Micropuncture and microperfusion study of glucose excretion in rat parotid saliva

Mangos, J. A.; Maragos, N; McSherry, NR

doi:10.1152/ajplegacy.1973.224.6.1260

Cited by 19 publications

(16 citation statements)

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“…This observation is in accord with the previous physiological data that the duct system is impermeable to water (Mangos and McSherry 1970;Mangos et al 1973), although other unknown AQP isoforms may be present in the ducts.…”

Section: Localization Of Aqp5supporting

confidence: 93%

Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation

Matsuzaki

Suzuki

Koyama

et al. 1999

Cell and Tissue Research

171

143

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Aquaporin-5 (AQP5) is a water channel protein and is considered to play an important role in water movement across the plasma membrane. We raised anti-AQP5 antibody and examined the localization of AQP5 protein in rat salivary and lacrimal glands by immunofluorescence microscopy. AQP5 was found in secretory acinar cells of submandibular, parotid, and sublingual glands, where it was restricted to apical membranes including intercellular secretory canaliculi. In the submandibular gland, abundant AQP5 was also found additionally at the apical membrane of intercalated duct cells. Upon stimulation by isoproterenol, apical staining for AQP5 in parotid acinar cells tended to appear as clusters of dots. These results suggest that AQP5 is one of the candidate molecules responsible for the water movement in the salivary glands.

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Section: Localization Of Aqp5supporting

confidence: 93%

Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation

Matsuzaki

Suzuki

Koyama

et al. 1999

Cell and Tissue Research

171

143

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“…To explain this supposed correlation, a study of the biochemical secretion of glucose by glandular cells is required. The glandular origin of salivary glucose was showed [5,6,8]. The variations of glucose concentration between diabetic and control patients supported this 326 hypothesis [2][3][4]7].…”

Section: Introductionmentioning

confidence: 73%

Glucose Transport by Acinar Cells in Rat Parotid Glands

Jurysta¹,

Nicaise

Cetik³

et al. 2012

Cell Physiol Biochem

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Background/Aims: Salivary glucose is often considered as being from glandular origin. Little information is available, however, on the possible role of glucose transporters in the secretion of the hexose by salivary glands. The major aim of the present study was to investigate the expression and localization of several distinct glucose transporters in acinar cells of rat parotid glands. Methods: Quantitative real-time PCR analysis, immunohistochemistry and western blotting techniques were used to assess the presence of SGLT1, GLUT1, GLUT2 and GLUT4 in acinar cells of rat parotid glands. Results: Quantitative real-time PCR documented the expression of SGLT1 and GLUT1 in parotid tissues, with a much lower level of GLUT4 mRNA and no expression of GLUT2 mRNA. Western blot analysis revealed the presence of SGLT1, GLUT1 and GLUT4 proteins, but not GLUT2 proteins in the parotid extract. Immunohistochemistry confirmed these findings. SGLT1 was specifically located at the baso-lateral membrane, co-localizing with Na⁺/K⁺ ATPase. GLUT1 was found both at the baso-lateral and apical level. GLUT4 appeared to be also located at the baso-lateral level. However, too little GLUT4 was present to allow co-localization labeling. Conclusion: Based on these findings, a model is proposed for the transport of glucose into the acinar cells and thereafter into the acinar lumen.

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“…al. , 1973;Takai et al, 1983). Burgen (1956), on the basis of flow-dependence studies with the dog parotid gland, suggested that there might exist two distinct but parallel transepithelial pathways for nonelectrolyte secretion, one permeable to molecules according to their lipid solubility and the other permeable to small polar molecules according to their molecular radius.…”

Section: Resultsmentioning

confidence: 99%

Transepithelial transport of nonelectrolytes in the rabbit mandibular salivary gland

et al. 1985

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The characteristics of nonelectrolyte secretion by the rabbit mandibular salivary gland have been investigated in an in vitro, perfused preparation. The concentrations of 14C-labeled nonelectrolytes were measured in saliva samples collected over a range of flow rates during the secretory response of the gland to continuous acetylcholine infusion. Of the nine nonelectrolytes studied, the two particularly lipid-soluble molecules, ethanol and antipyrine, appeared in the saliva at approximately the same concentration as in the perfusate, regardless of the secretory flow rate. The more polar molecules (urea, ethanediol, thiourea, glycerol, erythritol, mannitol and sucrose) appeared at saliva/perfusate concentration ratios (phi) which showed a strong dependence on flow. With the exception of thiourea, this could be attributed to the combined contributions of diffusion and solvent drag. For the polar nonelectrolytes, estimates have been obtained of both the permeability coefficients of the gland (P) and the solvent-drag filtration coefficients (1 - sigma). The relation between 1 - sigma and molecular radius suggests that small polar nonelectrolytes and the bulk of the secreted water cross the epithelium via aqueous channels that are approximately 0.8 nm in width. The location of the channels remains uncertain because tissue space measurements indicate that the nonelectrolytes most affected by solvent drag have access to both transcellular and paracellular pathways.

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Micropuncture and microperfusion study of glucose excretion in rat parotid saliva

Cited by 19 publications

References 0 publications

Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation

Aquaporin-5 (AQP5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation

Glucose Transport by Acinar Cells in Rat Parotid Glands

Transepithelial transport of nonelectrolytes in the rabbit mandibular salivary gland

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