β3-adrenergic receptor activation increases human atrial tissue contractility and stimulates the L-type Ca2+ current

Skeberdis, Vytenis Arvydas; Gendviliene,; Zablockaitė, Danguolė; Treinys, Rimantas; Mačianskienė, Regina; Bogdelis, Andrius; Jurevičius, Jonas; Fischmeister, Rodolphe

doi:10.1172/jci32519

Cited by 69 publications

(116 citation statements)

References 68 publications

(95 reference statements)

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“…Though being the lowest in abundance, the expression of ADRB3 mRNA in the heart of sheep was comparable with the studies reported by Chamberlain et al (1999) and Skeberdis et al (2008) in humans and by Evans et al (1996) in rats. The function of ADRB3 in the heart includes increasing the contractility of myocardial tissue as indicated in studies of patients with heart failure (Moniotte et al, 2001;Morimoto et al, 2004) and dogs with pacing-induced heart failure (Cheng et al, 2001).…”

Section: Discussionsupporting

confidence: 86%

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Liu

et al. 2011

Animal

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The b-3 adrenergic receptor (ADRB3) is a G-protein coupled receptor involved in regulating lipolysis, as part of homeostatic regulation. In this study, South African Mutton Merino and Shanxi Dam Line were used to study the distribution and quantification of ADRB3 in adipose (subcutaneous, omental, retroperitoneal, mesenteric and perirenal fat) and non-adipose (heart, liver, spleen, lung and kidney) tissues of sheep. The protein was determined by immunohistochemical technique and by mRNA abundance via real-time polymerase chain reaction. ADRB3 was detected in all studied tissues with abundance in adipose tissues higher than in non-adipose tissues ( P , 0.001). For adipose tissues, greater expression was found in deep deposits such as great omental and retroperitoneal fat than in subcutaneous fat ( P , 0.05). Significant differences ( P , 0.05) both for mRNA and for protein expression also existed between the two sheep flocks. These findings are consistent with the known function of ADRB3 in mediating lipolysis and homeostasis in adipose tissues.Keywords: b-3 adrenergic receptor, sheep, tissues, mRNA expression, immunohistochemistry ImplicationsIn this study, the b-3 adrenergic receptor (ADRB3) expression in various tissues of sheep was detected by immunohistochemical technique and by mRNA abundance via real-time PCR. Despite its low expression, the presence of ADRB3 in the spleen and kidney was found in livestock for the first time. Generally, ADRB3 expressed higher in adipose than in non-adipose tissues, and for the former, it was higher in deep fat deposits than in subcutaneous fat. The distributions are consistent with the known functions of ADRB3 in mediating lipolysis and homeostasis in adipose tissues, and relaxation of vascular smooth muscle in the cardiovascular system. The relation between low expression and its function in some viscera, for example, lung, spleen and kidney of sheep deserves further study.Introduction b-Adrenergic receptors (ADRBs) are G-protein coupled receptors that mediate effects of the endogenous catecholamines adrenaline and noradrenaline. Three subtypes of ADRBs have been identified, named ADRB1, ADRB2 and ADRB3, respectively. These receptors are present in most mammalian tissues, but the distribution of each subtype varies among tissues in a given species. Among the various physiological roles of ADRBs, the ADRB3 subtype mediates lipolysis and stimulates thermogenesis in adipose tissues (Cannon and Nedergaard, 2004) by activating uncoupling protein in mitochondria.In early studies, ADRB3 was identified mainly on the surface of white and brown adipocytes as reviewed by Strosberg (1997). In recent years, expression of the protein was also found in the human heart (Rozec and Gauthier , (Rodriguez et al., 1995).It has been confirmed that the mRNA of the ADRB3 gene is expressed in various tissues of domestic animals. The 2.0 kb ADRB3 transcript in the bovine brown adipose tissue (PietriRouxel et al., 1995), and two transcripts of 2.2 and 1.9 kb in porcine subcutaneous fat (McNeel and ...

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Section: Discussionsupporting

confidence: 86%

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Liu

et al. 2011

Animal

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“…We hypothesized that blocking the breakdown of endogenous cAMP by inhibition of cNMP phosphodiesterase activity could therefore affect NO generation in the plant cell. Animal and plant cNMP phosphodiesterase is sensitive to the inhibitor 1-methyl-3-(2-methylpropyl)-7H-purine-2,6-dione (IBMX) (31,32). Application of IBMX to leaf epidermal peels from WT plants evokes NO generation in the absence of a pathogen signal (i.e., the PAMP LPS) (Fig.…”

Section: Cnmp Cngcs and Immune Signalingmentioning

confidence: 99%

Ca²⁺, cAMP, and transduction of non-self perception during plant immune responses

Qi²,

Smigel³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

125

116

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Ca 2+ influx is an early signal initiating cytosolic immune responses to pathogen perception in plant cells; molecular components linking pathogen recognition to Ca 2+ influx are not delineated. Work presented here provides insights into this biological system of non-self recognition and response activation. We have recently identified a cyclic nucleotide-activated ion channel as facilitating the Ca 2+ flux that initiates immune signaling in the plant cell cytosol. Work in this report shows that elevation of cAMP is a key player in this signaling cascade. We show that cytosolic Ca 2+ elevation, nitric oxide (NO) and reactive oxygen species generation, as well as immune signaling, lead to a hypersensitive response upon application of pathogens and/or conserved molecules that are components of microbes and are all dependent on cAMP generation. Exogenous cAMP leads to Ca 2+ channel-dependent cytosolic Ca 2+ elevation, NO generation, and defense response gene expression in the absence of the non-self pathogen signal. Inoculation of leaves with a bacterial pathogen leads to cAMP elevation coordinated with Ca 2+ rise. cAMP acts as a secondary messenger in plants; however, no specific protein has been heretofore identified as activated by cAMP in a manner associated with a signaling cascade in plants, as we report here. Our linkage of cAMP elevation in pathogen-inoculated plant leaves to Ca 2+ channels and immune signaling downstream from cytosolic Ca 2+ elevation provides a model for how non-self detection can be transduced to initiate the cascade of events in the cell cytosol that orchestrate pathogen defense responses.

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“…[87][88][89][90] Other works reported full inhibition of effects of β-AR agonists in frog and rat ventricular cardiomyocytes by dialyzing cells with 2 to 5 mmol/L Rp-cAMPS, 16 µmol/L PKI (which is >3 orders of magnitude higher than its K i ), 20 µmol/L PKI peptide (PKI [15][16][17][18][19][20][21][22] ; K i =36 nmol/L), [91][92][93] or with 1 µmol/L H-89 applied externally. 94 Although the latter studies used rather high doses of inhibitors, the accumulated data strongly support the view that a major part and possibly all of the β-AR enhancement of cardiac Ca V 1.2 is mediated by activation of PKA.…”

Section: Pka Inhibitors and β-Ar Regulationmentioning

confidence: 79%

Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

Weiss

Benmocha

et al. 2013

Circulation Research

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Abstract:In the heart, adrenergic stimulation activates the β-adrenergic receptors coupled to the heterotrimeric stimulatory G s protein, followed by subsequent activation of adenylyl cyclase, elevation of cyclic AMP levels, and protein kinase A (PKA) activation. One of the main targets for PKA modulation is the cardiac L-type Ca 2+ channel (Ca V 1.2) located in the plasma membrane and along the T-tubules, which mediates Ca 2+ entry into cardiomyocytes. β-Adrenergic receptor activation increases the Ca 2+ current via Ca V 1.2 channels and is responsible for the positive ionotropic effect of adrenergic stimulation. Despite decades of research, the molecular mechanism underlying this modulation has not been fully resolved. On the contrary, initial reports of identification of key components in this modulation were later refuted using advanced model systems, especially transgenic animals. Some of the cardinal debated issues include details of specific subunits and residues in Ca

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β3-adrenergic receptor activation increases human atrial tissue contractility and stimulates the L-type Ca2+ current

Cited by 69 publications

References 68 publications

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Ca²⁺, cAMP, and transduction of non-self perception during plant immune responses

Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

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β3-adrenergic receptor activation increases human atrial tissue contractility and stimulates the L-type Ca2+ current

Cited by 69 publications

References 68 publications

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Distribution and quantification of β-3 adrenergic receptor in tissues of sheep

Ca2+, cAMP, and transduction of non-self perception during plant immune responses

Regulation of Cardiac L-Type Ca 2+ Channel Ca V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

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Ca²⁺, cAMP, and transduction of non-self perception during plant immune responses

Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway