scholarly journals MORFOLOGI DAN HISTOKIMIA KELENJAR MANDIBULARIS WALET LINCHI (Collocalia linchi) SELAMA SATU MUSIM BERBIAK DAN BERSARANG (Morphological and Histochemical Properties of Mandibular Glands of the Cave Swiflets (Collocalia linchi) During Reproductive and Nesting Period)

Author(s):  
Savitri Novelina

The aimed of present study is to investigate the morphological and histochemical of mandibular glands of the cave swiflet (Collocalia linchi). The study used 24 adult wallet linchii paired mandibular gland located in the ventral of the mandible. They were ovoid in form and whitish in color. The gland consisted of mucous acinar cells and waspositive with PAS but negative with AB (pH 2,5). The result suggested that the acinar cells of the mandibular gland contained only neutral mucopolysaccharides and no acid mucopolysaccharides. Staining with 7 biotinylated lectins, Con-A, DBA, WGA, RCA, PNA, SBA, and UEA which represent carbohydrates with galactosa-, Nacetylgalactosamine,sialic acid, 2-5 N-acetylglucosamine, á-D- mannose, showed various positive reaction in the secretion of the acinar cells depends on the type of lectin and sampling period. The result suggested possiblecorrelation between receptor gonadal hormone with the activity of reproductive and nesting period of walet linchi.Keywords: lectin, Collocalia linchi,salivary gland.

2021 ◽  
Vol 17 (1) ◽  
Author(s):  
Eloá Borges Luna ◽  
Pâmella Pinho Montovani ◽  
Rafaela Elvira Rozza-de-Menezes ◽  
Karin Soares Cunha

AbstractIntroductionNeurofibromin, a protein encoded by theNF1gene, is mutated in neurofibromatosis 1, one of the most common genetic diseases. Oral manifestations are common and a high prevalence of hyposalivation was recently described in individuals with neurofibromatosis 1. Although neurofibromin is ubiquitously expressed, its expression levels vary depending on the tissue type and developmental stage of the organism. The role of neurofibromin in the development, morphology, and physiology of salivary glands is unknown and a detailed expression of neurofibromin in human normal salivary glands has never been investigated.AimTo investigate the expression levels and distribution of neurofibromin in acinar and ductal cells of major and minor salivary glands of adult individuals without NF1.Material and methodTen samples of morphologically normal major and minor salivary glands (three samples of each gland: parotid, submandibular and minor salivary; and one sample of sublingual gland) from individuals without neurofibromatosis 1 were selected to assess neurofibromin expression through immunohistochemistry. Immunoquantification was performed by a digital method.ResultsNeurofibromin was expressed in the cytoplasm of both serous and mucous acinar cells, as well as in ducts from all the samples of salivary glands. Staining intensity varied from mild to strong depending on the type of salivary gland and region (acini or ducts). Ducts had higher neurofibromin expression than acinar cells (p = 0.003). There was no statistical association between the expression of neurofibromin and the type of the salivary gland, considering acini (p = 0.09) or ducts (p = 0.50) of the four salivary glands (parotid, submandibular, minor salivary, and sublingual gland). Similar results were obtained comparing the acini (p = 0.35) and ducts (p = 0.50) of minor and major salivary glands. Besides, there was no correlation between the expression of neurofibromin and age (p = 0.08), and sex (p = 0.79) of the individuals, considering simultaneously the neurofibromin levels of acini and duct (n = 34).ConclusionNeurofibromin is expressed in the cytoplasm of serous and mucous acinar cells, and ductal cells of salivary glands, suggesting that this protein is important for salivary gland function.


1964 ◽  
Vol 12 (7) ◽  
pp. 538-544 ◽  
Author(s):  
MAX WACHSTEIN ◽  
ELIZABETH MEISEL

By using an improved benzidine technique, peroxidase activity can be demonstrated in various locations in mammalian tissues. A relatively formalin resistant enzyme is found in hemoglobin and is also associated with mitochondria of striated muscle and heart. A somewhat less formalin resistant peroxidase occurs in the granules of myeloid and mast cells. A relatively formalin sensitive peroxidase is present in a number of additional locations, e.g. the acinar cells in thyroid and salivary gland, the medulla of the kidney, in hair follicles of the guinea pig skin and Kupffer cells of the liver.


1993 ◽  
Vol 4 (5) ◽  
pp. 639-677 ◽  
Author(s):  
Irving Dardick ◽  
Aileen P. Burford-Mason

Because of their complexity and relative infrequency, salivary gland tumors commonly result in diagnostic problems. Histogenetic and morphogenetic concepts of tumorigenesis in these glands are reviewed and their relevance to routine diagnosis and classification of salivary gland tumors evaluated. Evidence is presented from animal and human studies that under steady-state and pathophysiological conditions, all cell types present in the normal gland, including acinar cells, are capable of rapidly entering the cell cycle and are, therefore, possible targets for neoplastic transformation.


Author(s):  
K. R. Lau ◽  
A. C. Elliott ◽  
P. D. Brown ◽  
R. M. Case

2017 ◽  
Vol 2017 ◽  
pp. 1-4 ◽  
Author(s):  
Mark Weitzel ◽  
Jason E. Cohn ◽  
Harvey Spector

Myoepithelioma is a rare salivary gland neoplasm. They most commonly affect the major and minor salivary glands with the parotid gland being the most common, approximately 40%. Only 1% of all salivary gland neoplasms are myoepitheliomas. Myoepithelioma is usually a benign tumor arising from neoplastic myoepithelial or basket cells which are found between the basement membrane and the basal plasma membrane of acinar cells. They also contain multiple cellular elements. We present a case of a 73-year-old female with myoepithelioma of the parotid gland, an extremely rare neoplasm. There have been approximately 42 cases reported through 1985 and fewer than 100 cases through 1993. We will discuss the clinical presentation, pathophysiology, diagnosis, and treatment of such neoplasms.


2001 ◽  
Vol 280 (4) ◽  
pp. G694-G700
Author(s):  
James E. Melvin ◽  
Ha-Van Nguyen ◽  
Keith Nehrke ◽  
Claire M. Schreiner ◽  
Kelly G. Ten Hagen ◽  
...  

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.


10.4081/846 ◽  
2009 ◽  
Vol 47 (4) ◽  
pp. 353 ◽  
Author(s):  
F Parillo ◽  
C Dall’Aglio ◽  
A Verini Supplizi ◽  
P Ceccarelli ◽  
AM Gargiulo

An ultrastructural localization of lectin receptors on the zona pellucida (ZP) of porcine antral oocytes and on the granulosa cells was performed using a panel of horseradish peroxidase- labelled lectins in conjunction with antiperoxidase antibody and protein A-gold. In some cases, lectin incubation was preceded by sialidase digestion. WGA-, Con-A-, UEA-I-, RCA-I-, PNA- and SBA-reactive sites were distributed differently in the porcine ZP. Sialidase digestion increased the positivity obtained with RCA-I and it was necessary to promote PNA and SBA reactivity. These results indicated that the ZP contained N-acetylglucosamine, a-mannose, a- fucose, b-Gal-(1-4)GlcNAc, b-Gal- (1-3)GalNAc, b-GalNAc and sialic acid residues. We also observed the presence of vesicles in both the ooplasm and granulosa cells, showing a similar lectin binding pattern to that of the ZP, thus suggesting that the oocyte and granulosa cells are the site of synthesis of ZP glucidic determinants.


2007 ◽  
Vol 292 (6) ◽  
pp. R2380-R2390 ◽  
Author(s):  
Tetsuji Nakamoto ◽  
Alaka Srivastava ◽  
Victor G. Romanenko ◽  
Catherine E. Ovitt ◽  
Patricia Perez-Cornejo ◽  
...  

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.


Sign in / Sign up

Export Citation Format

Share Document