vasoactive-intestinal-peptide has been researched along with Parotid-Neoplasms* in 4 studies
4 other study(ies) available for vasoactive-intestinal-peptide and Parotid-Neoplasms
Article | Year |
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Immunocytochemical correlation of peptides and tyrosine hydroxylase in nerve fibres of the human parotid gland.
The peptidergic innervation of parenchymal and vascular components in the human parotid gland was investigated by double-labelling fluorescence. Peptide immunoreactivity in nerve fibres was correlated with the presence of tyrosine hydroxylase (TH). By light microscopy, acinar innervation consisted of fibres with the combinations neuropeptide Y (NPY)/TH and NPY/vasoactive intestinal polypeptide (VIP). Some fibres were solely NPY, TH or VIP immunoreactive. Rarely, substance P (SP)/calcitonin gene-related (CGRP)-immunolabelled fibres were associated with acini. Intercalated ducts were often approached by NPY/TH- and VIP-containing fibres. VIP innervation of excretory ducts was sparse. Intralobular and intralobar excretory ducts, in addition to NPY and TH, revealed CGRP and CGRP/SP innervation, whereas nerve fibres on interlobar excretory ducts very rarely contained NPY and none of the other mediators. Vascular innervation consisted of NPY/TH and SP/CGRP fibres; in a few fibres SP was colocalized with leu-enkephalin. Large arteries were encircled by some VIP-positive fibres. The findings suggest a specific participation of neuropeptides and of peptide combinations in the regulation of parotid exocrine function. Topics: Adenolymphoma; Adult; Arteries; Calcitonin Gene-Related Peptide; Enkephalin, Leucine; Female; Humans; Immunohistochemistry; Male; Middle Aged; Nerve Fibers; Neuropeptide Y; Neuropeptides; Parotid Gland; Parotid Neoplasms; Substance P; Tyrosine 3-Monooxygenase; Vasoactive Intestinal Peptide | 1994 |
Induction of cells with phenotypic features of neuronal cells by treatment with dibutyryl cyclic adenosine 3',5'-monophosphate in a human parotid gland adenocarcinoma cell line in culture.
A human parotid gland adenocarcinoma cell line, with an intercalated duct cell phenotype of the salivary gland and expression of vasoactive intestinal polypeptide and amylase, was cultivated in the presence of dibutyryl cyclic adenosine 3',5'-monophosphate (dB-cAMP). Morphological changes occurred; cells formed long cytoplasmic processes densely packed with ample microfibrils, as well as microtubules, and grew in a netlike appearance. In addition, it has been found by the immunofluorescence staining technique, immunoblotting, or immunoelectron microscopy that the cells treated with dB-cAMP express neurofilaments, neuron-specific enolase, synaptophysin, and HNK-1 antigen, as well as the alpha- and beta-chains of tubulin, whereas these antigens are not detected in untreated cells. The expression of vasoactive intestinal polypeptide detected diffusely in the cytoplasm of untreated cells was restricted to the cell membranes during the cultivation of cells in the presence of dB-cAMP, while expression of amylase persisted in the treated cells in a fashion similar to that in untreated cells. Moreover, both anchorage-independent and anchorage-dependent growth of the cells was markedly suppressed in the presence of dB-cAMP. After removal of dB-cAMP from the culture, the treated cells returned rapidly to the phenotype and growth rate of the untreated cells. These findings indicate that reversible conversion into cells with phenotypic features of neuronal cells of a human parotid adenocarcinoma cell line occurs in growth medium containing dB-cAMP. Topics: Adenocarcinoma; Amylases; Bucladesine; Cytoskeleton; Fluorescent Antibody Technique; Humans; Intermediate Filaments; Parotid Neoplasms; Phenotype; Time Factors; Tumor Cells, Cultured; Tumor Stem Cell Assay; Vasoactive Intestinal Peptide | 1990 |
Expression of vasoactive intestinal polypeptide and amylase in a human parotid gland adenocarcinoma cell line in culture.
A neoplastic epithelial cell line initially established in culture from a human parotid gland adenocarcinoma grown in athymic nude mice with a BALB/c genetic background, which has an ultrastructure similar to that of the intercalated duct cell of the salivary glands, was examined for the expression of amylase and vasoactive intestinal polypeptide (VIP). The cultured cells were found by the peroxidase-antiperoxidase (PAP) method to express amylase and ultrastructurally to have secretory granules showing positive immunoreaction with anti-amylase serum. In addition, the cells were found to secrete amylase into the culture medium. The expression of VIP in the cultured cells was observed by the PAP method, immunofluorescent staining method, or immunoelectron microscopy. Moreover, the presence of the polypeptide reactive to antibodies directed against VIP in the cultured cells was confirmed by immunoblotting and radioimmunoassay. These findings indicate that the cells proliferating in culture express both amylase and VIP. Topics: Adenocarcinoma; Amylases; Animals; Female; Humans; Mice; Mice, Inbred BALB C; Molecular Weight; Parotid Neoplasms; Tumor Cells, Cultured; Vasoactive Intestinal Peptide | 1987 |
Immunoreactive vasoactive intestinal polypeptide in acinic cell carcinoma of the parotid gland.
Vasoactive intestinal polypeptide (VIP) in the neoplastic cells of acinic cell carcinomas arising in the human parotid gland was found immunohistochemically, whereas other parotid gland tumors, such as pleomorphic adenoma, Warthin's tumor, oxyphilic adenoma, mucoepidermoid carcinoma, adenocarcinoma, and adenoid cystic carcinoma, did not show positive immunoreactivity for VIP. The acinic cell carcinoma stained with Grimelius impregnation and had dense core granules immunoreactive with anti-VIP serum. Moreover, a comparatively high concentration of immunoreactive VIP was detected by radioimmunoassay in an acinic cell carcinoma, whereas VIP concentration of the other tumors was undetectable. Topics: Carcinoma; Chromatography, Gel; Histocytochemistry; Humans; Immunoenzyme Techniques; Microscopy, Electron; Parotid Neoplasms; Radioimmunoassay; Vasoactive Intestinal Peptide | 1987 |