Potassium release by α2-adrenergic receptor stimulation of rat parotid acinar cells

1982 ◽  
Vol 31 (12) ◽  
pp. 2197-2199 ◽  
Author(s):  
Gerald D. Miller ◽  
James N. Davis
Keyword(s):  
Adrenergic Receptor ◽  
Acinar Cells ◽  
Receptor Stimulation ◽  
Potassium Release ◽  
Parotid Acinar Cells ◽  
Rat Parotid ◽  
Stimulation Of

scholarly journals β-Adrenergic stimulation alters oligosaccharide pyrophosphoryl dolichol metabolism in rat parotid acinar cells

1985 ◽  
Vol 231 (2) ◽  
pp. 431-438 ◽  
Author(s):  
S R Grant ◽  
E E Kousvelari ◽  
D K Banerjee ◽  
B J Baum
Keyword(s):  
Half Life ◽  
Specific Radioactivity ◽  
Acinar Cells ◽  
Protein Glycosylation ◽  
Significant Enhancement ◽  
Adrenergic Stimulation ◽  
Parotid Acinar Cells ◽  
Secretory Glycoproteins ◽  
Rat Parotid ◽  
Stimulation Of

beta-Adrenergic stimulation of rat parotid acinar cells markedly increases [3H]mannose incorporation into N-linked glycoproteins [Kousvelari, Grant, Banerjee, Newby & Baum (1984) Biochem. J. 222, 17-24]. More than 90% of this protein-bound [3H]mannose was preferentially incorporated into four secretory glycoproteins. The ratio of [3H]mannose/[14C]leucine present in these individual proteins was 1.7-4-fold greater with isoproterenol-treated cells than with untreated controls. In isoproterenol-stimulated cells, [3H]mannose incorporation into mannosylphosphoryl dolichol and oligosaccharide-PP-dolichol was increased 2-3-fold over that observed in unstimulated cells. Similarly, formation of mannosylated oligosaccharide-PP-dolichol was increased approx. 4-fold in microsomes prepared from isoproterenol-treated cells. Also, turnover of oligosaccharide-PP-dolichol was significantly increased (5-fold) by β-adrenergic stimulation; the half-life for oligosaccharide-PP-dolichol decreased from 6 min in control cells to 1.2 min in isoproterenol-stimulated cells. By 15 min after isoproterenol addition to acinar cells, the specific radioactivity of parotid oligosaccharide moieties increased about 3-fold over the value observed in the absence of the agonist. Taken together, these results strongly suggest that elevation of N-linked protein glycosylation in rat parotid acinar cells after β-adrenoreceptor stimulation resulted from significant enhancement in the synthesis of mannosylphosphoryl dolichol and oligosaccharide-PP-dolichol and the turnover of oligosaccharide-PP-dolichol.

scholarly journals Thiol-oxidation reduces the release of amylase induced by β-adrenergic receptor activation in rat parotid acinar cells

2010 ◽  
Vol 31 (5) ◽  
pp. 293-299 ◽  
Author(s):  
Ming-Yu Guo ◽  
Keitaro Satoh ◽  
Bing Qi ◽  
Takanori Narita ◽  
Osamu Katsumata-Kato ◽  
...  
Keyword(s):  
Adrenergic Receptor ◽  
Acinar Cells ◽  
Receptor Activation ◽  
Thiol Oxidation ◽  
Parotid Acinar Cells ◽  
Rat Parotid

scholarly journals Characterization of a phosphorylation event resulting in upregulation of the salivary Na+-K+-2Cl−cotransporter

1999 ◽  
Vol 277 (6) ◽  
pp. C1184-C1193 ◽  
Author(s):  
Kinji Kurihara ◽  
Marilyn L. Moore-Hoon ◽  
Masato Saitoh ◽  
R. James Turner
Keyword(s):  
Binding Sites ◽  
Acinar Cells ◽  
Close Correlation ◽  
Adrenergic Stimulation ◽  
High Affinity ◽  
Parotid Acinar Cells ◽  
Phosphorylation Event ◽  
Rat Parotid ◽  
Stimulation Of

Previous studies from our laboratory have shown a close correlation between increased Na+-K+-2Cl−cotransporter activity and increased cotransporter phosphorylation after β-adrenergic stimulation of rat parotid acinar cells. We demonstrate here that these effects are paralleled by an increase in the number of high-affinity binding sites for the cotransporter inhibitor bumetanide in membranes prepared from stimulated acini. We also show that the sensitivity of cotransporter fluxes to inhibition by bumetanide is the same in both resting and isoproterenol-stimulated cells, consistent with the hypothesis that β-adrenergic stimulation and the accompanying phosphorylation result in the activation of previously quiescent transporters rather than in a change in the properties of already active proteins. In addition, we demonstrate that the increased phosphorylation on the cotransporter resulting from β-adrenergic stimulation is localized to a 30-kDa phosphopeptide obtained by cyanogen bromide digestion. Immunoprecipitation and Western blotting experiments demonstrate that this peptide is derived from the NH2-terminal cytosolic tail of the cotransporter, which surprisingly does not contain the sole protein kinase A consensus site on the molecule.

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