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This paper describes a dynamic response analysis of a laser marker which has an eddy current damping mechanism. In this calculation the equation of magnetic field is coupled with the equation of motion employing the 3-D finite element method (FEM), and time variations of the pendulum are computed to estimate the damping time. The usefulness of the computation is clarified through the comparison with the measured results. Moreover, the effectiveness of proposed damping structures is also confirmed by the comparison with the conventional one.

1. Histamine acted on H2 receptors in rat parotid tissues and induced the amylase secretion. Immunoblot analysis by using anti-H2 receptor protein antiserum demonstrated that histamine induced the increase and decrease in the amounts of H2 receptor proteins in basolateral and intracellular membranes, respectively. 2. Short-term treatment with histamine resulted in decreases in amylase secretion, the density of H2 receptors and their affinity for the agonists during further incubation with histamine, but showed an unaltered secretory response to isoproterenol, indicating that the histamine-induced desensitization was confined to H2 receptors. 3. This treatment triggered a 20% decrease in the histamine-stimulated adenylate cyclase activity and a 40% decrease in the phosphorylation level of Gi2alpha protein in the tissues, resulting in an increase in pertussis toxin (IAP)-catalyzed ADP-ribosylation of the protein. An enhancement of cholera toxin-catalyzed ADP-ribosylation of Gs protein was observed only during the first incubation with histamine. 4. This treatment triggered a 30% decrease and a 60% increase in the histamine-stimulated activities of protein kinase A and protein phosphatase 2A in the tissues, respectively. 5. Pretreatment with okadaic acid completely blocked the histamine-induced decrease in amylase secretion and increase in IAP-catalyzed ADP-ribosylation of Gi protein. The levels of Gi2alpha and Gs alpha proteins in the tissues were not modified by histamine treatment and the level of Gi2alpha protein was not affected by pretreatment with okadaic acid, as assessed by immunoblot analyses with anti-Gi2alpha and anti-Gs alpha protein antiserum. 6. The regulation of Gi2alpha protein phosphorylation in parotid tissues plays an important role in the histamine-induced desensitization of amylase secretion.

To evaluate the role of aquaporin5 (AQP5) in salivary secretion induced by cholinergic stimulation, the alteration of the distribution of AQP5 in rat parotid tissues induced by acetylcholine (ACh) was studied by immunobolt analysis. The treatment of the tissues with ACh within 1 min induced the translocation of AQP5 from intracellular membranes (ICM) to apical membranes (APM), but that for more than 5 min resulted in the converse translocation from APM to ICM. The ACh-induced increase in the amount of AQP5 in APM was inhibited by atropine, p-F-HHSiD and TMB-8, but not by methoctramine, staurosporine or H-7. The calcium ionophore A-23187 alone stimulated the translocation of AQP5 between APM and ICM. These results indicated that ACh acted on M3 muscarinic receptors and induced the translocation of AQP5 between ICM and APM, and that the cytosolic Ca2+ elevation by ACh may play a key role in this translocation in rat parotid glands.

The perfusion of rat small intestine with 10 microM epinephrine (Epi) or 10 microM norepinephrine resulted in significant increases in the amount of 3-O-[methyl-3H]-D-glucose transported from the mucosal to serosal side. The Epi-induced increases in glucose transport were coupled with selective increases in beta-adrenoceptor density in the mucosal membranes. Treatment with 0.1 microM okadaic acid increased glucose transport even in the absence of Epi, but that with 1 microM staurosporine or 60 microM N-[2-(methylamino)ethyl]-5-isoquinoline-sulfonamide dihydrochloride completely inhibited the increases in glucose transport induced by 10 microM Epi or 10 microM dibutyryl cAMP. The maximal binding sites (Bmax) of [3H]phlorizin in brush border membrane (BBM) from tissues perfused with Epi was increased, showing increases in the binding ability of the Na+/glucose cotransporter (SGLT1) to glucose. Phosphorylation and dephosphorylation of BBM with protein kinase A (PKA) and alkaline phosphatase resulted in increases and decreases in Bmax of [3H]phlorizin, respectively. The phosphorylation state of SGLT1 immunoprecipitated from BBM incubated with [gamma-32P]ATP-Mg2+ and PKA, and the analysis of phosphoamino acids composed of SGLT1 in rats given [32P]orthophosphate indicate the presence of potential sites for PKA-mediated phosphorylation of SGLT1 at serine. These findings indicate that the regulation of phosphorylation of SGLT1 leads to an alteration of its function and results in the control of glucose transport in the rat small intestine.

Treatment of rat parotid tissues with 1 microM isoproterenol (IPR) for 10 min caused a 60% decrease in pertussis toxin (IAP)-catalyzed ADP-ribosylation of Gi alpha and resulted in supersensitivity of amylase secretion from the tissues. However, conversely, IPR treatment for 30 min caused a 40% increase in IAP-catalyzed ADP-ribosylation of Gi alpha, coupled with desensitization of amylase secretion. No changes in Gs function were observed in IPR-induced phenomena. Pretreatment with okadaic acid induced enhancement of the supersensitivity of amylase secretion and disappearance of the desensitization. These phenomena were accompanied with decreases in IAP-catalyzed ADP-ribosylation of Gi alpha. IPR treatment for 30 min caused a 50% decrease in phosphorylation of Gi2 alpha immunoprecipitated with anti-G protein antiserum (AS/7) from [32P]Pi-labeled cells, but such treatment for 10 min caused a 40% increase in phosphorylation in the cells pretreated with okadaic acid. Phosphorylation and dephosphorylation of immunoprecipitates with AS/7 by protein kinase A (PKA) and alkaline phosphatase caused decreases and increases in IAP-catalyzed ADP-ribosylation, respectively, indicating the presence of PKA-mediated phosphorylation sites on Gi2 alpha. Thus, the control of the phosphorylation of Gi2 alpha is of importance and relevance in the regulation of biological processes and cellular responses.

Short-term treatment of rat submandibular tissues with 10 microM isoproterenol (IPR) resulted in reduction of mucin secretion in response to the agonist during further incubation, and in increases in EC50 values. This IPR-induced reduction of secretion was coupled with selective decreases in the number of beta-adrenoceptors in the tissues and in their affinity for agonists, as assessed by measurement of the specific binding of [3H]dihydroalprenolol. Treatment of the tissues with IPR caused a 30% decrease in IPR-stimulated adenylate cyclase activity and a 25% increase in the GTP binding capacity of inhibitory G proteins (Gi proteins). This IPR treatment triggered a 60% increase in the ability of pertussis toxin (IAP) to catalyze ADP-ribosylation of Gi proteins in the tissue membranes. Enhanced function of stimulatory G proteins (Gs proteins) was observed only during the first incubation of the tissues with IPR. The IAP-catalyzed ADP-ribosylation of Gi proteins in tissues treated with IPR was decreased by prior treatment with cyclic AMP dependent protein kinase, but was increased markedly by prior treatment with alkaline phosphatase. Neither IPR-induced desensitization of protein secretion nor increase in the IAP-catalyzed ADP-ribosylation of Gi proteins was observed in the tissues pretreated with 0.25 microM okadaic acid. These findings suggest that the regulation of Gi protein phosphorylation plays an important role in the IPR-induced heterologous desensitization of mucin secretion from rat submandibular glands.

The beta-adrenergic agonist, isoproterenol (IPR), stimulated more significantly and sensitively amylase secretion from both the tissues of 7- and 56-day-old rats than a cholinergic agonist, carbachol, at the same concentration. The EC50 value of amylase secretion with IPR decreased significantly during development but that with carbachol did not change. Estimation by measuring bindings of [3H]dihydroalprenolol and [3H]quinuclidynylbenzylate indicated the marked increases in the numbers of both beta-adrenoceptors and muscarinic receptors in the tissues during development. The affinity of beta-adrenoceptors for the agonist was also enhanced during development, but that of muscarinic receptors for the agonist was not. These developmental changes in the number and affinity of beta-adrenoceptors and muscarinic receptors paralleled those in amylase secretory response of the tissues to their agonists. The response of adenylate cyclase (AC) of the tissues to 1 microM IPR was steadily enhanced after birth. In contrast, the response of AC to 1 microM forskolin was high until 14 days old, but markedly decreased at 28 days old and thereafter maintained this level. The increase in cholera toxin-catalyzed ADP-ribosylation (AR) of stimulatory GTP binding proteins (Gs proteins) in the tissues was apparent at 14 days old, reaching a maximum at 56 days old and thereafter decreasing with age. On the other hand, pertussis toxin-catalyzed AR of inhibitory GTP binding proteins (Gi proteins) did not change after birth. Thus, the ratio of apparent levels of Gs to Gi proteins increased significantly after birth, reaching a maximum at 56 days old, but decreased rapidly till 84 days old and thereafter maintained this level. These changes in the ratio paralleled those in the response of AC to IPR. These results showed that the rapid and marked increases in the number and affinity of beta-adrenoceptors and the ratio of apparent levels of Gs to Gi proteins in rat parotid tissues during development had a key role in the enhancement of the secretory response of the tissues to beta-agonists.