Immunolocalization of E-cadherin and αE-catenin in rat parotid acinar cell under chronic stimulation of isoproterenol

2007 ◽  
Vol 52 (2) ◽  
pp. 161-167 ◽  
Author(s):  
Fabio D’Amico ◽  
Evangelia Skarmoutsou
Keyword(s):  
Acinar Cell ◽  
Chronic Stimulation ◽  
Parotid Acinar Cell ◽  
Rat Parotid ◽  
Stimulation Of ◽  
E Cadherin

scholarly journals Interaction between zymogen granule and membrane of rat parotid acinar cell, in vitro.

1993 ◽  
Vol 61 ◽  
pp. 57
Author(s):  
Takahiro Nagao ◽  
Ritsuko Fujimoto ◽  
Hideaki Nishio ◽  
Fumiaki Hata
Keyword(s):  
Acinar Cell ◽  
Zymogen Granule ◽  
Parotid Acinar Cell ◽  
Rat Parotid

Mobilization of Intracellular Calcium by Methacholine and Inositol 1,4,5-Trisphosphate in Rat Parotid Acinar Cells

1987 ◽  
Vol 66 (2) ◽  
pp. 547-551 ◽  
Author(s):  
D.L. Aub ◽  
J.W. Putney
Keyword(s):  
Receptor Activation ◽  
Transient Phase ◽  
Cell Preparation ◽  
Similar Concentration ◽  
Parotid Acinar Cells ◽  
Parotid Acinar Cell ◽  
Inositol 1,4,5 Trisphosphate ◽  
Intracellular Ca ◽  
Rat Parotid ◽  
Stimulation Of

In the rat parotid acinar cell, methacholine caused an increase in [Ca2+]i as determined by quin-2 fluorescence. The increase in [Ca2+] i was initially independent of, and subsequently dependent on, the presence of extracellular Ca2+, indicating mobilization of intracellular Ca2+, as well as activation of Ca2+ entry. Methacholine mobilization of the internal Ca2+ pool and stimulation of the initial transient phase of K+ efflux have similar concentration dependencies; the EC50 value for Ca2+ mobilization is 80 nmollL, the EC50 value for K+ efflux is 200 nmol/L. In a permeable parotid cell preparation, inositol 1,4,5-trisphosphate, inositol 2,4,5-trisphosphate, and inositol 4,5-bisphosphate were able to release Ca2+ from an ATP-dependent, oligomycininsensitive pool. These observations, when taken with the previous finding that methacholine stimulates Ca-independent inositol trisphosphate formation, support the view that inositol 1,4,5-trisphosphate acts as a second messenger mediating the release of an intracellular Ca 2+ pool following muscarinic receptor activation in the parotid gland.

Morphological Effects of WR-2721 on the Rat Parotid Acinar Cell

1978 ◽  
Vol 75 (2) ◽  
pp. 327 ◽  
Author(s):  
N. E. Pratt ◽  
M. Sodicoff
Keyword(s):  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid

scholarly journals Effects of muscarinic, alpha-adrenergic, and substance P agonists and ionomycin on ion transport mechanisms in the rat parotid acinar cell. The dependence of ion transport on intracellular calcium.

1989 ◽  
Vol 93 (2) ◽  
pp. 285-319 ◽  
Author(s):  
S P Soltoff ◽  
M K McMillian ◽  
L C Cantley ◽  
E J Cragoe ◽  
B R Talamo
Keyword(s):  
Substance P ◽  
Ion Transport ◽  
Acinar Cell ◽  
Fluid Secretion ◽  
Ion Fluxes ◽  
Transport Systems ◽  
K Channel ◽  
Muscarinic Agonist ◽  
Parotid Acinar Cell ◽  
Rat Parotid

The relationship between receptor-mediated increases in the intracellular free calcium concentration [( Ca]i) and the stimulation of ion fluxes involved in fluid secretion was examined in the rat parotid acinar cell. Agonist-induced increases in [Ca]i caused the rapid net loss of up to 50-60% of the total content of intracellular chloride (Cli) and potassium (Ki), which is consistent with the activation of calcium-sensitive chloride and potassium channels. These ion movements were accompanied by a 25% reduction in the intracellular volume. The relative magnitudes of the losses of Ki and the net potassium fluxes promoted by carbachol (a muscarinic agonist), phenylephrine (an alpha-adrenergic agonist), and substance P were very similar to their characteristic effects on elevating [Ca]i. Carbachol stimulated the loss of Ki through multiple efflux pathways, including the large-conductance Ca-activated K channel. Carbachol and substance P increased the levels of intracellular sodium (Nai) to more than 2.5 times the normal level by stimulating the net uptake of sodium through multiple pathways; Na-K-2Cl cotransport accounted for greater than 50% of the influx, and approximately 20% was via Na-H exchange, which led to a net alkalinization of the cells. Ionomycin stimulated similar fluxes through these two pathways, but also promoted sodium influx through an additional pathway which was nearly equivalent in magnitude to the combined uptake through the other two pathways. The carbachol-induced increase in Nai and decrease in Ki stimulated the activity of the sodium pump, measured by the ouabain-sensitive rate of oxygen consumption, to nearly maximal levels. In the absence of extracellular calcium or in cells loaded with the calcium chelator BAPTA (bis[o-aminophenoxy]ethane-N,N,N',N'-tetraacetic acid) the magnitudes of agonist- or ionomycin-stimulated ion fluxes were greatly reduced. The parotid cells displayed a marked desensitization to substance P; within 10 min the elevation of [Ca]i and alterations in Ki, Nai, and cell volume spontaneously returned to near baseline levels. In addition to quantitating the activation of various ion flux pathways in the rat parotid acinar cell, these results demonstrate that the activation of ion transport systems responsible for fluid secretion in this tissue is closely linked to the elevation of [Ca]i.

Endotoxin can decrease isolated rat parotid acinar cell amylase secretion in a nitric oxide-independent manner

2005 ◽  
Vol 524 (1-3) ◽  
pp. 169-173 ◽  
Author(s):  
Adrienn Barta ◽  
Ildikó Tarján ◽  
Ágnes Kittel ◽  
Krisztina Horváth ◽  
Anikó Pósa ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Acinar Cell ◽  
Amylase Secretion ◽  
Independent Manner ◽  
Parotid Acinar Cell ◽  
Rat Parotid ◽  
Isolated Rat

Alpha-lactalbumin acts as a bimodal regulator of rat parotid acinar cell growth

1987 ◽  
Vol 147 (1) ◽  
pp. 174-181 ◽  
Author(s):  
Michael G. Humphreys-Beher ◽  
Charlotte A. Schneyer ◽  
Tivadar Zelles
Keyword(s):  
Cell Growth ◽  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid ◽  
Alpha Lactalbumin

scholarly journals Secretion of old versus new exportable protein in rat parotid slics. Control by neurotransmitters.

1976 ◽  
Vol 71 (1) ◽  
pp. 107-122 ◽  
Author(s):  
Y Sharoni ◽  
S Eimerl ◽  
M Schramm
Keyword(s):  
Acinar Cell ◽  
Adrenergic Receptor ◽  
Secretory Granules ◽  
Beta Adrenergic Receptor ◽  
Beta Adrenergic ◽  
Amylase Release ◽  
Chase Period ◽  
Parotid Acinar Cell ◽  
Rat Parotid

The possibility that old and new secretory granules do not mix and that older exportable protein can be secreted preferentially was tested on parotid gland in vitro. Slices from fasted animals were pulse labeled for 3 min with L-[3H]leucine. Subcellular fractionstion showed that after 1 90-min chase period, the formation of new labeled secretory granules was mostly completed. The ratio of label in secretory granules to label in microsomes increased 250-fold during the period 5--90 min postpulse. After the 90-min chase, a submaximal rate of secretion was initiated by adding a low concentration of isoproterenol to the slices. Preferential secretion of old unlabeled exportable protein was evident from the finding that the percent of total amylase secreted was 3.5-fold greater than the percent of labeled protein secreted. Preferential secretion of old unlabeled exportable amylase was undiminished even when the chase period before addition of isoproterenol was extended to 240 min. Such long chase incubations were still meaningful due to the fact that the spontaneous rat of amylase release and radioactive protein release from the slices was negligibly low. A high isoproterenol concentration added to the slices after a 90-min chase produced the following results. An initial phase of preferential secretion of old unlabeled protein was soon replaced by secretion of a random mixture of new and old exportable protein. Electron micrographs indicated that high rates of secretion involved sequential fusion of secretory granules so that the lumen extended deep into the cell where the new labeled granules were presumably located. At low rates of secretion, the lumen showed no such deep extensions. Experiments were also conducted on slices from glands which had been largely depleted of old granules by prior injection of isoproterenol into the animals. Secretion of labeled protein from such slices stopped with the export of 80% of the labeled protein. This finding indicates that about 20% of the radioactive protein is cellular nonexportable protein and that the slices are capable of exporting the entire amount of secretory protein which was symthesized in vitrol. In addition to the beta-adrenergic receptor which mediates protein secretion, the parotid acinar cell also possesses an alpha-adrenergic and a cholinergic receptor both of which cause K+ release, vacuole formation, and water secretion. Activation of either of the latter two receptors in conjunction with the beta-adrenergic receptor increased randomization of the protein secreted. It is concluded that in the rat parotid acinar cell there is little spontaneous mixing between old granules near the luminal cell membrane and new granules coming up behind from the Golgi complex. The neurotransmitters which induce secretion produce the observed randomization.

Development and characterization of SV40 immortalized rat parotid acinar cell lines

1998 ◽  
Vol 34 (1) ◽  
pp. 58-67 ◽  
Author(s):  
D. O. Quissell ◽  
K. A. Barzen ◽  
R. S. Redman ◽  
J. M. Camden ◽  
J. T. Turner
Keyword(s):  
Cell Lines ◽  
Acinar Cell ◽  
Parotid Acinar Cell ◽  
Rat Parotid
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