The Difference of Aquaporin 5 Distribution in Acinar and Ductal Cells in Lacrimal and Parotid Glands

2007 ◽  
Vol 32 (11) ◽  
pp. 923-929 ◽  
Author(s):  
Yasumasa Sasaki ◽  
Kazuo Tsubota ◽  
Jitesh D. Kawedia ◽  
Anil G. Menon ◽  
Masato Yasui
Keyword(s):  
Parotid Glands ◽  
Aquaporin 5 ◽  
Ductal Cells ◽  
The Difference

Evaluation of the toxic effect of silver nanoparticles and the possible protective effect of ascorbic acid on the parotid glands of albino rats: An in vivo study

2020 ◽  
Vol 36 (6) ◽  
pp. 446-453
Author(s):  
Salma Awad Taghyan ◽  
Hend El Messiry ◽  
Medhat Ahmed El Zainy
Keyword(s):  
Silver Nanoparticles ◽  
Ascorbic Acid ◽  
Vitamin C ◽  
Protective Effect ◽  
Toxic Effect ◽  
Toxic Effects ◽  
Control Group ◽  
Albino Rats ◽  
Parotid Glands ◽  
Ductal Cells

This study aimed to evaluate the toxic effect of silver nanoparticles (AgNPs) on the parotid glands (PGs) of albino rats histologically and ultrastructurally and assess the possible protective effect of ascorbic acid as an antioxidant. Thirty male albino rats weighing between 150 mg and 200 mg were divided into three groups: the control group (C1) contained 10 rats that received 2 mg/kg (body weight (bw)) of aqueous nitrate buffer by intraperitoneal (IP) injection daily for 28 days; the AgNPs group contained 10 rats that received 2 mg/kg (bw) IP AgNPs daily for 28 days; and the AgNPs-vitamin C group contained 10 albino rats that received 2 mg/kg (bw) AgNPs IP daily for 28 days with oral administration of 100 mg/kg (bw) vitamin C in drinking water daily for 28 days. The PG acinar and ductal cells of the AgNPs group showed signs of toxicity and degeneration characterized as pleomorphic nuclei, binucleation, cytoplasmic vacuolations, and stagnated secretion in the ductal lumen. In addition to degenerated mitochondria, dilated rough endoplasmic reticulum and lysosomes were filled with AgNPs ( p < 0.001). The AgNPs-vitamin C group showed significantly less degenerative changes histologically and ultrastructurally compared to the AgNPs group ( p = 0.002). AgNPs produced significant toxic effects on the PG of albino rats, presumably through the generation of reactive oxygen species and toxic ion release, and administration of vitamin C was shown effective in decreasing these toxic effects.

scholarly journals Aquaporin-5 water channel in lipid rafts of rat parotid glands

2006 ◽  
Vol 1758 (8) ◽  
pp. 1053-1060 ◽  
Author(s):  
Yasuko Ishikawa ◽  
Gota Cho ◽  
Zhenfang Yuan ◽  
Noriko Inoue ◽  
Yoshiko Nakae
Keyword(s):  
Lipid Rafts ◽  
Water Channel ◽  
Parotid Glands ◽  
Aquaporin 5 ◽  
Rat Parotid

scholarly journals In situ localization of amylase mRNA and protein. An investigation of amylase gene activity in normal human parotid gland.

1987 ◽  
Vol 35 (1) ◽  
pp. 9-14 ◽  
Author(s):  
D J Morley ◽  
M E Hodes
Keyword(s):  
In Situ Hybridization ◽  
Cellular Localization ◽  
Cdna Probe ◽  
Immunohistochemical Localization ◽  
Frozen Sections ◽  
Parotid Glands ◽  
Ductal Cells ◽  
Ethanol Acetic Acid ◽  
Mrna And Protein Expression

The distribution of human salivary amylase mRNA was studied by in situ hybridization to a [32P]-labeled amylase cDNA probe. Amylase mRNA was localized to the apical portion of acinar cells in frozen sections of human parotid salivary gland. No hybridization was noted in ductal cells, skeletal muscle, or in connective tissue. These results were consistent with immunohistochemical localization of amylase. The technique of in situ hybridization was modified to permit localization of amylase mRNA in variously fixed, paraffin-embedded parotid glands. Although the hybridization signal decreased with all fixatives, the pattern of localization paralleled that obtained with frozen sections. No advantage was noted in fixation with ethanol-acetic acid or Bouin solution over routine fixation with formalin. These results have important implications for researchers interested in studies of gene expression. We have demonstrated that routinely fixed paraffin blocks of human tissue can be used for cellular localization of specific mRNA. In coordination with immunocytochemistry, in situ hybridization offers a powerful tool for studies of mRNA and protein expression in individual cells.

Age-related Decreases in the Response of Aquaporin-5 to Acetylcholine in Rat Parotid Glands

2003 ◽  
Vol 82 (6) ◽  
pp. 476-480 ◽  
Author(s):  
N. Inoue ◽  
H. Iida ◽  
Z. Yuan ◽  
Y. Ishikawa ◽  
H. Ishida
Keyword(s):  
Parotid Glands ◽  
Aquaporin 5 ◽  
Age Related ◽  
Rat Parotid

Epithelial-Myoepithelial Carcinoma of Salivary Glands

1992 ◽  
Vol 101 (6) ◽  
pp. 540-542 ◽  
Author(s):  
John G. Batsakis ◽  
Adel K. El-Naggar ◽  
Mario A. Luna
Keyword(s):  
Salivary Gland ◽  
Salivary Glands ◽  
Cell Population ◽  
Phenotypic Expression ◽  
Myoepithelial Cells ◽  
Salivary Gland Neoplasms ◽  
Myoepithelial Carcinoma ◽  
Parotid Glands ◽  
Ductal Cells ◽  
Epithelial Myoepithelial Carcinoma

Epithelial-myoepithelial carcinomas comprise approximately 1 % of all salivary gland neoplasms. They are preponderantly tumors of the parotid glands with a relatively low mortality but a decided locoregional aggressiveness. Histopathologically, the carcinomas are characterized by a dual cell population of epithelial (ductal) cells and myoepithelial cells. These cells vary in their dominance and phenotypic expression

scholarly journals AN ELECTRON MICROSCOPIC STUDY OF ECCRINE SWEAT GLANDS OF THE CAT FOOT AND TOE PADS—EVIDENCE FOR DUCTAL REABSORPTION IN THE HUMAN

1961 ◽  
Vol 11 (2) ◽  
pp. 403-417 ◽  
Author(s):  
Bryce L. Munger ◽  
Saul W. Brusilow
Keyword(s):  
Light And Electron Microscopy ◽  
Sweat Glands ◽  
Striking Difference ◽  
Electron Microscopic ◽  
Ductal Cells ◽  
Before And After ◽  
The Difference ◽  
Foot Pad ◽  
Eccrine Sweat Glands ◽  
Eccrine Sweat

The eccrine sweat glands of the cat foot and toe pads have been studied by light and electron microscopy before and after stimulation with mecholyl. The ultrastructure of these glands in the cat is found to be entirely comparable to that in the human (13). The ultrastructure and staining properties of the secretory segment of the two species are identical. The ductal part of the feline gland is shorter and the ductal cells have only scant mitochondria as compared with the human. Since Brusilow et al. (1) have observed that the secretion of the cat foot pad is isotonic as compared with human sweat, which is hypotonic, and since the secretory segments of the two species are structurally identical, the striking difference in the morphology of the duct is regarded as being responsible for the difference in the chemistry of the secretion of the two species. Thus the duct in the human is capable of reabsorbing sodium and chloride.

scholarly journals The Effect of Adrenergic Agonists and Antagonists on the Expression of Proteins in Rat Submandibular and Parotid Glands

1993 ◽  
Vol 4 (3) ◽  
pp. 565-571 ◽  
Author(s):  
Gurrinder Singh Bedi
Keyword(s):  
Acinar Cells ◽  
Salivary Proteins ◽  
Cysteine Proteinase Inhibitor ◽  
Concomitant Treatment ◽  
Adrenergic Agonists ◽  
Parotid Glands ◽  
Submandibular Glands ◽  
Ductal Cells ◽  
Differential Control ◽  
Control Of Expression

The present investigation was undertaken to study the effect of adrenoreceptor modulators on the expression of salivary proteins. Sprague-Dawley rats were treated for 10 consecutive days with adrenergic agonists isoproterenol, dobutamine, terbutaline, salbutamol, methoxyphenamine, or methoxamine. Antiserum to selected salivary proteins was used to compare the concentration of these proteins in the submandibular and parotid glands of treated animals. Chronic treatments of rats (50 μmol/ kg body weight for 10 d) with either isoproterenol or dobutamine induced synthesis of a cysteine-proteinase inhibitor (cystatin) in the submandibular glands. When isoproterenol was injected concomitantly with the mixed β-antagonist propranolol or the β1-adrenergic antagonists metaprolol, proctocol, or atenolol, the induction of cystatin was totally suppressed. However, the β2-antagonist, ICI-118551, produced only partial reduction in cystatin induction elicited by isoproterenol. On the contrary, rats treated with either isoproterenol or P,-agonists demonstrated a significantly reduced concentration of serine-proteinase kallikrein in submandibular glands. The decrease observed in submandibular kallikrein of rats treated with isoproterenol was prevented by concomitant treatment with β 1,-antagonists but not with β2-antagonists. Because kallikreins are produced by ductal cells and cystatins are produced by acinar cells of submandibular glands, these observations suggest that there may be differential control of expression of proteins synthesized by ductal and acinar cells. Chronic treatment of rats with nonselective P-agonist isoproterenol or β 1,-selective agonists increased markedly the proline-rich proteins (PRP) in parotid glands, but the parotid amylase concentration was not significantly affected by β-adrenergic agonists. Coinjection of β1-antagonists along with isoproterenol blocked the induction of PRP in the parotid glands. These findings suggest that there may be a differential control of expression of proteins by different cell populations of salivary glands.

Temporal Reduction in Size of Salivary Acinus in Rats Induced by Theophylline

2005 ◽  
Vol 33 (2) ◽  
pp. 218-224 ◽  
Author(s):  
Satoru Kajikawa ◽  
Ayano Takeuchi ◽  
Aisuke Nii ◽  
Hiroyuki Nakayama ◽  
Kunio Doi
Keyword(s):  
Salivary Glands ◽  
Time Course ◽  
Water Channel ◽  
Phosphodiesterase Inhibitor ◽  
Repeated Administration ◽  
Receptor Activation ◽  
Parotid Glands ◽  
Aquaporin 5 ◽  
Submaxillary Glands ◽  
Immuno Histochemistry

Repeated administration of theophylline, a phosphodiesterase inhibitor, induces the enlargement of the salivary glands in rats. Time-course changes after a single administration of theophylline were examined in the salivary glands, including phosphodiesterase enzyme activity, and the expression of aquaporin 5 (AQP5), a water channel. We also examined the contribution of β-adrenergic receptors to theophylline-induced salivary changes. Male F344 rats were given 50 mg/kg of theophylline intraperitoneally either alone or concurrently with a 10 mg/kg subcutaneous injection of propranolol. After treatment with theophylline alone, the weight and histology of the submaxillary and parotid glands were examined. Phosphodiesterase activity and AQP5 were detected by enzyme- and immuno-histochemistry, respectively. At 4 hours, 8 hours, or both, organ weights were decreased with depletion of secretory vesicles in the acinar cells. In the submaxillary glands, reduced activity of phosphodiesterase and increased expression of AQP5 in the intercalated ducts were observed at 4 hours. When co-administered, propranolol partially abolished theophylline-induced glandular reduction. These results suggest that the theophylline-induced transient reduction in size of the salivary glands is attributable not only to phosphodiesterase inhibition but also to β-adrenergic receptor activation and that the intercalated ducts in submaxillary glands play a role in the production of saliva.

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