scholarly journals Prostaglandin E2-Activated Housekeeping Cl- Channels in the Basolateral Membrane of Rat Gastric Parietal Cells.

1999 ◽  
Vol 49 (4) ◽  
pp. 365-372 ◽  
Author(s):  
Akira IKARI ◽  
Hideki SAKAI ◽  
Akiko TANAKA ◽  
Atsushi IKEDA ◽  
Kanako INOUE ◽  
...  
Keyword(s):  
Prostaglandin E2 ◽  
Basolateral Membrane ◽  
Parietal Cells ◽  
Cl Channels ◽  
Gastric Parietal Cells

scholarly journals Polarized Distribution of IQGAP Proteins in Gastric Parietal Cells and Their Roles in Regulated Epithelial Cell Secretion

2003 ◽  
Vol 14 (3) ◽  
pp. 1097-1108 ◽  
Author(s):  
Rihong Zhou ◽  
Zhen Guo ◽  
Charles Watson ◽  
Emily Chen ◽  
Rong Kong ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Actin Cytoskeleton ◽  
Acid Secretion ◽  
Rho Gtpase ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Parietal Cells ◽  
Actin Dynamics ◽  
Cell Secretion ◽  
Gastric Parietal Cells

Actin cytoskeleton plays an important role in the establishment of epithelial cell polarity. Cdc42, a member of Rho GTPase family, modulates actin dynamics via its regulators, such as IQGAP proteins. Gastric parietal cells are polarized epithelial cells in which regulated acid secretion occurs in the apical membrane upon stimulation. We have previously shown that actin isoforms are polarized to different membrane domains and that the integrity of the actin cytoskeleton is essential for acid secretion. Herein, we show that Cdc42 is preferentially distributed to the apical membrane of gastric parietal cells. In addition, we revealed that two Cdc42 regulators, IQGAP1 and IQGAP2, are present in gastric parietal cells. Interestingly, IQGAP2 is polarized to the apical membrane of the parietal cells, whereas IQGAP1 is mainly distributed to the basolateral membrane. An IQGAP peptide that competes with full-length IQGAP proteins for Cdc42-binding in vitro also inhibits acid secretion in streptolysin-O-permeabilized gastric glands. Furthermore, this peptide disrupts the association of IQGAP and Cdc42 with the apical actin cytoskeleton and prevents the apical membrane remodeling upon stimulation. We propose that IQGAP2 forms a link that associates Cdc42 with the apical cytoskeleton and thus allows for activation of polarized secretion in gastric parietal cells.

scholarly journals Polarized distribution of actin isoforms in gastric parietal cells.

1995 ◽  
Vol 6 (5) ◽  
pp. 541-557 ◽  
Author(s):  
X Yao ◽  
C Chaponnier ◽  
G Gabbiani ◽  
J G Forte
Keyword(s):  
Epithelial Cells ◽  
Basolateral Membrane ◽  
Parietal Cells ◽  
Gastric Epithelial Cells ◽  
Intense Staining ◽  
Actin Isoforms ◽  
Specific Antibodies ◽  
Beta Actin ◽  
Actin Isoform ◽  
Gastric Parietal Cells

The actin genes encode several structurally similar, but perhaps functionally different, protein isoforms that mediate contractile function in muscle cells and determine the morphology and motility in nonmuscle cells. To reveal the isoform profile in the gastric monomeric actin pool, we purified actin from the cytosol of gastric epithelial cells by DNase I affinity chromatography followed by two-dimensional gel electrophoresis. Actin isoforms were identified by Western blotting with a monoclonal antibody against all actin isoforms and two isoform-specific antibodies against cytoplasmic beta-actin and gamma-actin. Densitometry revealed a ratio for beta-actin/gamma-actin that equaled 0.73 +/- 0.09 in the cytosol. To assess the distribution of actin isoforms in gastric glandular cells in relation to ezrin, a putative membrane-cytoskeleton linker, we carried out double immunofluorescence using actin-isoform-specific antibodies and ezrin antibody. Immunostaining confirmed that ezrin resides mainly in canaliculi and apical plasma membrane of parietal cells. Staining for the beta-actin isoform was intense along the entire gland lumen and within the canaliculi of parietal cells, thus predominantly near the apical membrane of all gastric epithelial cells, although lower levels of beta-actin were also identified near the basolateral membrane. The gamma-actin isoform was distributed heavily near the basolateral membrane of parietal cells, with much less intense staining of parietal cell canaliculi and no staining of apical membranes. Within parietal cells, the cellular localization of beta-actin, but not gamma-actin, isoform superimposed onto that of ezrin. In a search for a possible selective interaction between actin isoforms and ezrin, we carried out immunoprecipitation experiments on gastric membrane extracts in which substantial amounts of actin were co-eluted with ezrin from an anti-ezrin affinity column. The ratio of beta-actin/gamma-actin in the immunoprecipitate (beta/gamma = 2.14 +/- 0.32) was significantly greater than that found in the cytosolic fraction. In summary, we have shown that beta- and gamma-actin isoforms are differentially distributed in gastric parietal cells. Furthermore, our data suggest a preferential, but not exclusive, interaction between beta-actin and ezrin in gastric parietal cells. Finally, our results suggest that the beta- and gamma-actin-based cytoskeleton networks might function separately in response to the stimulation of acid secretion.

Prostaglandin E2 output by isolated rat gastric parietal cells and non-parietal epithelial cells

1988 ◽  
Vol 36 (5) ◽  
pp. 589-600 ◽  
Author(s):  
S. Ota ◽  
M. Razandi ◽  
W. Krause ◽  
A. Terano ◽  
H. Hiraishi ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Prostaglandin E2 ◽  
Parietal Cells ◽  
Parietal Epithelial Cells ◽  
Gastric Parietal Cells ◽  
Isolated Rat

Identification of a basolateral Cl−/HCO 3 − exchanger specific to gastric parietal cells

2003 ◽  
Vol 284 (6) ◽  
pp. G1093-G1103 ◽  
Author(s):  
Snezana Petrovic ◽  
Xie Ju ◽  
Sharon Barone ◽  
Ursula Seidler ◽  
Seth L. Alper ◽  
...  
Keyword(s):  
Acid Secretion ◽  
Gastric Acid Secretion ◽  
Gastric Acid ◽  
Basolateral Membrane ◽  
Parietal Cells ◽  
Rt Pcr ◽  
Functional Studies ◽  
Distribution Studies ◽  
Immunofluorescence Labeling ◽  
Gastric Parietal Cells

The basolateral Cl−/HCO[Formula: see text] exchanger in parietal cells plays an essential role in gastric acid secretion mediated via the apical gastric H+-K+-ATPase. Here, we report the identification of a new Cl−/HCO[Formula: see text]exchanger, which shows exclusive expression in mouse stomach and kidney, with expression in the stomach limited to the basolateral membrane of gastric parietal cells. Tissue distribution studies by RT-PCR and Northern hybridizations demonstrated the exclusive expression of this transporter, also known as SLC26A7, to stomach and kidney, with the stomach expression significantly more abundant. No expression was detected in the intestine. Cellular distribution studies by RT-PCR and Northern hybridizations demonstrated predominant localization of SLC26A7 in gastric parietal cells. Immunofluorescence labeling localized this exchanger exclusively to the basolateral membrane of gastric parietal cells, and functional studies in oocytes indicated that SLC26A7 is a DIDS-sensitive Cl−/HCO[Formula: see text] exchanger that is active in both acidic and alkaline pHi. On the basis of its unique expression pattern and function, we propose that SLC26A7 is a basolateral Cl−/HCO[Formula: see text] exchanger in gastric parietal cells and plays a major role in gastric acid secretion.

scholarly journals Sonic hedgehog is associated with H+-K+-ATPase-containing membranes in gastric parietal cells and secreted with histamine stimulation

2008 ◽  
Vol 295 (1) ◽  
pp. G99-G111 ◽  
Author(s):  
Yana Zavros ◽  
Melissa A. Orr ◽  
Chang Xiao ◽  
Danuta H. Malinowska
Keyword(s):  
Sonic Hedgehog ◽  
Proteolytic Enzymes ◽  
Gradient Centrifugation ◽  
Basolateral Membrane ◽  
Gastric Gland ◽  
Parietal Cells ◽  
Human Gastric Cancer ◽  
Gastric Glands ◽  
Α Subunit ◽  
Gastric Parietal Cells

Sonic hedgehog (Shh) is found within gastric parietal cells and processed from a 45-kDa to a 19-kDa bioactive protein by an acid- and protease-dependent mechanism. To investigate whether Shh is associated with the parietal cell membrane compartment that becomes exposed to both acid and proteolytic enzymes during acid secretion, the cellular location of Shh within resting and stimulated gastric parietal cells was examined. Immunofluorescence microscopy of rabbit stomach sections showed that Shh colocalized predominantly with parietal and pit, not chief/zymogen or neck, cell markers. In resting and histamine-stimulated rabbit gastric glands Shh was expressed only in parietal cells close to H+-K+-ATPase-containing tubulovesicular and secretory membranes with some colocalizing with γ-actin at the basolateral membrane. Gastric gland microsomal membranes were prepared by differential and sucrose gradient centrifugation and immunoisolation with an anti-H+-K+-ATPase-α subunit antibody. The 45- and 19-kDa Shh proteins were detected by immunoblot in immunopurified H+-K+-ATPase-containing membranes from resting and stimulated gastric glands, respectively. Incubating glands with a high KCl concentration removed Shh from the membranes. Histamine stimulated 19-kDa Shh secretion from gastric glands into the medium. In human gastric cancer 23132/87 cells cultured on permeable membranes, histamine increased 19-kDa Shh secretion into both apical and basolateral media. These findings show that Shh is a peripheral protein associated with resting and stimulated H+-K+-ATPase-expressing membranes. In addition, Shh appears to be expressed at or close to the basolateral membrane of parietal cells.

scholarly journals Inhibition of small-conductance Cl- channels by the interleukin-1 -stimulated production of superoxide in rabbit gastric parietal cells

2003 ◽  
Vol 551 (1) ◽  
pp. 207-217 ◽  
Author(s):  
H. Sakai ◽  
Y. Ohira ◽  
A. Tanaka ◽  
T. Suzuki ◽  
A. Ikari ◽  
...  
Keyword(s):  
Interleukin 1 ◽  
Parietal Cells ◽  
Cl Channels ◽  
Gastric Parietal Cells ◽  
Small Conductance

A basolateral CHIP28/MIP26-related protein (BLIP) in kidney principal cells and gastric parietal cells

1994 ◽  
Vol 267 (3) ◽  
pp. C812-C820 ◽  
Author(s):  
G. Valenti ◽  
J. M. Verbavatz ◽  
I. Sabolic ◽  
D. A. Ausiello ◽  
A. S. Verkman ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Basolateral Membrane ◽  
Water Channel ◽  
Protein S ◽  
High Water ◽  
Protein Band ◽  
Parietal Cells ◽  
Toad Urinary Bladder ◽  
Principal Cells ◽  
Gastric Parietal Cells

The water channel CHIP28 accounts for the high water permeability of proximal tubules and thin descending limbs of Henle; a homologous water channel, WCH-CD, in the apical membrane of collecting duct principal cells, may be the vasopressin-sensitive water channel. We show here that one antiserum, raised against CHIP28, immunostains the basolateral membrane of collecting duct principal cells, in addition to staining CHIP28 in other cells. This serum was named anti-basolateral integral protein (anti-BLIP) to distinguish it from other anti-CHIP28 antisera. By Western blotting, BLIP serum recognized both CHIP28 and MIP26, and it stained lens fibers, which contain MIP26 but not CHIP28. BLIP antiserum immunoprecipitated a 28-kDa band, a broad 35- to 50-kDa band, and an approximately 16-kDa band from kidney papilla. It also stained the basolateral membrane of gastric parietal cells, which were not stained with anti-CHIP28 or anti-MIP26 antibodies. BLIP antiserum immunoprecipitated a 28-kDa protein band from stomach; this protein was not precipitated by anti-CHIP28 antibodies. These results suggest that basolateral membranes of principal cells and parietal cells contain a protein(s) that shares common epitopes with CHIP28 and MIP26. Finally, BLIP but not CHIP28 antiserum stained mesothelial (but not epithelial) cells of toad urinary bladder, a further indication that the BLIP antiserum recognizes a protein distinct from CHIP28.

Prostaglandin E2 output is greater by isolated rat gastric parietal cells than non-parietal cells

1988 ◽  
Vol 36 (5) ◽  
pp. 585-587 ◽  
Author(s):  
S. Ota ◽  
M. Razandi ◽  
W. Krause ◽  
A. Terano ◽  
H. Hiraishi ◽  
...  
Keyword(s):  
Prostaglandin E2 ◽  
Parietal Cells ◽  
Gastric Parietal Cells ◽  
Isolated Rat
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