Mediation of most atypical effects by species homologues of the β<sub>3</sub>‐adrenoceptor

Blin, Nathalie; Nahmias, Clara; Drumare, Marie F.; Strosberg, A. Donny

doi:10.1111/j.1476-5381.1994.tb13167.x

Cited by 93 publications

(67 citation statements)

References 38 publications

(57 reference statements)

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“…Partial agonism at the cloned human, rat, and murine β 3 -adrenoceptor was also reported from other studies (Blin et al 1994;Liggett 1992). Accordingly, CGP 12,177 was also only a partial agonist for relaxation of isolated rat bladder strips, an effect not antagonized by low propranolol concentrations (Frazier et al 2006;Longhurst and Levendusky 1999).…”

Section: Adrenaline and Noradrenalinesupporting

confidence: 77%

“…Another study measuring cAMP accumulation in intact cells confirmed the rank order of potency of β 3 >β 2 >β 1 , but BRL 37,344 was an agonist for all three human subtypes, and the difference in potency between the subtypes was less than ten-fold (Tate et al 1991). Studies including only β 3 -adrenoceptors reported BRL 37,344 to be a full agonist for cAMP accumulation in intact CHO cells at human and mouse but a partial agonist at rat β 3 -adrenoceptors (Blin et al 1994;Liggett 1992). BRL 37,344 has similar affinity for both splice variants of the murine β 3 -adrenoceptor, but its effects, similar to that of many other agonists, are somewhat lower at the β 3b -compared with the β 3a -adrenoceptor, as the former couples to both G s and G i proteins (Hutchinson et al 2002).…”

Section: Adrenaline and Noradrenalinementioning

confidence: 75%

“…Adenylyl cyclase stimulation studies based upon the same cell lines found both adrenaline and noradrenaline to be full agonists at all three subtypes relative to isoprenaline (Hoffmann et al 2004). Using a similar approach with independently created CHO cells, other investigators reported an order of potency for cAMP accumulation in intact cells of β 2 ≥β 1 >β 3 for adrenaline and of β 1 >β 3 >β 2 for noradrenaline (Tate et al 1991 (Blin et al 1994;Hoffmann et al 2004;Liggett 1992). Similar values were reported for the murine receptor (Blin et al 1994), but the affinity of BRL 37,344 at the rat and bovine receptor may be 20-fold and 100-fold higher, respectively, compared with its human orthologue (Liggett 1992;Pietri-Rouxel and Strosberg 1995).…”

Section: Adrenaline and Noradrenalinementioning

confidence: 96%

“…Using a similar approach with independently created CHO cells, other investigators reported an order of potency for cAMP accumulation in intact cells of β 2 ≥β 1 >β 3 for adrenaline and of β 1 >β 3 >β 2 for noradrenaline (Tate et al 1991 (Blin et al 1994;Hoffmann et al 2004;Liggett 1992). Similar values were reported for the murine receptor (Blin et al 1994), but the affinity of BRL 37,344 at the rat and bovine receptor may be 20-fold and 100-fold higher, respectively, compared with its human orthologue (Liggett 1992;Pietri-Rouxel and Strosberg 1995). A direct comparative study of all three human subtypes found a rank order of potency of β 3 >β 2 >β 1 with an approximately 20-and 100-fold selectivity, respectively, for the former vs. the two latter subtypes (Table 2) (Hoffmann et al 2004).…”

Section: Adrenaline and Noradrenalinementioning

confidence: 99%

“…A variety of other drugs have been reported to be agonists at β 3 -adrenoceptors, including clenbuterol (Hutchinson et al 2006) and zinterol (Hutchinson et al 2006) and the experimental compounds ICI 215,001 (Baker 2005;Blin et al 1994;Tesfamariam and Allen 1994), FK175 (Fujimura et al 1999), FR 149175 (Hatakeyama et al 2004), FR 165101 (Uchida et al 2005), GS-332 (Morita et al 2000), KUL-7211 (Tomiyama et al 2003), andL-796,568 (van Baak et al 2002). Some of these compounds may have much greater selectivity for β 3 -compared with β 1 -and β 2 -adrenoceptors and may also lack the ancillary properties of BRL 37,344 or CGP 12,177, but overall, too little data have been published to allow a thorough evaluation.…”

Section: Miscellaneous Other Agonistsmentioning

confidence: 99%

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Tools to study β3-adrenoceptors

Vrydag

Michel

2007

Naunyn-Schmied Arch Pharmacol

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β 3 -adrenoceptors mediate some of the effects of catecholamines on tissues such as blood vessels or the urinary bladder and are putative targets for the treatment of diseases such as the overactive bladder syndrome. Progress in the understanding of the presence, function, and regulation of β 3 -adrenoceptors has been hampered by a lack of highly specific tools. "Classical" is not selective for β 3 -adrenoceptors, at least in humans, and may actually be a partial agonist. Radioligands, which are suitable either for the selective labeling of β 3 -adrenoceptors or for the nonselective labeling of all β-adrenoceptor subtypes, are also missing. β 3 -and β 1 /β 2 double knockout mice have been reported, but their usefulness for extrapolations in humans is questionable based upon major differences between humans and rodents with regard to the ligand recognition and expression profiles of β 3 -adrenoceptors. While the common availability of more selective agonists and antagonists at the β 3 -adrenoceptor is urgently awaited, the limitations of the currently available tools need to be considered in studies of β 3 -adrenoceptor for the time being.

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Section: Adrenaline and Noradrenalinesupporting

confidence: 77%

Section: Adrenaline and Noradrenalinementioning

confidence: 75%

Section: Adrenaline and Noradrenalinementioning

confidence: 96%

Section: Adrenaline and Noradrenalinementioning

confidence: 99%

Section: Miscellaneous Other Agonistsmentioning

confidence: 99%

See 3 more Smart Citations

Tools to study β3-adrenoceptors

Vrydag

Michel

2007

Naunyn-Schmied Arch Pharmacol

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Regulation of Glucose Transporters by Insulin and Exercise: Cellular Effects and Implications for Diabetes

Klip

Marette

2001

Comprehensive Physiology

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The sections in this article are: Properties of the Glucose Transporter Families The GLUT Family Acute Regulation of Glucose Transporters by Insulin‐Responsive Tissues The Glucose Transporter Recruitment Hypothesis Insulin‐Responsive Glucose Transporters Testing and Verification of the Recruitment Hypothesis Biochemical Characteristics of The Glut‐4‐Containing Organelle Resident Proteins Proteins Involved in Vesicle Docking and Fusion Low‐Molecular‐Weight G Proteins Insulin Signals Involved in The Mobilization of Glucose Transporters Testing the Participation of a Signaling Pathway Effects of Prolonged Exposure to Insulin on the Glucose Transporters Regulation of Glucose Transporters by Exercise Effects of Exercise In Vivo: Roles of Hypoxia, Blood Flow, and Muscle Fiber Composition Glucose Transporters in Exercised Muscles Signaling Mechanism of Contraction‐Induced Glucose Transport Glucose Transporters in Diabetes Glucose Transporters in Insulin‐Dependent Diabetes Mellitus Glucose Transporters in Obesity and Non‐Insulin‐Dependent Diabetes Mellitus Proposed Mechanisms Leading to Impaired GLUT‐4 Translocation in Diabetes GLUT‐4 Translocation Defect: Primary or Acquired? Effects of Antidiabetic Drugs on Glucose Transporters Lessons from the Manipulation of Glucose‐Transporter Expression by Transgenic Mouse Approaches and Natural Mutations GLUT‐1 Overexpression in Muscle GLUT‐4 Overexpression in Tissues of Natural Expression Selective Overexpression of GLUT‐4 in Muscle GLUT‐4 Overexpression in Fat GLUT‐4 Ablation A Naturally Occurring Genetic Abnormality in GLUT‐1 Expression Concluding Remarks

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Structure, Function, and Regulation of the Three β‐Adrenergic Receptors

Ad¹

1995

Obesity Research

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STROSBERG,A DONNY. Structure,function and regulation of the three P-adrenergic receptors. Obes Res.Three P-adrenergicreceptorsubtypes arenow known to be functionally expressedin mammals. Allthree belong to the R,G family of receptors coupled to Gproteins, and characterized by an extracellular glycosylatedN-terminal and an intracellular C-terminal region and seven transmembrane domains,linkedby threeexta-and threeintracellularloops.The catecholamine ligand binding domain, studied using affinity-labeling and site-directed mutagenesis, is a pocket lined by residues belonging to the transmembrane domains. The region responsibleforthe interactionwith the Gs proteinwhich,when activated,stimulates adenylyl cyclase, is composed of residues belonging to the parts most proximaltothemembraneofintracellular loopi,andthe Cterminal region.The pharmacology of the three subtypes is quite distinct: in fact most of the potent P,/P,antagonists (the well known P blockers) act as agonists on p,. The subtype is resistant to short-term desensitization mediated by phosphorylationthroughPKAor PARK,instarkcontratto the P, or P, subtypes. Various compounds (dexamethasone, butyrate,insulin) upregulate P, or P, subtypes whiledownregulating P, whose expression strictly correlates with differentiation of 3T3-F442A fibroblasts into adipocytes, thus confirming that the expression of the three subtypes may each be regulated independently to exert a specific physiologic role in different tissues or at different stages of development. 1995;3(S~ppl4) :SO 1 S-505s.

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Mediation of most atypical effects by species homologues of the β₃‐adrenoceptor

Cited by 93 publications

References 38 publications

Tools to study β3-adrenoceptors

Tools to study β3-adrenoceptors

Regulation of Glucose Transporters by Insulin and Exercise: Cellular Effects and Implications for Diabetes

Structure, Function, and Regulation of the Three β‐Adrenergic Receptors

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Mediation of most atypical effects by species homologues of the β3‐adrenoceptor

Cited by 93 publications

References 38 publications

Tools to study β3-adrenoceptors

Tools to study β3-adrenoceptors

Regulation of Glucose Transporters by Insulin and Exercise: Cellular Effects and Implications for Diabetes

Structure, Function, and Regulation of the Three β‐Adrenergic Receptors

Contact Info

Product

Resources

About

Mediation of most atypical effects by species homologues of the β₃‐adrenoceptor