scholarly journals Tissue and species distribution of the secreted carbonic anhydrase isoenzyme

1989 ◽  
Vol 259 (1) ◽  
pp. 91-96 ◽  
Author(s):  
R T Fernley ◽  
P Darling ◽  
P Aldred ◽  
R D Wright ◽  
J P Coghlan
Keyword(s):  
Acinar Cells ◽  
High Molecular Mass ◽  
Northern Analysis ◽  
Carbonic Anhydrases ◽  
Parotid Glands ◽  
Hybridization Histochemistry ◽  
Western Analysis ◽  
Mouse Sequence ◽  
Sheep Parotid ◽  
Aromatic Cluster

The secreted carbonic anhydrases, CA VI, are high molecular mass, oligomeric enzymes originally found in the sheep parotid gland and saliva. The enzymes have been purified from the saliva or parotid glands of several different species. All the CA VI enzymes studied have an apparent subunit Mr of about 45,000 as previously reported for the sheep enzyme. By Western analysis, CA VI from human, cow and dog cross-reacted with antibody raised against the purified sheep enzyme whereas that of the mouse did not. The N-terminal sequences of the sheep, human, cow and mouse enzymes are reported. The sheep, cow and human N-terminal sequences are similar to one another while the mouse sequence is substantially different. Nevertheless, the amino acids in the aromatic cluster I (Trp-5, Tyr-7, Trp-16 and Tyr/Phe-20) have all been conserved, as is the case with the cytoplasmic carbonic anhydrases. Eighteen tissues from the sheep have been examined for the presence of CA VI by Western analysis but it has been found only in the salivary glands. Northern analysis and hybridization histochemistry show that the mRNA for CA VI in sheep is expressed specifically in the acinar cells of the parotid and submandibular glands.

scholarly journals Preparation and characterization of basolateral plasma-membrane vesicles from sheep parotid glands. Mechanisms of phosphate and d-glucose transport

1991 ◽  
Vol 279 (3) ◽  
pp. 843-848 ◽  
Author(s):  
S Vayro ◽  
R Kemp ◽  
R B Beechey ◽  
S Shirazi-Beechey
Keyword(s):  
Basolateral Membrane ◽  
Membrane Vesicles ◽  
Acinar Cells ◽  
Tissue Homogenate ◽  
Basolateral Membrane Vesicles ◽  
Parotid Glands ◽  
Plasma Membrane Vesicles ◽  
Basolateral Plasma Membrane ◽  
Sheep Parotid

A procedure is described for the preparation of basolateral membrane vesicles from the acinar cells of the sheep parotid gland. The ouabain-sensitive K(+)-activated phosphatase activity was enriched 30-fold over the tissue homogenate; 45% of this activity was recovered in the final membrane fraction. The presence of membranes from other organelles was negligible. Evidence is presented for the location of Na(+)-dependent symporters for phosphate and D-glucose on the basolateral membrane.

Ultrastructure of the Parotid Gland of the Nine-Banded Armadillo

1977 ◽  
Vol 35 ◽  
pp. 640-641
Author(s):  
J. R. Ruby
Keyword(s):  
Endoplasmic Reticulum ◽  
Parotid Gland ◽  
Periodic Acid ◽  
Acinar Cells ◽  
Duct System ◽  
Parotid Glands ◽  
Dasypus Novemcinctus ◽  
Anterior Portion ◽  
Periodic Acid Schiff ◽  
Thin Sections

Parotid glands were obtained from five adult (four male and one female) armadillos (Dasypus novemcinctus) which were perfusion-fixed. The glands were located in a position similar to that of most mammals. They extended interiorly to the anterior portion of the submandibular gland.In the light microscope, it was noted that the acini were relatively small and stained strongly positive with the periodic acid-Schiff (PAS) and alcian blue techniques, confirming the earlier results of Shackleford (1). Based on these qualities and other structural criteria, these cells have been classified as seromucous (2). The duct system was well developed. There were numerous intercalated ducts and intralobular striated ducts. The striated duct cells contained large amounts of PAS-positive substance.Thin sections revealed that the acinar cells were pyramidal in shape and contained a basally placed, slightly flattened nucleus (Fig. 1). The rough endoplasmic reticulum was also at the base of the cell.

scholarly journals Electrogenic NBCe1 (SLC4A4), but not electroneutral NBCn1 (SLC4A7), cotransporter undergoes cholinergic-stimulated endocytosis in salivary ParC5 cells

2008 ◽  
Vol 295 (5) ◽  
pp. C1385-C1398 ◽  
Author(s):  
Clint Perry ◽  
David O. Quissell ◽  
Mary E. Reyland ◽  
Irina I. Grichtchenko
Keyword(s):  
Membrane Trafficking ◽  
Basolateral Membrane ◽  
Fluorescent Microscopy ◽  
Acinar Cells ◽  
Fluid Secretion ◽  
Parotid Glands ◽  
Calmodulin Antagonist ◽  
Parotid Acinar Cells ◽  
Early Endosomes ◽  
Gf 109203X

Cholinergic agonists are major stimuli for fluid secretion in parotid acinar cells. Saliva bicarbonate is essential for maintaining oral health. Electrogenic and electroneutral Na+-HCO3− cotransporters (NBCe1 and NBCn1) are abundant in parotid glands. We previously reported that angiotensin regulates NBCe1 by endocytosis in Xenopus oocytes. Here, we studied cholinergic regulation of NBCe1 and NBCn1 membrane trafficking by confocal fluorescent microscopy and surface biotinylation in parotid epithelial cells. NBCe1 and NBCn1 colocalized with E-cadherin monoclonal antibody at the basolateral membrane (BLM) in polarized ParC5 cells. Inhibition of constitutive recycling with the carboxylic ionophore monensin or the calmodulin antagonist W-13 caused NBCe1 to accumulate in early endosomes with a parallel loss from the BLM, suggesting that NBCe1 is constitutively endocytosed. Carbachol and PMA likewise caused redistribution of NBCe1 from BLM to early endosomes. The PKC inhibitor, GF-109203X, blocked this redistribution, indicating a role for PKC. In contrast, BLM NBCn1 was not downregulated in parotid acinar cells treated with constitutive recycling inhibitors, cholinergic stimulators, or PMA. We likewise demonstrate striking differences in regulation of membrane trafficking of NBCe1 vs. NBCn1 in resting and stimulated cells. We speculate that endocytosis of NBCe1, which coincides with the transition to a steady-state phase of stimulated fluid secretion, could be a part of acinar cell adjustment to a continuous secretory response. Stable association of NBCn1 at the membrane may facilitate constitutive uptake of HCO3− across the BLM, thus supporting HCO3− luminal secretion and/or maintaining acid-base homeostasis in stimulated cells.

Targeted disruption of the Nhe1 gene fails to inhibit β1-adrenergic receptor-induced parotid gland hypertrophy

2001 ◽  
Vol 280 (4) ◽  
pp. G694-G700
Author(s):  
James E. Melvin ◽  
Ha-Van Nguyen ◽  
Keith Nehrke ◽  
Claire M. Schreiner ◽  
Kelly G. Ten Hagen ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Adrenergic Receptor ◽  
Acinar Cells ◽  
Receptor Activation ◽  
Parotid Glands ◽  
Targeted Disruption ◽  
Nhe1 Activity ◽  
Salivary Gland Hypertrophy ◽  
The Relationship

Chronic β1-adrenergic receptor activation results in hypertrophy and hyperplasia of rodent salivary gland acinar cells. Na+/H+ exchanger isoform 1 (NHE1) regulates cell volume and the induction of cell proliferation in many tissues. To investigate the relationship between NHE1 and the response of parotid glands to β1-adrenergic agonists, we examined by Northern blot analysis NHE1 expression in saline-treated mice and mice 30 min and 2, 6, and 24 h after isoproterenol injection. NHE1 transcripts increased ∼50% by 2 h, and a more than twofold increase was noted at 24 h. Isoproterenol did not acutely increase Na+/H+ exchanger activity; however, exchanger activity was significantly elevated by 24 h. To test whether NHE1 activity is essential for inducing salivary gland hypertrophy in vivo, mice with targeted disruption of Nhe1 were treated with isoproterenol. Na+/H+ exchanger activity was absent in acinar cells from Nhe1−/− mice, nevertheless, the lack of NHE1 failed to inhibit isoproterenol-induced hypertrophy. These data directly demonstrate that acinar cell hypertrophy induced by chronic β1-adrenergic receptor stimulation occurs independently of NHE1 activity.

Relationship between muscarinic receptor occupancy and response in rat parotid acinar cells

1993 ◽  
Vol 265 (6) ◽  
pp. G1122-G1127 ◽  
Author(s):  
Y. Dai ◽  
B. J. Baum
Keyword(s):  
Binding Sites ◽  
Equilibrium Constants ◽  
Acinar Cells ◽  
Scatchard Analysis ◽  
Parotid Glands ◽  
Response Curves ◽  
Parotid Acinar Cells ◽  
Receptor Number ◽  
Rat Parotid ◽  
Q Values

To determine whether spare muscarinic cholinergic receptors (mAChRs) exist in rat parotid acinar cells, we examined the effect of propylbenzilylcholine mustard (PBCM) on agonist (carbachol)-stimulated inositol trisphosphate (IP3) formation and on mAChR number, using l-[N-methyl-3H]scopolamine methyl chloride (NMS)-binding assays. Treatment with PBCM (1, 3, 10, 30, 50 nM) for 15 min caused a 5, 22, 60, 66, and 72% decrease, respectively, in maximal IP3 formation stimulated by carbachol as well as a large reduction in the potency of carbachol in eliciting this response. Using these data, equilibrium constants (Ka) for activation of the mAChRs by carbachol were calculated. These Ka values agreed well with Kd values of high-affinity mAChR binding sites determined from carbachol displacement of [3H]NMS binding in parotid acinar cells. Reduction in mAChR number after PBCM treatment was determined by Scatchard analysis of specific [3H]-NMS binding sites and compared with the expected reduction (q values) calculated from dose-response curves for carbachol-stimulated IP3 formation before and after PBCM treatment. PBCM (1, 3, 10, 30 nM) decreased mAChR maximal binding in cells 47.5, 68.9, 82.4, and 85.3%, respectively, which did agree with the approximately 38, 70, 90, and 92% decrease in receptor number expected from the calculated q values. Data demonstrate that PBCM irreversibly inactivates mAChRs in rat parotid cells, and the decrease in receptor number, measured directly from [3H]NMS binding or calculated from receptor theory, is greater than that observed for stimulated IP3 production. These results suggest that a modest (30-40%) population of spare receptors exists for mAChR-mediated IP3 production in rat parotid glands.

Differences in regulation of Ca2+-activated Cl− channels in colonic and parotid secretory cells

1998 ◽  
Vol 274 (1) ◽  
pp. C161-C166 ◽  
Author(s):  
Jorge Arreola ◽  
James E. Melvin ◽  
Ted Begenisich
Keyword(s):  
Kinase Inhibitor ◽  
Acinar Cells ◽  
Secretory Cells ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Parotid Glands ◽  
T84 Cells ◽  
Patch Clamp Technique ◽  
Calmodulin Binding ◽  
Parotid Acinar Cells

We investigated the regulation of Ca2+-activated Cl− channels in cells from the human colonic cell line T84 and acinar cells from rat parotid glands. The participation of multifunctional Ca2+- and calmodulin-dependent protein kinase (CaM kinase) II in the activation of these channels was studied using selective inhibitors of calmodulin and CaM kinase II. Ca2+-dependent Cl− currents were recorded using the whole cell patch-clamp technique. Direct inhibition of CaM kinase II by 40 μM peptide 281–302 or by 10 μM KN-62, another CaM kinase inhibitor, did not block the Cl− current in parotid acinar cells, whereas in T84 cells KN-62 markedly inhibited the Ca2+-dependent Cl− current. We also used the calmodulin-binding domain peptide 290–309 (0.5 μM), which competitively inhibits the activation of CaM kinase II. This peptide reduced the Cl− current in T84 cells by ∼70% but was without effect on the channels in parotid acinar cells. We conclude that the Ca2+-dependent Cl− channels in T84 cells are activated by CaM kinase II but that the channels in parotid acinar cells must be regulated by a fundamentally different Ca2+-dependent mechanism that does not utilize CaM kinase II or any calmodulin-dependent process.

scholarly journals Lorazepam induces acinar cells apoptosis of rat parotid glands

2020 ◽  
Vol 32 (6) ◽  
pp. 276-282
Author(s):  
Patrícia Vida Cassi Bettega ◽  
Aline Cristina Batista Rodrigues Johann ◽  
Mariana Rinaldi ◽  
Sérgio Aparecido Ignácio ◽  
Edvaldo Antônio Ribeiro Rosa ◽  
...  
Keyword(s):  
Acinar Cells ◽  
Parotid Glands ◽  
Rat Parotid

Functional and molecular characterization of the fluid secretion mechanism in human parotid acinar cells

2007 ◽  
Vol 292 (6) ◽  
pp. R2380-R2390 ◽  
Author(s):  
Tetsuji Nakamoto ◽  
Alaka Srivastava ◽  
Victor G. Romanenko ◽  
Catherine E. Ovitt ◽  
Patricia Perez-Cornejo ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Ion Transport ◽  
Acinar Cells ◽  
Fluid Secretion ◽  
K Channel ◽  
Resting Membrane Potential ◽  
Specific Cell ◽  
Parotid Glands ◽  
Voltage Dependent ◽  
Intracellular Ca

The strategies available for treating salivary gland hypofunction are limited because relatively little is known about the secretion process in humans. An initial microarray screen detected ion transport proteins generally accepted to be critically involved in salivation. We tested for the activity of some of these proteins, as well as for specific cell properties required to support fluid secretion. The resting membrane potential of human acinar cells was near −51 mV, while the intracellular [Cl−] was ∼62 mM, about fourfold higher than expected if Cl ions were passively distributed. Active Cl− uptake mechanisms included a bumetanide-sensitive Na+-K+-2Cl− cotransporter and paired DIDS-sensitive Cl−/HCO3− and EIPA-sensitive Na+/H+ exchangers that correlated with expression of NKCC1, AE2, and NHE1 transcripts, respectively. Intracellular Ca2+ stimulated a niflumic acid-sensitive Cl− current with properties similar to the Ca2+-gated Cl channel BEST2. In addition, intracellular Ca2+ stimulated a paxilline-sensitive and voltage-dependent, large-conductance K channel and a clotrimazole-sensitive, intermediate-conductance K channel, consistent with the detection of transcripts for KCNMA1 and KCNN4, respectively. Our results demonstrate that the ion transport mechanisms in human parotid glands are equivalent to those in the mouse, confirming that animal models provide valuable systems for testing therapies to prevent salivary gland dysfunction.

scholarly journals Acinar Cells Are Target Cells for Androgens in Mouse Submandibular Glands

1998 ◽  
Vol 46 (5) ◽  
pp. 669-678 ◽  
Author(s):  
Mario Señorale-Pose ◽  
Arnaud Jacqueson ◽  
François Rougeon ◽  
Isabelle Rosinski-Chupin
Keyword(s):  
In Situ Hybridization ◽  
Acinar Cells ◽  
Target Cells ◽  
Parotid Glands ◽  
Specific Expression ◽  
Rnase Protection ◽  
Submandibular Glands ◽  
Androgen Action ◽  
Proline Rich Protein

The variable coding sequence (VCS) multigene family encodes diverse salivary proteins, such as the SMR1 prohormone and the PR-VB1 proline-rich protein in the rat. In situ hybridization was used to study the cell-specific expression of two new mouse VCS genes, Vcs1 and Vcs2. We show that the Vcs1 transcripts, which code for a proline-rich protein, MSG1, are highly abundant in male and female parotid glands, in which they are specifically detected in acinar cells. No expression was seen in the submandibular or sublingual glands. In contrast, Vcs2 transcripts were found only in the acinar cells of the submandibular glands (SMGs) of male mice, in which they are expressed in response to androgens. Expression was found to be heterogeneous within acinar structures. No Vcs2 transcripts were detected in the SMGs of females or castrated males by Northern blot, RNase protection, or in situ hybridization. Androgen administration to females or castrated males induced expression at a level comparable to that of intact males. The Vcs2 gene is the first example of a mouse androgen-regulated gene that is expressed in SMG acinar cells. This result, in addition to our previous observation on SMR1 expression in rats, demonstrates that both acinar cells and granular convoluted tubule (GCT) cells are target cells for androgen action in rodent SMG.

Antigen-presenting cells in parotid glands contain cystatin D originating from acinar cells

2013 ◽  
Vol 530 (1) ◽  
pp. 32-39 ◽  
Author(s):  
Tomoko Nashida ◽  
Ritsuko Sato ◽  
Maiko Haga-Tsujimura ◽  
Sumio Yoshie ◽  
Ken Yoshimura ◽  
...  
Keyword(s):  
Acinar Cells ◽  
Antigen Presenting Cells ◽  
Parotid Glands ◽  
Antigen Presenting
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