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

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.

Author(s):  
Dwight K. Romanovicz ◽  
Jacob S. Hanker

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.


1987 ◽  
Vol 35 (10) ◽  
pp. 1053-1058 ◽  
Author(s):  
J I Morrell ◽  
E W Gresik ◽  
T Barka

Mouse submandibular glands show an androgen-dependent sexual dimorphism, reflected in higher concentrations in males than in females of bioactive peptides, such as epidermal growth factor (EGF), nerve growth factor, and renin in the cells of the granular convoluted tubules (GCT). Biochemical studies have demonstrated androgen receptors in submandibular gland and other androgen-responsive organs in mouse. We have determined the cellular localization of these receptors using steroid autoradiography. Fifteen adult gonadectomized male mice were injected intravenously with 0.13 microgram or 0.26 microgram [3H]-dihydrotestosterone (SA 135 Ci/mM); some animals were pre-treated with cyclocytidine to stimulate secretion by GCT cells. Animals were killed 15 min, 1, 2, or 3 hr after isotope injection. Steroid autoradiographs were prepared, and some were stained immunocytochemically for EGF. Of the different cell types of submandibular gland, the acinar cells most frequently and intensely concentrated [3H]-DHT; GCT cells also concentrated the hormone, as did a small number of striated duct cells. In the other major salivary glands, the only cells that concentrated the androgen were interlobular striated duct cells in sublingual gland. In prostate, anterior pituitary, and brain a large number of cells concentrated androgen, as has been previously reported. Androgen binding by the GCT cells was a predictable finding, since androgen-induced alterations in composition and form of these cells are well documented. The intense androgen concentration by the acinar cells was an unexpected finding and suggests a hitherto unknown androgen regulation of these cells. An incidental finding was intense concentration of [3H]-DHT in the nuclei of the endothelial cells of the post-capillary venules of the cervical lymph nodes.


2002 ◽  
Vol 283 (2) ◽  
pp. G473-G480 ◽  
Author(s):  
V. Gresz ◽  
T.-H. Kwon ◽  
H. Vorum ◽  
T. Zelles ◽  
I. Kurtz ◽  
...  

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.


2021 ◽  
Vol 14 (8) ◽  
pp. e244218
Author(s):  
Shiv Rajan ◽  
Ajay Kumar Singh ◽  
Sumaira Qayoom ◽  
Palavalasa Niranjan ◽  
Deep Chakrabarti

Polymorphous adenocarcinoma (PA) of the salivary glands is a rare malignancy that predominantly affects the minor salivary glands of the palate. Major salivary gland involvement is rare (<5%). The submandibular gland is a highly unusual location for this tumour. Recently, the WHO has updated the classification of salivary gland tumours in which the PA subtype has been modified. We report a very uncommon case of a classical variant of PA involving the submandibular gland in a 49-year-old woman managed at our institute and discuss the most recent pathological criteria for diagnosis, management strategy and prognosis of PA.


2003 ◽  
Vol 51 (3) ◽  
pp. 385-396 ◽  
Author(s):  
Phyllis A. Shaw ◽  
Xu Zhang ◽  
Andrew F. Russo ◽  
Brad A. Amendt ◽  
Scott Henderson ◽  
...  

Homeobox-containing (Hox) genes play important roles in development, particularly in the development of neurons and sensory organs, and in specification of body plan. The Hmx gene family is a new class of homeobox-containing genes defined by a conserved homeobox region and a characteristic pattern of expression in the central nervous system that is more rostral than that of the Hox genes. To date, three closely related members of the Hmx family, Hmx1, Hmx2, and Hmx3, have been described. All three Hmx genes are expressed in the craniofacial region of developing embryos. Here we show, for the first time, the expression of the transcription factor Hmx3 in postnatally developing salivary glands. Hmx3 protein is expressed in a cell type-specific manner in rat salivary glands. Hmx3 is present in both the nuclei and cytoplasm of specific groups of duct cells of the submandibular, parotid, and sublingual glands. Hmx3 expression increases during postnatal development of the submandibular gland. The duct cells show increasing concentrations of Hmx3 protein with progressive development of the submandibular gland. In contrast, the acinar cells of the three salivary glands do not exhibit detectable levels of Hmx3 protein.


1992 ◽  
Vol 21 (5) ◽  
pp. 214-220 ◽  
Author(s):  
J. Hashimoto ◽  
K. Yamada ◽  
K. Ogata ◽  
Y. Takai ◽  
M. Mori

1992 ◽  
Vol 282 (3) ◽  
pp. 891-897 ◽  
Author(s):  
O K Tollersrud ◽  
N N Aronson

Structural and physical properties of glycosylasparaginase (EC 3.5.1.26) from the livers of human, pig, cow, rat, mouse and chicken were compared. The enzyme in all species had a common basic structure of two N-glycosylated subunits of about 24 (alpha) and 20 (beta) kDa joined by non-covalent forces. Subunit-specific antisera against the rat glycosylasparaginase bound specifically and sensitively to the corresponding subunits from all species. Identity of 80% of the amino acids was found between the N-terminal sequences of corresponding pig and rat glycosylasparaginase alpha- and beta-subunits and the deduced sequence from a human glycosylasparaginase cDNA [Fisher, Tollersrud & Aronson (1990) FEBS Lett. 269, 440-444]. The beta-subunit from all three species has an N-terminal threonine reported to be involved in the reaction mechanism for the human enzyme [Kaartinen, Williams, Tomich, Yates, Hood & Mononen (1991) J. Biol. Chem. 266, 5860-5869]. The native enzyme appeared as a heterodimer among the mammals, whereas the chicken enzyme had a greater molecular mass and is probably either a tetramer or a heterodimer bound to an unrelated peptide(s). All glycosylasparaginases were thermostable, requiring temperatures between 65 degrees C and 80 degrees C to be irreversibly inactivated. In addition, they were unusually stable at high pH and remained active in the presence of SDS except at low pH. The pH maximum was between 5.5 and 6 except for the rat and mouse enzymes which had a broad maximum between pH 7 and 8. A number of other properties were observed which also distinguish the enzyme from individual and closely related species.


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