| Secretory state regulates Zn2+ transport in gastric parietal cell of the rabbit. | |
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MedLine Citation:
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PMID: 19675302 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Secretory compartments of neurons, endocrine cells, and exocrine glands are acidic and contain high levels of labile Zn2+. Previously, we reported evidence that acidity is regulated, in part, by the content of Zn2+ in the secretory [i.e., tubulovesicle (TV)] compartment of the acid-secreting gastric parietal cell. Here we report studies focusing on the mechanisms of Zn2+ transport by the TV compartment in the mammalian (rabbit) gastric parietal cell. Uptake of Zn2+ by isolated TV structures was monitored with a novel application of the fluorescent Zn2+ reporter N-(6-methoxy-8-quinolyl)-para-toluenesulfonamide (TSQ). Uptake was suppressed by removal of external ATP or blockade of H+-K+-ATPase that mediates luminal acid secretion. Uptake was diminished with dissipation of the proton gradient across the TV membrane, suggesting Zn2+/H+ antiport as the connection between Zn2+ uptake and acidity in the TV lumen. In isolated gastric glands loaded with the reporter fluozin-3, inhibition of H+-K+-ATPase arrested the flow of Zn(2+) from the cytoplasm to the TV compartment and secretory stimulation with forskolin enhanced vectorial movement of cytoplasmic Zn2+ into the tubulovesicle/lumen (TV/L) compartment. Our findings suggest that Zn2+ accumulation in the TV/L compartment is physiologically coupled to secretion of acid. These findings offer novel insight into mechanisms regulating Zn2+ homeostasis in the gastric parietal cell and potentially other cells in which acidic subcellular compartments serve signature functional roles. |
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Authors:
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Haley B Naik; Melissa Beshire; Breda M Walsh; Jingjing Liu; David I Soybel |
Publication Detail:
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Type: In Vitro; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2009-08-12 |
Journal Detail:
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Title: American journal of physiology. Cell physiology Volume: 297 ISSN: 1522-1563 ISO Abbreviation: Am. J. Physiol., Cell Physiol. Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-10-02 Completed Date: 2009-12-03 Revised Date: 2010-10-04 |
Medline Journal Info:
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Nlm Unique ID: 100901225 Medline TA: Am J Physiol Cell Physiol Country: United States |
Other Details:
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Languages: eng Pagination: C979-89 Citation Subset: IM |
Affiliation:
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Department of Surgery, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aminoquinolines Animals Cations, Divalent / metabolism Fluorescent Dyes H(+)-K(+)-Exchanging ATPase / metabolism* Hydrogen-Ion Concentration Ion Transport Parietal Cells, Gastric / metabolism*, secretion Rabbits Tosyl Compounds |
| Grant Support | |
ID/Acronym/Agency:
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R01-DK-069929/DK/NIDDK NIH HHS; //Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
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0/Aminoquinolines; 0/Cations, Divalent; 0/Fluorescent Dyes; 0/Tosyl Compounds; 109628-27-5/N-(6-methoxy-8-quinolyl)-4-toluenesulfonamide; EC 3.6.1.10/H(+)-K(+)-Exchanging ATPase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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