Comparison of phosphodiesterase isozymes in rodent parotid glands

Imai, Akane; Nashida, Tomoko; Shimomura, Hiromi

doi:10.1016/s0305-0491(99)00131-5

Cited by 9 publications

(6 citation statements)

References 24 publications

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“…Various PDE isozymes have been reported to be present in the parotid glands of rodents (15). In this study, we demonstrated involvement of PDE4 in amylase release induced by β-adrenoceptor activation in acinar cells isolated from mouse, rat and rabbit parotid glands.…”

Section: Discussionsupporting

confidence: 54%

Involvement of phosphodiesterase 4 in β-adrenoceptor agonist-induced amylase release in parotid acinar cells

2009

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beta-Adrenoceptor activation increases intracellular cAMP levels and consequently induces exocytotic amylase release in parotid acinar cells. Phosphodiesterase (PDE) catalyses the hydrolysis of cAMP, which terminates the downstream signaling of this second messenger. We investigated the involvement of PDE4, a cAMP-PDE, in beta-adrenoceptor agonist-induced amylase release in mouse, rat and rabbit parotid acinar cells by using the specific PDE4 inhibitor rolipram. cAMP-PDE activity was detected in mouse, rat and rabbit parotid acinar cells. In the presence of rolipram, cAMP-PDE activity was reduced by about 31%, 38% and 33% in mouse, rat and rabbit parotid acinar cells, respectively. The increase in cAMP levels induced by the beta-adrenoceptor agonist isoproterenol was enhanced in the presence of rolipram in mouse, rat and rabbit parotid acinar cells. Isoproterenol-induced amylase release, but not constitutive amylase release, was also enhanced in the presence of rolipram in mouse, rat and rabbit parotid acinar cells. These results suggest that the rolipram-sensitive cAMP-PDE, PDE4, is involved in beta-adrenoceptor agonist-induced amylase release in parotid acinar cells.

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Section: Discussionsupporting

confidence: 54%

Involvement of phosphodiesterase 4 in β-adrenoceptor agonist-induced amylase release in parotid acinar cells

2009

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“…There are multiple studies showing that PDE4 distribution in some tissues differs between rodent and non-rodent species (Kajimoto et al, 1997;Imai et al, 1999;Perez-Torres et al, 2000). A recent study has found that levels of PDE4 enzyme activity are much higher in rats than humans in multiple tissues, making rats more susceptible to PDE4-inhibitor toxicities than other species (Bian et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the Inflammatory Response to a Highly Selective PDE4 Inhibitor in the Rat and the Identification of Biomarkers that Correlate with Toxicity

et al. 2006

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The primary toxicity associated with repeated oral administration of the PDE4 inhibitor IC542 to the rat is an inflammatory response leading to tissue damage primarily in the gastrointestinal tract and mesentery. Although necrotizing vasculitis is frequently seen with other PDE4 inhibitors, blood vessel injury was rare following IC542 administration and was always associated with inflammation in the surrounding tissue. The incidence and severity of the histologic changes in these studies correlated with elevated peripheral blood leukocytes, serum IL-6, haptoglobin, and fibrinogen, and with decreased serum albumin. By monitoring haptoglobin, fibrinogen and serum albumin changes in IC542-treated rats, it was possible to identify rats with early histologic changes that were reversible. Since PDE4 inhibition is generally associated with anti-inflammatory activity, extensive inflammation in multiple tissues was unexpected with IC542. Co-administration of dexamethasone completely blocked IC542-induced clinical and histologic changes in the rat, confirming the toxicity resulted from inflammatory response. In addition, IC542 augmented release of the proinflammatory cytokine IL-6 in LPS-activated whole blood from rats but not monkeys or humans. The effect of IC542 on IL-6 release from rat leukocytes in vitro is consistent with the proinflammatory response observed in vivo and demonstrates species differences to PDE4 inhibition.

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“…However, it is not clear as to the specific cell expression and role of PDEs in salivary gland. PDE isozymes were isolated from the supernatant fraction of rodent parotid glands by Q-Sepharose Fast Flow column chromatography and/or Mono Q ion-exchange chromatography: in rat and mouse parotid glands, PDE1, PDE2, PDE3 and PDE4; in hamster, PDE1, PDE2 and PDE4; and in guinea pig, PDE1, PDE2 and PDE3 [61][62][63]. In submandibular glands from young rat, PDE1, PDE2, PDE3, PDE4 and PDE5 activities were present; in the adult rat gland, PDE1, PDE3, PDE4 and PDE5 activities [64].…”

Section: Salivary Glandmentioning

confidence: 99%

Phosphodiesterase 3 (PDE3): Structure, Localization and Function

Murata¹,

Shimizu²,

Hiramoto³

et al. 2009

CHAMC

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Cyclic adenosine 3'5'-monophosphate (cAMP) and cyclic guanosine 3'5'-monophosphate (cGMP) are critical intracellular messengers involved in transduction of signals generated by a wide variety of extracellular stimuli, including growth factors, cytokines, peptide hormones, light and neurotransmitters. These messengers modulate many fundamental biological processes, including myocardial contractility, platelet aggregation, vascular smooth muscle relaxation, proliferation and apoptosis, etc. Cyclic nucleotide phosphodiesterases (PDEs) catalyze the hydrolysis of cAMP and cGMP, and are important in regulating intracellular concentrations and biological actions of these signal-transducing molecules. These enzymes contain at least 11 highly regulated and structurally related gene families (PDE1-11). In this review, we will discuss some general information of PDEs and then focus on PDE3 gene family, including the molecular biology, structure, function and potential as therapeutic targets. Furthermore, we show the possibilities of PDE3 as therapeutic targets in malignant tumor cells and salivary gland.

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Comparison of phosphodiesterase isozymes in rodent parotid glands

Cited by 9 publications

References 24 publications

Involvement of phosphodiesterase 4 in β-adrenoceptor agonist-induced amylase release in parotid acinar cells

Involvement of phosphodiesterase 4 in β-adrenoceptor agonist-induced amylase release in parotid acinar cells

Characterization of the Inflammatory Response to a Highly Selective PDE4 Inhibitor in the Rat and the Identification of Biomarkers that Correlate with Toxicity

Phosphodiesterase 3 (PDE3): Structure, Localization and Function

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