ArticleThe Histochemical journal2001
H+ and HCO3- transporters in human salivary ducts. An immunohistochemical study.
Article in The Histochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 20 citations in OpenAlex.
- Role of Sodium Bicarbonate Cotransporters in Intracellular pH Regulation and Their Regulatory Mechanisms in Human Submandibular Glands.PloS one · 2015Article
- Chaperone stress 70 protein (STCH) binds and regulates two acid/base transporters NBCe1-B and NHE1.The Journal of biological chemistry · 2013Article
- The chick chorioallantoic membrane: a model of molecular, structural, and functional adaptation to transepithelial ion transport and barrier function during embryonic development.Journal of biomedicine & biotechnology · 2010Review
- Studies on bicarbonate transporters and carbonic anhydrase in porcine nonpigmented ciliary epithelium.Investigative ophthalmology & visual science · 2009Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence and cellular distribution of key H+ and HCO3- transport proteins was studied in human salivary ducts. Immunofluorescence and immunoperoxidase light microscopy was applied, using specific antibodies against the NHE1 and NHE3 isoforms of the Na+/H+ exchanger, against the 31 and 70 kDa subunits of the vacuolar H+-ATPase and against the electrogenic Na+-HCO3- cotransporter. The results show basolateral NHE1 and apical NHE3 in human submandibular, parotid and sublingual duct cells. Vacuolar H+-ATPase was found predominantly in the apical membrane of parotid, submandibular and sublingual duct cells, although it was absent in certain parotid striated duct cells. The Na+-HCO3- cotransporter was predominantly expressed in the apical membrane of parotid and sublingual striated ducts, and intracellularly distributed in the distal parts of the gland tree and in submandibular ducts. The results indicate that HCO3- transport properties of salivary ducts may vary not only between gland and species, but even in different duct segments of the same gland as well.
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Registered trials
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