A cAMP-activated chloride channel in the plasma membrane of cultured human gastric cells (HGT-1)

Sandle, Geoffrey I.; Fraser, Gerald; Long, S.; Warhurst, Geoffrey

doi:10.1007/bf00370990

Cited by 11 publications

(5 citation statements)

References 19 publications

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“…The importance of chloride efflux for the process of gastric acid secretion has been established in the 1980s. Patch-clamp measurements demonstrated the presence of chloride conductance on the apical pole of the parietal cell in Necturus, the human parietal cell line HGT-1, and rabbit parietal cells (259,935,940). All reports demonstrated a sensitivity of the chloride current to cAMP or histamine, which is a common second messenger promoting acid secretion or a direct acid secretagogue, respectively (259,935,940).…”

Section: Chloride Secretionmentioning

confidence: 96%

“…Patch-clamp measurements demonstrated the presence of chloride conductance on the apical pole of the parietal cell in Necturus, the human parietal cell line HGT-1, and rabbit parietal cells (259,935,940). All reports demonstrated a sensitivity of the chloride current to cAMP or histamine, which is a common second messenger promoting acid secretion or a direct acid secretagogue, respectively (259,935,940). Simple flux measurements in isolated parietal cell vesicles had indicated the presence of a chloride conductance pathway even earlier (232,895,1169).…”

Section: Chloride Secretionmentioning

confidence: 99%

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Gastric Acid, Calcium Absorption, and Their Impact on Bone Health

Kopic

Geibel

2013

Physiological Reviews

138

106

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Calcium balance is essential for a multitude of physiological processes, ranging from cell signaling to maintenance of bone health. Adequate intestinal absorption of calcium is a major factor for maintaining systemic calcium homeostasis. Recent observations indicate that a reduction of gastric acidity may impair effective calcium uptake through the intestine. This article reviews the physiology of gastric acid secretion, intestinal calcium absorption, and their respective neuroendocrine regulation and explores the physiological basis of a potential link between these individual systems.

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Section: Chloride Secretionmentioning

confidence: 96%

Section: Chloride Secretionmentioning

confidence: 99%

Gastric Acid, Calcium Absorption, and Their Impact on Bone Health

Kopic

Geibel

2013

Physiological Reviews

138

106

View full text Add to dashboard Cite

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“…The HGT-1 cell line was established in vitro from the primary tumour of a sixty-year-old patient and shares a number of physiological features with the acid-secreting gastric parietal cells, including the expression of H 2 histamine receptors [16], cAMP-mediated Cl -channels [24], Ca ++ -activated K + channels and specific [ 3 H]omeprazole binding sites [23]. In addition, Sandle et al have shown the existence of specific omeprazole binding sites (H + /K + -ATPase) within the plasma membrane of control HGT-1 cells, the density of which increases 100% after histamine stimulation [23].…”

Section: Discussionmentioning

confidence: 99%

“…In addition HGT-1 cells also possess low conductance Cl -channels activated by histamine. These may represent the apical Clchannel activated in parietal cells during acid secretion [24]. Moreover, HGT-1 plasma membrane exhibits a high K + conductance that may represent the K + channels expressed in the basolateral membrane of gastric parietal cells [23].…”

Section: Introductionmentioning

confidence: 99%

The cultured human gastric cells HGT-1 express the principal transporters involved in acid secretion

Carmosino¹,

Procino²,

Casavola³

et al. 2000

Pflugers Arch - Eur J Physiol

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HGT-1 is a human cell line sharing a number of physiological features with gastric parietal cells. HGT-1 cell monolayers were able to secrete H+ when stimulated with histamine (calculated external pH variation, deltapH(e) 0.46+/-0.05) as assessed using the impermeant, pH-sensitive fluorescence dye 8-hydroxypyrene-1,3,6-trisulphonic acid, trisodium salt (HPTS). Treatment with 100 microM omeprazole inhibited the histamine-induced apical acidification by about 60%. Intracellular pH (pH(i)) measurements using the fluorescent pH-sensitive dye 2',7'-bis-carboxyethyl-5(6)-carboxyfluorescein (BCECF) demonstrated the expression of a functional, omeprazole-sensitive H+/K+-pump. A monoclonal antibody directed against the alpha subunit of the H+/K+-ATPase immunoprecipitated a 95-kDa protein from HGT-1 cells and human stomach which corresponds to the expected molecular size of the native protein. HGT-1 cells were also positive for the anion exchanger AE2 that is expressed in gastric parietal cells. In addition, we identified a histamine- and pH(i)-sensitive Na+/H+ exchanger in HGT-1 cells, which might correspond to the functional expression of the NHE4 isoform that has been detected in gastric epithelial cells as well as in primary cultured parietal cells. HGT-1 cells therefore display the principal features of parietal cells and might represent an interesting cell culture model for studying the regulatory mechanisms involved in acid secretion.

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“…We obtained HGT-1 cells stably expressing a short-hairpin RNA that knocks down TRPML1 expression (a kind gift of Dr. Ehud Goldin, NIH/NHGRI). The HGT-1 cell line is ideal to model the MLIV disease because it exhibits many characteristics found in primary parietal cells such as the presence of omeprazole-inhibited H + /K + -ATPase, calcium-activated potassium channels, cAMP-activated chloride channels, histamine receptors, and protein transporters involved in acid secretion [14, 65, 90, 91]. Indeed, cultured HGT-1 cells secrete gastric acid in its milieu upon exposure to histamine and/or 3-isobutyl-1-methylxanthine (IBMX, a phosphodiesterase inhibitor) [14].…”

Section: Exploiting the Functional Redundancy Or Similarity Between Tmentioning

confidence: 99%

The mucolipin-2 (TRPML2) ion channel: a tissue-specific protein crucial to normal cell function

Cuajungco

Silva

Habibi

et al. 2015

Pflugers Arch - Eur J Physiol

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The discovery of the TRPML subfamily of ion channels has created an exciting niche in the fields of membrane trafficking, signal transduction, autophagy, and metal homeostasis. The TRPML protein subfamily consist three members, TRPML1, -2, and -3, which are encoded by MCOLN1, -2, and -3 genes, respectively. They are non-selective cation channels with six predicted transmembrane domains, and intracellular amino- and carboxyl-terminus regions. They localize to the plasma membrane, endosomes, and lysosomes of cells. TRPML1 is associated with the human lysosomal storage disease known as Mucolipidosis type IV (MLIV), but TRPML2 and TRPML3 have not been linked with a human disease. Although TRPML1 is expressed in many tissues, TRPML3 is expressed in a varied but limited set of tissues, while TRPML2 has a more limited expression pattern where it is mostly detected in lymphoid and myeloid tissues. This review focuses on TRPML2 because it appears to play an important, yet unrecognized role in the immune system. While the evidence has been mostly indirect, we present and discuss relevant data that strengthen the connection of TRPML2 with cellular immunity. We also discuss the functional redundancy between the TRPML proteins, and how such features could be exploited as a potential therapeutic strategy for MLIV disease. We present evidence that TRPML2 expression may complement certain phenotypic alterations in MLIV cells, and briefly examine the challenges of functional complementation. In conclusion, the function of TRPML2 still remains obscure, but emerging data show that it may serve a critical role in immune cell development and inflammatory responses.

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A cAMP-activated chloride channel in the plasma membrane of cultured human gastric cells (HGT-1)

Cited by 11 publications

References 19 publications

Gastric Acid, Calcium Absorption, and Their Impact on Bone Health

Gastric Acid, Calcium Absorption, and Their Impact on Bone Health

The cultured human gastric cells HGT-1 express the principal transporters involved in acid secretion

The mucolipin-2 (TRPML2) ion channel: a tissue-specific protein crucial to normal cell function

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