Bitter-Tasting Amino Acids l-Arginine and l-Isoleucine Differentially Regulate Proton Secretion via T2R1 Signaling in Human Parietal Cells in Culture

2019 ◽  
Vol 68 (11) ◽  
pp. 3434-3444 ◽  
Author(s):  
Verena Stoeger ◽  
Ann-Katrin Holik ◽  
Kathrin Hölz ◽  
Tamir Dingjan ◽  
Joachim Hans ◽  
...  
2017 ◽  
Vol 66 (10) ◽  
pp. 2295-2300 ◽  
Author(s):  
Kathrin I. Liszt ◽  
Joachim Hans ◽  
Jakob P. Ley ◽  
Elke Köck ◽  
Veronika Somoza

1988 ◽  
Vol 448 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Ann Kingsbury ◽  
Vittorio Gallo ◽  
Robert Balazs

2003 ◽  
Vol 278 (23) ◽  
pp. 21018-21023 ◽  
Author(s):  
Niv Papo ◽  
Michal Shahar ◽  
Lea Eisenbach ◽  
Yechiel Shai

1997 ◽  
Vol 322 (3) ◽  
pp. 801-808 ◽  
Author(s):  
Daniel T. DRANSFIELD ◽  
Jennifer L. YEH ◽  
Alvin J. BRADFORD ◽  
James R. GOLDENRING

The type-II cAMP-dependent protein kinase (A-Kinase) partitions primarily into the particulate fraction in gastric parietal cells. Localization of this kinase to particular subcellular domains is mediated through the binding of the regulatory subunit (RII) dimer to A-Kinase-anchoring proteins (AKAPs). Using a [32P]RII overlay assay, we have screened a rabbit gastric parietal cell cDNA library and have isolated a single RII-binding protein clone. Sequence analysis revealed an open reading frame coding for 1022 amino acids (AKAP120). Recombinant fragments of the full-length clone were prepared and the RII-binding region mapped to an area between amino acids 489 and 549. This area contained a putative α-helical RII-binding region between amino acids 503 and 516. Incubation of [32P]RII with a synthetic peptide of AKAP120-(489–522) completely inhibited the binding of [32P]RII to the recombinant AKAP120 fragments that demonstrated RII binding. In vitroRII -binding affinity studies indicated a high-affinity interaction between AKAP120 and RII with a Kapp between 50 and 120 nM for the three recombinant fragments that bound [32P]RII. RNase-protection analysis revealed that AKAP120 is a widely distributed protein, with the highest levels of mRNA observed in gastric fundus. The presence of this novel high-affinity AKAP in gastric parietal cells suggests that it may regulate RII subcellular sequestration in this cell type.


Author(s):  
Carl Waldmann ◽  
Neil Soni ◽  
Andrew Rhodes

H2 blockers and proton pump inhibitors 194Antiemetics 196Gut motility agents 198Antidiarrhoeals 200Constipation in critical care 202There is continual basal acid secretion and an increase after meals, from the parietal cells in the body and fundus of the stomach. The dominant mechanism for acid secretion is mediated by histamine from enterochromaffin cells, in turn stimulated by gastrin, released from antral G cells in response to amino acids. Other stimuli acting on parietal cells include acetylcholine, gastrin, calcium and pituitary adenylate cyclase-activating polypeptide....


2005 ◽  
Vol 289 (4) ◽  
pp. G664-G669 ◽  
Author(s):  
Stephanie M. Busque ◽  
Jane E. Kerstetter ◽  
John P. Geibel ◽  
Karl Insogna

Parietal cells are the primary acid secretory cells of the stomach. We have previously shown that activation of the calcium-sensing receptor (CaSR) by divalent (Ca2+) or trivalent (Gd3+) ions stimulates acid production in the absence of secretagogues by increasing H+,K+-ATPase activity. When overexpressed in HEK-293 cells, the CaSR can be allosterically activated by l-amino acids in the presence of physiological concentrations of extracellular Ca2+ (Cao2+; 1.5–2.5 mM). To determine whether the endogenously expressed parietal cell CaSR is allosterically activated by l-amino acids, we examined the effect of the amino acids l-phenylalanine (l-Phe), l-tryptophan, and l-leucine on acid secretion. In ex vivo whole stomach preparations, exposure to l-Phe resulted in gastric luminal pH significantly lower than controls. Studies using d-Phe (inactive isomer) failed to elicit a response on gastric pH. H+-K+-ATPase activity was monitored by measuring the intracellular pH (pHi) of individual parietal cells in isolated rat gastric glands and calculating the rate of H+ extrusion. We demonstrated that increasing Cao2+ in the absence of secretagogues caused a dose-dependent increase in H+ extrusion. These effects were amplified by the addition of amino acids at various Cao2+ concentrations. Blocking the histamine-2 receptor with cimetidine or inhibiting system l-amino acid transport with 2-amino-2-norbornane-carboxylic acid did not affect the rate of H+ extrusion in the presence of l-Phe. These data support the conclusion that amino acids, in conjunction with a physiological Cao2+ concentration, can induce acid secretion independent of hormonal stimulation via allosteric activation of the stomach CaSR.


In Vitro ◽  
1974 ◽  
Vol 9 (6) ◽  
pp. 414-420 ◽  
Author(s):  
Otto Grahl-Nielsen ◽  
P. Ødegaard ◽  
George L. Tritsch

Sign in / Sign up

Export Citation Format

Share Document