scholarly journals Immunolocalization of electroneutral Na+-HCO 3 − cotransporters in human and rat salivary glands

2002 ◽  
Vol 283 (2) ◽  
pp. G473-G480 ◽  
Author(s):  
V. Gresz ◽  
T.-H. Kwon ◽  
H. Vorum ◽  
T. Zelles ◽  
I. Kurtz ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Basolateral Membrane ◽  
Salivary Secretion ◽  
Rat Tissues ◽  
Submandibular Glands ◽  
Rat Salivary Glands ◽  
Duct Cells ◽  
Mrna And Protein Expression ◽  
Rat Parotid ◽  
Apical Membranes

Patterns of salivary HCO[Formula: see text]secretion vary widely among species and among individual glands. In particular, virtually nothing is known about the molecular identity of the HCO[Formula: see text] transporters involved in human salivary secretion. We have therefore examined the distribution of several known members of the Na+-HCO[Formula: see text] cotransporter (NBC) family in the parotid and submandibular glands. By use of a combination of RT-PCR and immunoblotting analyses, the electroneutral cotransporters NBC3 and NBCn1 mRNA and protein expression were detected in both human and rat tissues. Immunohistochemistry demonstrated that NBC3 was present at the apical membranes of acinar and duct cells in both human and rat parotid and submandibular glands. NBCn1 was strongly expressed at the basolateral membrane of striated duct cells but not in the acinar cells in the human salivary glands, whereas little or no NBCn1 labeling was observed in the rat salivary glands. The presence of NBCn1 at the basolateral membrane of human striated duct cells suggests that it may contribute to ductal HCO[Formula: see text] secretion. In contrast, the expression of NBC3 at the apical membranes of acinar and duct cells in both human and rat salivary glands indicates a possible role of this isoform in HCO[Formula: see text] salvage under resting conditions.

5-Hydroxytryptamine Modulation of Rat Parotid Salivary Gland Secretion

1989 ◽  
Vol 68 (1) ◽  
pp. 59-63 ◽  
Author(s):  
W. Chernick ◽  
E. Bobyock ◽  
P. Bradford
Keyword(s):  
Salivary Glands ◽  
Salivary Secretion ◽  
Threshold Concentration ◽  
Amylase Secretion ◽  
Cell Aggregates ◽  
Salivary Gland Secretion ◽  
Combined Use ◽  
Rat Parotid

5-Hydroxytryptamine (5-HT) has been reported to produce significant responses in blowfly salivary glands, but little information is available concerning its action on mammalian salivary glands. When 5-HT (0.1 μmol/L to 10 μmol/L) is infused i. a. into anesthetized rats, no salivary secretion is obtained from either parotid or submandibular glands. However, when 5-HT is infused along with a threshold concentration of acetylcholine (0-1 mmol/L), potentiation of parotid secretory response is seen with 5-HT (1 μmol/L, 260% increase; 10 μmol/L, 146% increase). Substance P (0.3 μmol/L) combined with 5-HT (1 μmol/L) also resulted in a potentiation of parotid secretion (160% increase). Protein and calcium concentrations were not altered during such treatments. No potentiation of submandibular secretion was noted. Experiments in vitro with parotid cell aggregates exhibited no potentiation associated with the combined use of 5-HT and carbachol, as measured by amylase secretion and inositol trisphosphate accumulation. The experiments indicate that 5-HT substantially modulates parotid salivary secretion in vivo; however, the in vitro findings suggest that 5-HT does not act directly on surface glandular receptors. The magnitude of the in vivo potentiation could very well implicate circulating or released 5-HT as a physiological modulator of endogenous neurotransmitter action.

scholarly journals Quantitative immunoelectron microscopic localization of (Na+,K+)ATPase in rat parotid gland.

1987 ◽  
Vol 35 (8) ◽  
pp. 871-879 ◽  
Author(s):  
T Iwano ◽  
M Akayama ◽  
A Yamamoto ◽  
K Omori ◽  
T Kumazawa ◽  
...  
Keyword(s):  
Parotid Gland ◽  
Plasma Membranes ◽  
Basolateral Membrane ◽  
Protein A ◽  
Acinar Cells ◽  
Gold Particles ◽  
Duct Cells ◽  
Rat Parotid Gland ◽  
Basal Plasma ◽  
Rat Parotid

Distribution of (Na+,K+)ATPase on the cell membranes of acinar and duct cells of rat parotid gland was investigated quantitatively by immunoelectron microscopy using the post-embedding protein A-gold technique. In acinar cells, ATPase was localized predominantly on the basolateral plasma membranes. A small but significant amount of (Na+,K+)ATPase was, however, detected on the luminal plasma membranes, especially on the microvillar region of the acinar cells; the surface density on the luminal membrane was approximately one third of that on the basolateral membranes. In duct cells, many gold particles were found on the basolateral membrane, especially along the basal infoldings of the plasma membranes, whereas no significant gold particles were found on the luminal plasma membranes, suggesting unilateral distribution of ATPase in duct cells. We suggest that in acinar cells sodium ion is not only transported paracellularly but is also actively transported intracellularly into the luminal space by the (Na+,K+)ATPase located on the luminal plasma membranes, and that water is passively transported to the luminal space to form a plasma-like isotonic primary saliva, while in the duct cells the same ion is selectively re-absorbed intracellularly by (Na+,K+)ATPase found in abundance along the many infoldings of the basal plasma membranes, thus producing the hypotonic saliva.

scholarly journals Kallikrein localization in rodent salivary glands and kidney with the immunoglobulin-enzyme bridge technique.

1979 ◽  
Vol 27 (12) ◽  
pp. 1567-1576 ◽  
Author(s):  
J A Simson ◽  
S S Spicer ◽  
J Chao ◽  
L Grimm ◽  
H S Margolius
Keyword(s):  
Salivary Glands ◽  
Distal Tubule ◽  
Female Rats ◽  
Apical Region ◽  
Submandibular Glands ◽  
Granular Convoluted Tubule ◽  
Duct Cells ◽  
Male And Female Rats ◽  
Rats And Mice ◽  
Convoluted Tubules

Kallikrein has been localized in rodent kidney and salivary glands by means of an immunoglobulin-enzyme bridge technique. In sections of kidney, anti-kallikrein antibodies bound to the apical region of certain distal tubule segments in the cortex, to reabsorption droplets of proximal convoluted tubules, and to certain duct segments in the papilla. In salivary glands of both male and female rats and mice, and apical rim of most striated duct cells of submandibular, parotid and sublingual glands and granular tubules of submandibular glands exhibited immunoreactivity. Granular intercalated duct cells in female submandibular glands also displayed immunostaining for kallikrein. Phenylephrine administration resulted in loss of immunoreactive granules from the granular convoluted tubule cells of male mouse submandibular gland. This response was paralleled by a biochemically demonstrable decrease in kallikrein-like tosylarginine methyl ester (TAME) esterase activity.

Dopamine stimulates salivary duct cells in the cockroach Periplaneta americana

1999 ◽  
Vol 202 (6) ◽  
pp. 729-738 ◽  
Author(s):  
I. Lang ◽  
B. Walz
Keyword(s):  
Membrane Potential ◽  
Salivary Glands ◽  
Periplaneta Americana ◽  
Basolateral Membrane ◽  
Fluid Secretion ◽  
Intracellular Recordings ◽  
Salivary Duct ◽  
Duct Cells ◽  
Dose Dependent ◽  
Basolateral Membrane Potential

This study examines whether the salivary duct cells of the cockroach Periplaneta americana can be stimulated by the neurotransmitters dopamine and serotonin. We have carried out digital Ca2+-imaging experiments using the Ca2+-sensitive dye fura-2 and conventional intracellular recordings from isolated salivary glands. Dopamine evokes a slow, almost tonic, and reversible dose-dependent elevation in [Ca2+]i in the duct cells. Upon stimulation with 10(−)6 mol l-1 dopamine, [Ca2+]i rises from 48+/−4 nmol l-1 to 311+/−43 nmol l-1 (mean +/− s.e.m., N=18) within 200–300 s. The dopamine-induced elevation in [Ca2+]i is absent in Ca2+-free saline and is blocked by 10(−)4 mol l-1 La3+, indicating that dopamine induces an influx of Ca2+ across the basolateral membrane of the duct cells. Stimulation with 10(−)6 mol l-1 dopamine causes the basolateral membrane to depolarize from −67+/−1 to −41+/−2 mV (N=10). This depolarization is also blocked by La3+ and is abolished when Na+ in the bath solution is reduced to 10 mmol l-1. Serotonin affects neither [Ca2+]i nor the basolateral membrane potential of the duct cells. These data indicate that the neurotransmitter dopamine, which has previously been shown to stimulate fluid secretion from the glands, also stimulates the salivary duct cells, suggesting that dopamine controls their most probable function, the modification of primary saliva.

scholarly journals Differential localization of "brain-specific" S-100 and its subunits in rat salivary glands.

1984 ◽  
Vol 32 (8) ◽  
pp. 805-814 ◽  
Author(s):  
S O Molin ◽  
L Rosengren ◽  
K Haglid ◽  
J Baudier ◽  
A Hamberger
Keyword(s):  
Salivary Glands ◽  
Submandibular Gland ◽  
Beta Subunit ◽  
Ependymal Cells ◽  
Beta Subunits ◽  
Differential Distribution ◽  
Rat Salivary Glands ◽  
Duct Cells ◽  
S 100

In the rat, the S-100 antigens in the submandibular gland were found to be immunochemically identical with those in the brain (glial cells) when compared using crossed immunoelectrophoresis. Specific antibodies against the S-100a non-beta and against the S-100 beta subunit were prepared from antibodies against crude S-100 protein and from S-100 components (S-100a and b) by affinity chromatography. In the rat salivary glands a differential distribution of subunit immunoreactivity was clearly evidenced using indirect immunofluorescence. Certain intercalated duct cells of the submandibular gland as well as Schwann cells contained the S-100 beta subunit immunoreactivity exclusively, while other duct cells in parotid, submandibular, and sublingual glands contained S-100a non-beta subunit immunoreactivity. Both subunits were present in astrocytes and ependymal cells. The immunocytochemical localization of alpha and beta subunits is a promising technique for the classification of various types of S-100-containing cells.

Immunolocalization of AQP-5 in rat parotid and submandibular salivary glands after stimulation or inhibition of secretion in vivo

2004 ◽  
Vol 287 (1) ◽  
pp. G151-G161 ◽  
Author(s):  
Veronika Gresz ◽  
Tae-Hwan Kwon ◽  
Hong Gong ◽  
Peter Agre ◽  
Martin C. Steward ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Subcellular Localization ◽  
Salivary Glands ◽  
Salivary Secretion ◽  
Apical Plasma Membrane ◽  
Secretory Cells ◽  
Muscarinic Agonist ◽  
Rat Parotid

In vitro studies of cultured salivary gland cells and gland slices have indicated that there may be regulated translocation of aquaporin (AQP)-5 between the apical plasma membrane and intracellular compartments of the secretory cells. However, it remains unknown whether AQP-5 in salivary glands is subject to regulated trafficking in vivo. To examine this possibility, we have investigated the subcellular localization of AQP-5 in rat parotid and submandibular glands fixed in vivo under conditions of stimulated or inhibited salivary secretion. Immunofluorescence and immunoelectron microscopy was used to determine the subcellular distribution of AQP-5 in control conditions following the stimulation of secretion with pilocarpine (a muscarinic agonist) or epinephrine (an α-adrenoceptor agonist) or during inhibition of basal secretion with atropine (a muscarinic antagonist) or phentolamine (an α-adrenoceptor antagonist). Under control conditions, >90% of AQP-5 was associated with the apical plasma membrane of acinar and intercalated duct cells, with only rare gold particles associated with intracellular membrane domains. Pilocarpine treatment dramatically increased saliva production but had no discernible effect on AQP-5 distribution. However, the increased salivary secretion was associated with luminal dilation and the appearance of a markedly punctate AQP-5 labeling pattern due to clustering of AQP-5 at the microvilli (especially evident in the parotid gland) after 10 min of drug injection. No changes in the subcellular localization of AQP-5 were seen in response to epinephrine, atropine, or phentolamine treatment compared with control tissues. Thus AQP-5 is localized predominantly in the apical plasma membrane under control conditions, and neither the onset nor the cessation of secretion is associated in vivo with any significant short-term translocation of AQP-5 between intracellular structures and the apical plasma membrane.

Biogenesis of Catalase-Positive Rods in Excretory Duct Cells of Salivary Glands

1976 ◽  
Vol 34 ◽  
pp. 62-63
Author(s):  
Dwight K. Romanovicz ◽  
Jacob S. Hanker
Keyword(s):  
Light Microscopy ◽  
Salivary Glands ◽  
Submandibular Gland ◽  
Excretory Duct ◽  
Exocrine Glands ◽  
Duct Cells ◽  
Peroxidatic Activity ◽  
Microscopic Studies ◽  
Different Dimensions

The presence of catalase-positive rods (Fig. 1) of different dimensions, which frequently have a crystalline appearance by light microscopy, has been reported. They seem to be related to peroxisomes which were characterized morphologically and cytochemically in parotid and other exocrine glands of the rat by Hand in 1973. Our light microscopic studies of these spherical microbodies and rods of different sizes, stained by virtue of the peroxidatic activity of their catalase, indicate that they are almost entirely confined to the cells of the striated and execretory ducts of the submandibular gland in the mouse. The rods were usually noted only in the proximity of the ductal microbodies. The latter frequently showed a tendency to appear in linear close array, or even to be contiguous (Fig. 2). This suggested that the rods could be formed by the fusion of microbodies.

scholarly journals Electron Microscopic Immunogold Localization of Salivary Mucins MG1 and MG2 in Human Submandibular and Sublingual Glands

2003 ◽  
Vol 51 (1) ◽  
pp. 69-79 ◽  
Author(s):  
Marco Piludu ◽  
Sean A. Rayment ◽  
Bing Liu ◽  
Gwynneth D. Offner ◽  
Frank G. Oppenheim ◽  
...  
Keyword(s):  
Salivary Glands ◽  
Expression Patterns ◽  
Cell Types ◽  
Mucous Cells ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Dense Cores ◽  
Duct Cells ◽  
Rabbit Igg ◽  
Lowicryl K4m

The human salivary mucins MG1 and MG2 are well characterized biochemically and functionally. However, there is disagreement regarding their cellular and glandular sources. The aim of this study was to define the localization and distribution of these two mucins in human salivary glands using a postembedding immunogold labeling method. Normal salivary glands obtained at surgery were fixed in 3% paraformaldehyde-0.1% glutaraldehyde and embedded in Lowicryl K4M or LR Gold resin. Thin sections were labeled with rabbit antibodies to MG1 or to an N-terminal synthetic peptide of MG2, followed by gold-labeled goat anti-rabbit IgG. The granules of all mucous cells of the submandibular and sublingual glands were intensely reactive with anti-MG1. No reaction was detected in serous cells. With anti-MG2, the granules of both mucous and serous cells showed reactivity. The labeling was variable in both cell types, with mucous cells exhibiting a stronger reaction in some glands and serous cells in others. In serous granules, the electron-lucent regions were more reactive than the dense cores. Intercalated duct cells near the acini displayed both MG1 and MG2 reactivity in their apical granules. In addition, the basal and lateral membranes of intercalated duct cells were labeled with anti-MG2. These results confirm those of earlier studies on MG1 localization in mucous cells and suggest that MG2 is produced by both mucous and serous cells. They also indicate differences in protein expression patterns among salivary serous cells.

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