Beta-Adrenergic Agonists for Acute, Severe Asthma

1992 ◽  
Vol 26 (1) ◽  
pp. 81-91 ◽  
Author(s):  
H. William Kelly ◽  
Shirley Murphy
Keyword(s):  
Severe Asthma ◽  
Acute Asthma ◽  
The Body ◽  
Beta Agonist ◽  
Acute Severe Asthma ◽  
Adrenergic Agonists ◽  
Aerosol Delivery ◽  
Beta Adrenergic ◽  
Beta Agonists ◽  
Beta Adrenergic Agonists

OBJECTIVE: To critically review the use of beta-adrenergic agonists in acute, severe asthma with particular focus on aerosol administration. DATA SOURCES: English language articles published since 1971 on the use of beta-agonists for acute asthma. Studies were identified from bibliographies of book chapters, review articles, and other research articles. STUDY SELECTION: All studies (21 total) comparing systemic with inhaled beta-agonists were reviewed, regardless of their design or outcome. Selected studies highlighting specific aspects of beta-agonist use in acute asthma such as beta-agonists versus other bronchodilators, aerosol delivery, and intravenous beta-agonists were also reviewed. DATA EXTRACTION: Performed subjectively by the authors with specific aspects of quality discussed within the body of the article. DATA SYNTHESIS: The beta-agonists provide superior bronchodilation in acute severe asthma compared with either the methylxanthines and/or anticholinergics. The majority of studies found aerosolized beta-agonists to be either as effective as or more effective than parenteral beta-agonists and to produce fewer adverse cardiovascular effects. Studies showing preference for parenteral therapy have either been of poor design or used low doses of an aerosolized beta-agonist. Based on studies of aerosol delivery, there is no advantage of jet nebulization over metered-dose inhalers; however, other aspects, including ease of administration, favor nebulization as the delivery method of choice. The articles recommending intravenous beta-agonists consist of a series of uncontrolled cases. CONCLUSIONS: Aerosolized selective beta2-agonists are the bronchodilator treatments of choice for acute, severe asthma. Attention to the details of dosing and delivery are required for optimal results. The final dose and dosing interval are determined by the patient's response. Intravenous beta-agonists are hazardous and cannot be recommended.

Combined Methylxanthines and Beta-Adrenergic Agonists in the Treatment of Severe Asthma

1983 ◽  
Vol 17 (11) ◽  
pp. 820-821
Author(s):  
Ferrari Morell ◽  
Ramon Orriols ◽  
J. de Gracia ◽  
Joan-Ramon Laporte
Keyword(s):  
Severe Asthma ◽  
Adrenergic Agonists ◽  
Beta Adrenergic ◽  
Beta Adrenergic Agonists

scholarly journals Demonstration of beta-adrenergic receptors in rat bronchiolar epithelial cells employing 9-amino-acridyl propranolol fluorescent microscopy.

1984 ◽  
Vol 32 (1) ◽  
pp. 122-123 ◽  
Author(s):  
G D Massaro ◽  
L D Davis
Keyword(s):  
Adrenergic Receptors ◽  
Fluorescent Microscopy ◽  
Clara Cell ◽  
Clara Cells ◽  
Adrenergic Agonists ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Beta Agonists ◽  
Beta Adrenergic Agonists ◽  
Anatomical Localization

Prior work has provided ultrastructural evidence that beta-adrenergic agonists stimulate secretion by nonciliated bronchiolar epithelial (Clara) cells of the rat (J Clin Invest 67:345, 1981). However, since the lung is a multicellular organ it is not clear if the beta-agonists act directly on the Clara cell. The absence in Clara cells of beta-adrenergic receptors would indicate an indirect action of the beta-adrenergic agonists. In the present study, we used 9-amino-acridyl propranolol in an attempt to determine if beta-adrenergic receptors are present in rat bronchiolar Clara cells. Discrete, intense yellow fluorescent dots were identified microscopically in ciliated and in Clara cells of the rat. This anatomical localization of beta-adrenergic receptors supports the notion that beta-adrenergic agonists stimulate secretion by acting directly on Clara cells.

scholarly journals The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src.

1993 ◽  
Vol 13 (4) ◽  
pp. 2391-2400 ◽  
Author(s):  
J S Moyers ◽  
A H Bouton ◽  
S J Parsons
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Beta Agonist ◽  
Adrenergic Agonists ◽  
Beta Adrenergic ◽  
Beta Adrenergic Agonists ◽  
Kinase C ◽  
Gs Alpha ◽  
In Cells

Previously we demonstrated that C3H10T1/2 murine fibroblasts overexpressing avian c-src exhibit elevated levels of cyclic AMP (cAMP) in response to beta-adrenergic agonists compared with that in control cells and that this enhanced response requires c-src kinase activity (W. A. Bushman, L. K. Wilson, D. K. Luttrell, J. S. Moyers, and S. J. Parsons, Proc. Natl. Acad. Sci. USA 87:7462-7466, 1990). However, it is not yet known which components of the beta-adrenergic receptor pathway, if any, interact with pp60c-src. It has recently been shown that immune complexes of pp60c-src phosphorylate recombinant G alpha proteins in vitro to stoichiometric levels, resulting in alterations of GTP binding and GTPase activity (W. P. Hausdorff, J. A. Pitcher, D. K. Luttrell, M. E. Linder, H. Kurose, S. J. Parsons, M. G. Caron, and R. J. Lefkowitz, Proc. Natl. Acad. Sci. USA 89:5720-5724, 1992), raising the possibility that the Gs alpha protein may be an in vivo target for the interaction with pp60c-src. To further characterize the involvement of pp60c-src in the beta-adrenergic signalling pathway, we have overexpressed, in 10T1/2 cells, pp60c-src containing mutations in several domains which are believed to be important for signalling processes. In this study we show that the sites of phosphorylation by protein kinase C (PKC) (Ser-12 and Ser-48) as well as the SH2 region of pp60c-src are required for the enhanced response of c-src overexpressors to beta-agonist stimulation. Mutation at the site of myristylation (Gly-2) results in a decrease in the enhanced response, while mutation at the site of phosphorylation by cAMP-dependent protein kinase (Ser-17) has no effect. Two-dimensional phosphotryptic analyses indicate that phosphorylation on Ser-12 and Ser-48 in unstimulated cells is associated with the ability of overexpressed pp60c-src to potentiate beta-adrenergic signalling. Cells overexpressing wild-type c-src also exhibit enhanced cAMP accumulation upon treatment with cholera toxin, an effect that is abated in cells overexpressing pp60c-src defective in the kinase or SH2 domains or altered at the sites of phosphorylation by PKC. These studies provide the first evidence for the physiological significance of the pp60c-src sites of PKC phosphorylation. In addition, they show that the SH2, Ser-12/48, and myristylation regions may be important for efficient interaction of pp60c-src with components of the beta-adrenergic pathway. Our data also support the possibility that the Gs alpha protein may be an in vivo target for alteration by pp60c-src.

Regulation of secretion in cultured tracheal serous cells by protein kinases A and C

1991 ◽  
Vol 261 (2) ◽  
pp. L172-L177 ◽  
Author(s):  
A. Paul ◽  
M. Mergey ◽  
D. Veissiere ◽  
B. Hermelin ◽  
G. Cherqui ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Beta Agonist ◽  
Dependent Manner ◽  
Adrenergic Agonists ◽  
Cellular Mechanisms ◽  
Concentration Dependent Manner ◽  
Beta Adrenergic ◽  
Camp Content ◽  
Beta Adrenergic Agonists ◽  
Kinase C

We recently reported that cultured gland serous cells release chondroitin sulfate proteoglycans (CSPGs) in response to beta-adrenergic agonists. In this study, we analyzed this regulatory pathway and other cellular mechanisms responsible for CSPG secretion. We show the following. 1) Isoproterenol increased CSPG secretion in a concentration-dependent manner, with maximal stimulation (50%) obtained at 10(-5) M; at this concentration, the beta-agonist also stimulated protein kinase A (PKA) by 50%, whereas it increased cellular adenosine 3',5'-cyclic monophosphate (cAMP) content by 300%. 2) Phenylephrine (10(-5) M), 4 beta-phorbol 12 beta-myristate 13 alpha-acetate (1.6 x 10(-7) M), and A23187 (10(-6) M) also stimulated CSPG secretion; this stimulation was concomitant with protein kinase C (PKC) translocation from cytosol to membrane, was blocked by sphingosine (2 x 10(-5) M), and was additive with that elicited by isoproterenol. 3) All PKC activators potentiated the isoproterenol-induced increased in cAMP accumulation without modifying the activation of PKA elicited by the beta-agonist. Our results indicate that although the signaling pathways triggered by alpha- and beta-adrenergic agonists converge at the level of adenylate cyclase in tracheal serous cells, PKA and PKC independently regulate CSPG secretion.

The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src

1993 ◽  
Vol 13 (4) ◽  
pp. 2391-2400
Author(s):  
J S Moyers ◽  
A H Bouton ◽  
S J Parsons
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Beta Agonist ◽  
Adrenergic Agonists ◽  
Beta Adrenergic ◽  
Beta Adrenergic Agonists ◽  
Kinase C ◽  
Gs Alpha ◽  
In Cells

Previously we demonstrated that C3H10T1/2 murine fibroblasts overexpressing avian c-src exhibit elevated levels of cyclic AMP (cAMP) in response to beta-adrenergic agonists compared with that in control cells and that this enhanced response requires c-src kinase activity (W. A. Bushman, L. K. Wilson, D. K. Luttrell, J. S. Moyers, and S. J. Parsons, Proc. Natl. Acad. Sci. USA 87:7462-7466, 1990). However, it is not yet known which components of the beta-adrenergic receptor pathway, if any, interact with pp60c-src. It has recently been shown that immune complexes of pp60c-src phosphorylate recombinant G alpha proteins in vitro to stoichiometric levels, resulting in alterations of GTP binding and GTPase activity (W. P. Hausdorff, J. A. Pitcher, D. K. Luttrell, M. E. Linder, H. Kurose, S. J. Parsons, M. G. Caron, and R. J. Lefkowitz, Proc. Natl. Acad. Sci. USA 89:5720-5724, 1992), raising the possibility that the Gs alpha protein may be an in vivo target for the interaction with pp60c-src. To further characterize the involvement of pp60c-src in the beta-adrenergic signalling pathway, we have overexpressed, in 10T1/2 cells, pp60c-src containing mutations in several domains which are believed to be important for signalling processes. In this study we show that the sites of phosphorylation by protein kinase C (PKC) (Ser-12 and Ser-48) as well as the SH2 region of pp60c-src are required for the enhanced response of c-src overexpressors to beta-agonist stimulation. Mutation at the site of myristylation (Gly-2) results in a decrease in the enhanced response, while mutation at the site of phosphorylation by cAMP-dependent protein kinase (Ser-17) has no effect. Two-dimensional phosphotryptic analyses indicate that phosphorylation on Ser-12 and Ser-48 in unstimulated cells is associated with the ability of overexpressed pp60c-src to potentiate beta-adrenergic signalling. Cells overexpressing wild-type c-src also exhibit enhanced cAMP accumulation upon treatment with cholera toxin, an effect that is abated in cells overexpressing pp60c-src defective in the kinase or SH2 domains or altered at the sites of phosphorylation by PKC. These studies provide the first evidence for the physiological significance of the pp60c-src sites of PKC phosphorylation. In addition, they show that the SH2, Ser-12/48, and myristylation regions may be important for efficient interaction of pp60c-src with components of the beta-adrenergic pathway. Our data also support the possibility that the Gs alpha protein may be an in vivo target for alteration by pp60c-src.

scholarly journals Beta-adrenergic agonists increase maximal output of oxidative phosphorylation in bovine satellite cells1

2020 ◽  
Vol 4 (Supplement_1) ◽  
pp. S94-S97
Author(s):  
Renae L Sieck ◽  
Leah K Treffer ◽  
Martonio Ponte Viana ◽  
Oleh Khalimonchuk ◽  
Ty B Schmidt ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Adrenergic Agonists ◽  
Beta Adrenergic ◽  
Beta Adrenergic Agonists ◽  
Maximal Output

Interaction between the antidepressant-like behavioral effects of beta adrenergic agonists and the cyclic AMP PDE inhibitor rolipram in rats

2005 ◽  
Vol 182 (1) ◽  
pp. 104-115 ◽  
Author(s):  
Han-Ting Zhang ◽  
Ying Huang ◽  
Kathleen Mishler ◽  
Sandra C. Roerig ◽  
James M. O'Donnell
Keyword(s):  
Cyclic Amp ◽  
Behavioral Effects ◽  
Adrenergic Agonists ◽  
Beta Adrenergic ◽  
Beta Adrenergic Agonists
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