Human Salivary Glands (human + salivary_gland)

Distribution by Scientific Domains


Selected Abstracts


Levels of pre-kallikrein in resting and stimulated human parotid and submandibular saliva

EUROPEAN JOURNAL OF ORAL SCIENCES, Issue 5 2001
Carol A. Francis
Salivary tissue kallikrein is stored in an active form in human salivary glands. Pre-kallikrein has been demonstrated in mixed saliva, but it is not clear if the various salivary glands contribute equally. This study set out to determine if pre-kallikrein is present in human parotid and submandibular salivas at rest, whether levels change during stimulation, and to compare the pattern of pre-kallikrein and kallikrein secretion with that of total protein. Resting and citric acid-stimulated parotid and submandibular, and gum-stimulated parotid saliva samples were collected from 6 healthy subjects. Salivary flows were determined gravimetrically. Total protein concentration and kallikrein enzymic activity were assayed using standard techniques. Pre-kallikrein was assayed following trypsinisation of duplicate samples. Pre-kallikrein was present in parotid and submandibular ductal saliva. Proportions of pre-kallikrein and active kallikrein were similar in salivas secreted at rest and during stimulation, and both outputs mirrored protein output in both major glands. Gum-stimulated parotid saliva showed lower activity than resting, and no differences were seen between resting and stimulated submandibular samples. [source]


Electron microscopic detection of statherin in secretory granules of human major salivary glands

JOURNAL OF ANATOMY, Issue 5 2008
M. Isola
Abstract In order to increase current knowledge regarding statherin secretion into the oral cavity, ultrastructural localization of this peptide was investigated in human salivary glands by using a post-embedding immunogold staining technique. Statherin reactivity was found inside the granules of serous cells of parotid and submandibular glands. In parotid granules immunostaining was preferentially present in the less electron-dense region, whereas in submandibular serous granules the reactivity was uniform and the dense core always stained. By contrast, none or weak reactivity was observed in serous cells of major sublingual glands. These findings reveal for the first time the subcellular localization of statherin by electron transmission microscopy and confirm that of the three major types of salivary glands, the parotid and submandibular glands are the greatest source of salivary statherin. Moreover, they suggest that more than one packaging mechanism may be involved in the storage of statherin within serous granules of salivary glands. [source]


Intralobular ducts of human major salivary glands contain leptin and its receptor

JOURNAL OF ANATOMY, Issue 5 2002
R. De Matteis
Abstract Leptin, a 16-kDa hormone, plays an important role in the control of food intake and in energy homeostasis both in rodents and in man. Leptin is mainly produced and secreted by adipocytes, but other tissues and gastric glands have also recently been shown to produce it in a dual (endocrine and exocrine) mode. In addition, a leptin receptor has been detected in taste cells of mouse circumvallate papillae and in rat intestinal epithelium. These data prompted us to carry out a detailed study of human salivary glands as potential leptin-producing organs. Biopsies of salivary glands (submandibular and parotid) obtained from male and female patients during surgery for different clinical indications were subjected to immunohistochemical study for the presence of leptin, its functional receptor, insulin and glucagon. The presence and cellular distribution of glucocorticoid receptor in leptin-secreting cells were also investigated. Double immunohistochemical staining (silver,gold intensification and avidin,biotin,peroxidase) was used for the visualization of glucocorticoid receptor and leptin labelling, respectively. The results show that intralobular duct cells of submandibular and parotid glands are immunoreactive for leptin, leptin receptor and glucagon but not for insulin. Leptin was also detected in some microglobules in whole saliva obtained from four healthy volunteers. Co-localization for leptin, leptin receptor and glucocorticoid receptor in the same cell type suggested a functional relationship between glucocorticoid hormone and leptin secretion also at the level of the salivary glands. [source]


Amylase and cyclic amp receptor protein expression in human diabetic parotid glands

JOURNAL OF ORAL PATHOLOGY & MEDICINE, Issue 9 2010
Monica Piras
J Oral Pathol Med (2010) 39: 715,721 Background:, Salivary dysfunction and oral disorders have been described in both type 1 and type 2 diabetes mellitus. However, the cellular and molecular consequences of diabetes on oral tissues remain to be ascertained. The purpose of this investigation was to study, by means of electron microscopy, the morphologic and molecular changes that occur in salivary glands during diabetes. Methods:, Biopsy samples of parotid glands were excised from non-diabetic and diabetic (type 1 and type 2) consenting patients and processed by standard methods for routine morphology and electron microscopic immunogold labeling. Specific antibodies were used to determine and quantify the expression of secretory proteins (alphaamylase and the regulatory subunit of type II protein kinase A). Results:, Morphologic changes in the diabetic samples included increased numbers of secretory granules, and alterations in internal granule structure. Quantitative analysis of immunogold labeling showed that labeling densities were variable among the parotid gland samples. In type 1 diabetes amylase expression was greater than in non-diabetic glands, whereas in type 2 diabetes it was not significantly changed. Expression of type II regulatory subunits was slightly, although not significantly, increased in acinar secretory granules of type 1 diabetic samples and was unchanged in type 2 diabetic samples. Conclusions:, Our data show that diabetes elicits specific changes in secretory protein expression in human salivary glands, thus contributing to the altered oral environment and oral disease associated with diabetes. [source]


MUC-1 mucin in normal human salivary glands detected by HMFG-1 and HMFG-2 monoclonal antibodies,

APMIS, Issue 2 2008
SANTA PONCE-BRAVO
The aim of this study was to determine the immunoexpression of normal salivary gland cells using two human milk fat globule membrane protein antibodies (HMFG-1 and HMFG-2). Paraffin-embedded, 5 ,m-thick slides from parotid and submandibular gland tissues were cut and immunostained with monoclonal antibodies HMFG-1 and HMFG-2 against MUC1 protein. HMFG antigens were found in secretory epithelial cells and ductal cells lining the striated and intercalated ducts in the intraductal secretion material, and sometimes in the myoepithelial cells. Our results suggest that HMFG-1 and HMFG-2 proteins may play a role in normal salivary gland function, mainly in the manufacturing and secretion of saliva. [source]