatum 2023-01-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2146305-0
    ISSN 1555-8576 ; 1538-4047
    ISSN (online) 1555-8576
    ISSN 1538-4047
    DOI 10.1080/15384047.2023.2170669
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Morphological characterization of Etv2 vascular explants using fractal analysis and atomic force microscopy.

    Adelson, Robert P / Palikuqi, Brisa / Weiss, Zachary / Checco, Antonio / Schreiner, Ryan / Rafii, Shahin / Rabbany, Sina Y

    Microvascular research

    2021  Band 138, Seite(n) 104205

    Abstract: The rapid engraftment of vascular networks is critical for functional incorporation of tissue explants. However, existing methods for inducing angiogenesis utilize approaches that yield vasculature with poor temporal stability or inadequate mechanical ... ...

    Abstract The rapid engraftment of vascular networks is critical for functional incorporation of tissue explants. However, existing methods for inducing angiogenesis utilize approaches that yield vasculature with poor temporal stability or inadequate mechanical integrity, which reduce their robustness in vivo. The transcription factor Ets variant 2 (Etv2) specifies embryonic hematopoietic and vascular endothelial cell (EC) development, and is transiently reactivated during postnatal vascular regeneration and tumor angiogenesis. This study investigates the role for Etv2 upregulation in forming stable vascular beds both in vitro and in vivo. Control and Etv2
    Mesh-Begriff(e) Cell Shape ; Cells, Cultured ; Coculture Techniques ; Colonic Neoplasms/blood supply ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Fractals ; Human Umbilical Vein Endothelial Cells/metabolism ; Human Umbilical Vein Endothelial Cells/pathology ; Humans ; Image Processing, Computer-Assisted ; Microscopy, Atomic Force ; Neovascularization, Pathologic ; Neovascularization, Physiologic ; Protocadherins/metabolism ; Tissue Culture Techniques ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Vascular Endothelial Growth Factor Receptor-2/metabolism
    Chemische Substanzen ETV2 protein, human ; PCDH12 protein, human ; Protocadherins ; Transcription Factors ; KDR protein, human (EC 2.7.10.1) ; Vascular Endothelial Growth Factor Receptor-2 (EC 2.7.10.1)
    Sprache Englisch
    Erscheinungsdatum 2021-06-17
    Erscheinungsland United States
    Dokumenttyp Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Video-Audio Media
    ZDB-ID 80307-8
    ISSN 1095-9319 ; 0026-2862
    ISSN (online) 1095-9319
    ISSN 0026-2862
    DOI 10.1016/j.mvr.2021.104205
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  6. Artikel ; Online: Apical CLC-2 in retinal pigment epithelium is crucial for survival of the outer retina.

    Hanke-Gogokhia, Christin / Lehmann, Guillermo L / Benedicto, Ignacio / de la Fuente-Ortega, Erwin / Arshavsky, Vadim Y / Schreiner, Ryan / Rodriguez-Boulan, Enrique

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2021  Band 35, Heft 7, Seite(n) e21689

    Abstract: Knockout of the chloride channel protein 2 (CLC-2; CLCN2) results in fast progressing blindness in mice. Retinal Pigment Epithelium (RPE) and photoreceptors undergo, in parallel, rapid, and profound morphological changes and degeneration. ... ...

    Abstract Knockout of the chloride channel protein 2 (CLC-2; CLCN2) results in fast progressing blindness in mice. Retinal Pigment Epithelium (RPE) and photoreceptors undergo, in parallel, rapid, and profound morphological changes and degeneration. Immunohistochemistry and electron microscopy of the outer retina and electroretinography of the CLC-2 KO mouse demonstrated normal morphology at postnatal day 2, followed by drastic changes in RPE and photoreceptor morphology and loss of vision during the first postnatal month. To investigate whether the RPE or the photoreceptors are the primary cause of the degeneration, we injected lentiviruses carrying HA-tagged CLC-2 with an RPE-specific promotor in the subretinal space of CLC-2-KO mice at the time of eye opening. As expected, CLC-2-HA was expressed exclusively in RPE; strikingly, this procedure rescued the degeneration of both RPE and photoreceptors. Light response in transduced eyes was also recovered. Only a fraction of RPE was transduced with the lentivirus; however, the entire RPE monolayer appears healthy, even the RPE cells not expressing the CLC-2-HA. Surprisingly, in contrast with previous physiological observations that postulate that CLC-2 has a basolateral localization in RPE, our immunofluorescence experiments demonstrated CLC-2 has an apical distribution, facing the subretinal space and the photoreceptor outer segments. Our findings suggest that CLC-2 does not play the postulated role in fluid transport at the basolateral membrane. Rather, they suggest that CLC-2 performs a critical homeostatic role in the subretinal compartment involving a chloride regulatory mechanism that is critical for the survival of both RPE and photoreceptors.
    Mesh-Begriff(e) Animals ; Chloride Channels/physiology ; Disease Models, Animal ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Photoreceptor Cells/cytology ; Photoreceptor Cells/metabolism ; Retina/cytology ; Retina/metabolism ; Retinal Degeneration ; Retinal Pigment Epithelium/metabolism
    Chemische Substanzen Chloride Channels ; ClC-2 chloride channels
    Sprache Englisch
    Erscheinungsdatum 2021-06-04
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.202100349R
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Endothelial Jak3 expression enhances pro-hematopoietic angiocrine function in mice.

    Barcia Durán, José Gabriel / Lu, Tyler / Houghton, Sean / Geng, Fuqiang / Schreiner, Ryan / Xiang, Jenny / Rafii, Shahin / Redmond, David / Lis, Raphaël

    Communications biology

    2021  Band 4, Heft 1, Seite(n) 406

    Abstract: Jak3 is the only non-promiscuous member of the Jak family of secondary messengers. Studies to date have focused on understanding and targeting the cell-autonomous role of Jak3 in immunity, while functional Jak3 expression outside the hematopoietic system ...

    Abstract Jak3 is the only non-promiscuous member of the Jak family of secondary messengers. Studies to date have focused on understanding and targeting the cell-autonomous role of Jak3 in immunity, while functional Jak3 expression outside the hematopoietic system remains largely unreported. We show that Jak3 is expressed in endothelial cells across hematopoietic and non-hematopoietic organs, with heightened expression in the bone marrow. The bone marrow niche is understood as a network of different cell types that regulate hematopoietic function. We show that the Jak3
    Mesh-Begriff(e) Animals ; Endothelial Cells/metabolism ; Female ; Gene Knock-In Techniques ; Hematopoiesis/genetics ; Hematopoietic Stem Cells/metabolism ; Janus Kinase 3/genetics ; Janus Kinase 3/metabolism ; Male ; Mice
    Chemische Substanzen Jak3 protein, mouse (EC 2.7.10.2) ; Janus Kinase 3 (EC 2.7.10.2)
    Sprache Englisch
    Erscheinungsdatum 2021-03-25
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-021-01846-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: Copper(II) import and reduction are dependent on His-Met clusters in the extracellular amino terminus of human copper transporter-1.

    Kar, Sumanta / Sen, Samarpita / Maji, Saptarshi / Saraf, Deepashri / Ruturaj / Paul, Rupam / Dutt, Sohini / Mondal, Basudeb / Rodriguez-Boulan, Enrique / Schreiner, Ryan / Sengupta, Durba / Gupta, Arnab

    The Journal of biological chemistry

    2022  Band 298, Heft 3, Seite(n) 101631

    Abstract: Copper(I) is an essential metal for all life forms. Though Cu(II) is the most abundant and stable state, its reduction to Cu(I) via an unclear mechanism is prerequisite for its bioutilization. In eukaryotes, the copper transporter-1 (CTR1) is the primary ...

    Abstract Copper(I) is an essential metal for all life forms. Though Cu(II) is the most abundant and stable state, its reduction to Cu(I) via an unclear mechanism is prerequisite for its bioutilization. In eukaryotes, the copper transporter-1 (CTR1) is the primary high-affinity copper importer, although its mechanism and role in Cu(II) reduction remain uncharacterized. Here we show that extracellular amino-terminus of human CTR1 contains two methionine-histidine clusters and neighboring aspartates that distinctly bind Cu(I) and Cu(II) preceding its import. We determined that hCTR1 localizes at the basolateral membrane of polarized MDCK-II cells and that its endocytosis to Common-Recycling-Endosomes is regulated by reduction of Cu(II) to Cu(I) and subsequent Cu(I) coordination by the methionine cluster. We demonstrate the transient binding of both Cu(II) and Cu(I) during the reduction process is facilitated by aspartates that also act as another crucial determinant of hCTR1 endocytosis. Mutating the first Methionine cluster (
    Mesh-Begriff(e) Copper/metabolism ; Copper Transporter 1/chemistry ; Copper Transporter 1/metabolism ; Endocytosis ; Histidine ; Humans ; Methionine/chemistry ; Methionine/metabolism
    Chemische Substanzen Copper Transporter 1 ; SLC31A1 protein, human ; Histidine (4QD397987E) ; Copper (789U1901C5) ; Methionine (AE28F7PNPL)
    Sprache Englisch
    Erscheinungsdatum 2022-01-26
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.101631
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel: Structural and functional analysis of endosomal compartments in epithelial cells.

    Bay, Andres E Perez / Schreiner, Ryan / Rodriguez-Boulan, Enrique

    Methods in cell biology

    2015  Band 130, Seite(n) 271–288

    Abstract: Epithelial cells display segregated early endosomal compartments, termed apical sorting endosomes and basolateral sorting endosomes, that converge into a common late endosomal-lysosomal degradative compartment and common recycling endosomes (CREs). ... ...

    Abstract Epithelial cells display segregated early endosomal compartments, termed apical sorting endosomes and basolateral sorting endosomes, that converge into a common late endosomal-lysosomal degradative compartment and common recycling endosomes (CREs). Unlike recycling endosomes of nonpolarized cells, CREs have the ability to sort apical and basolateral plasma membrane proteins into distinct apical and basolateral recycling routes, utilizing mechanisms similar to those employed by the trans Golgi network in the biosynthetic pathway. The apical recycling route includes an additional compartment, the apical recycling endosomes, consisting of multiple vesicles bundled around the basal body. Recent evidence indicates that, in addition to their role in internalizing ligands and recycling their receptors back to the cell surface, endosomal compartments act as intermediate stations in the biosynthetic routes to the plasma membrane. Here we review methods employed by our laboratory to study the endosomal compartments of epithelial cells and their multiple trafficking roles.
    Mesh-Begriff(e) Animals ; Dogs ; Endocytosis ; Endosomes/metabolism ; Endosomes/ultrastructure ; Epithelial Cells/metabolism ; Epithelial Cells/ultrastructure ; Fluorescent Antibody Technique, Indirect ; Madin Darby Canine Kidney Cells ; Microscopy, Fluorescence ; Protein Transport
    Sprache Englisch
    Erscheinungsdatum 2015
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 0091-679X
    ISSN 0091-679X
    DOI 10.1016/bs.mcb.2015.06.019
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  10. Artikel ; Online: Apolipoprotein L-1 renal risk variants form active channels at the plasma membrane driving cytotoxicity.

    Giovinazzo, Joseph A / Thomson, Russell P / Khalizova, Nailya / Zager, Patrick J / Malani, Nirav / Rodriguez-Boulan, Enrique / Raper, Jayne / Schreiner, Ryan

    eLife

    2020  Band 9

    Abstract: Recently evolved alleles of Apolipoprotein L-1 ( ...

    Abstract Recently evolved alleles of Apolipoprotein L-1 (
    Mesh-Begriff(e) Animals ; Apolipoprotein L1/genetics ; Apolipoprotein L1/metabolism ; CHO Cells ; Cell Death ; Cell Membrane/metabolism ; Cricetulus ; Cytotoxins/metabolism ; Endoplasmic Reticulum/metabolism ; HEK293 Cells ; Humans ; Hydrogen-Ion Concentration ; Ion Channels/metabolism ; Kidney Diseases/etiology ; Kidney Diseases/metabolism ; Microscopy, Fluorescence ; Potassium/metabolism ; Risk Factors ; Sodium/metabolism
    Chemische Substanzen APOL1 protein, human ; Apolipoprotein L1 ; Cytotoxins ; Ion Channels ; Sodium (9NEZ333N27) ; Potassium (RWP5GA015D)
    Sprache Englisch
    Erscheinungsdatum 2020-05-19
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.51185
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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