Opioid receptors in rat cardiac sarcolemma: effect of phenylephrine and isoproterenol

Ventura, Carlo; Bastagli, L; Bernardi, P; Caldarera, Claudio Marcello; Guarnieri, Carlo

doi:10.1016/0005-2736(89)90456-2

Cited by 127 publications

(69 citation statements)

References 38 publications

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“…However, ambiguity exists regarding the receptor subtypes expressed and activated by agonists in the myocardium (46); in particular, the presence of -OR has been disputed (47). Past studies that utilized radioligand binding experiments were performed on membranes prepared from whole hearts, making it difficult to distinguish sarcolemmal from intracellular CM membranes and membranes contributed by other cell types.…”

Section: Discussionmentioning

confidence: 99%

G-protein-coupled Receptor Signaling Components Localize in Both Sarcolemmal and Intracellular Caveolin-3-associated Microdomains in Adult Cardiac Myocytes

Head

Patel

Roth

et al. 2005

Journal of Biological Chemistry

198

196

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This study tests the hypothesis that G-protein-coupled receptor (GPCR) signaling components involved in the regulation of adenylyl cyclase (AC) localize with caveolin (Cav), a protein marker for caveolae, in both cellsurface and intracellular membrane regions. Using sucrose density fractionation of adult cardiac myocytes, we detected Cav-3 in both buoyant membrane fractions (BF) and heavy/non-buoyant fractions (HF); ␤ 2 -adrenergic receptors (AR) in BF; and AC5/6, ␤ 1 -AR, M 4 -muscarinic acetylcholine receptors (mAChR), -opioid receptors, and G␣ s in both BF and HF. In contrast, M 2 -mAChR, G␣ i3 , and G␣ i2 were found only in HF. Immunofluorescence microscopy showed co-localization of Cav-3 with AC5/6, G␣ s , ␤ 2 -AR, and -opioid receptors in both sarcolemmal and intracellular membranes, whereas M 2 -mAChR were detected only intracellularly. Immunofluorescence of adult heart revealed a distribution of Cav-3 identical to that in isolated adult cardiac myocytes. Upon immunoelectron microscopy, Cav-3 co-localized with AC5/6 and G␣ s in sarcolemmal and intracellular vesicles, the latter closely allied with T-tubules. Cav-3 immunoprecipitates possessed components that were necessary and sufficient for GPCR agonist-promoted stimulation and inhibition of cAMP formation. The distribution of GPCR, G-proteins, and AC with Cav-3 in both sarcolemmal and intracellular T-tubule-associated regions indicates the existence of multiple Cav-3-localized cellular microdomains for signaling by hormones and drugs in the heart.

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Section: Discussionmentioning

confidence: 99%

G-protein-coupled Receptor Signaling Components Localize in Both Sarcolemmal and Intracellular Caveolin-3-associated Microdomains in Adult Cardiac Myocytes

Head

Patel

Roth

et al. 2005

Journal of Biological Chemistry

198

196

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“…As a result, oxygen consumption, as reflected by the product of force ϫ rate, was significantly increased. Interestingly, despite the increase in oxygen consumption, survival of the heart was greatly prolonged the presence of ␦-and -, but not -, opioid receptors in the rat heart (31,32,36).…”

Section: [ 3 H]ne Uptake In Cardiac Synaptosomesmentioning

confidence: 96%

A highly potent peptide analgesic that protects against ischemia-reperfusion-induced myocardial stunning

Soong

Zhao

et al. 2002

American Journal of Physiology-Heart and Circulatory Physiology

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We recently discovered an opioid peptide analgesic, 2′,6′-dimethyltyrosine (Dmt)-d-Arg-Phe-Lys-NH2([Dmt1]DALDA), that can protect against ischemia-induced myocardial stunning. In buffer-perfused hearts, 30-min global ischemia followed by reperfusion resulted in a significant increase in norepinephrine (NE) overflow immediately upon reperfusion and significant decline in contractile force (45%). Pretreatment with [Dmt1]DALDA before ischemia completely abolished myocardial stunning and significantly reduced NE overflow (68%). In contrast, pretreatment with morphine before ischemia only provided brief protection against myocardial stunning and no reduction in NE overflow. [Dmt1]DALDA inhibited [3H]NE uptake into cardiac synaptosomes in vitro (IC50 = 3.9 μM), whereas morphine had no effect. Surprisingly, protection against myocardial stunning was apparent even when hearts were perfused with [Dmt1]DALDA only upon reperfusion, whereas reperfusion with morphine had no effect. Binding studies with [3H][Dmt1]DALDA revealed no high-affinity specific binding in cardiac membranes, suggesting that the cardioprotective actions of [Dmt1]DALDA are not mediated via opioid receptors. These findings suggest that [Dmt1]DALDA is a potent analgesic that may be useful for myocardial stunning resulting from cardiac interventions or myocardial ischemia.

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“…However, opioid receptors are also present in non-neuronal tissues. The opioid receptor is present in human placenta (Porthe et al, 1981;Mansson et al, 1994) and rat heart myocytes (Ventura et al, 1989;Wong et al, 1990). Caveolins are widely distributed in peripheral tissues, including heart and placenta.…”

Section: Cho Cells As a Modelmentioning

confidence: 99%

“…Salvinorin A, a potent hallucinogen extracted from leaves of the plant Salvia divinorum, is a potent and selective agonist of the opioid receptor (Roth et al, 2002). opioid receptors are also present in non-neuronal tissues, including the human placenta (Porthe et al, 1981;Mansson et al, 1994) and the rat heart (Ventura et al, 1989). In the human placenta, opioid receptors regulate secretion of human chorionic gonadotropin (Valette et al, 1983) and release of human lactogen (Petit et al, 1991).…”

mentioning

confidence: 99%

Localization of the κ Opioid Receptor in Lipid Rafts

Xu¹,

Yoon²,

Huang³

et al. 2006

J Pharmacol Exp Ther

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Lipid rafts are microdomains of plasma membranes enriched in cholesterol and sphingolipids in the outer layer. We determined whether opioid receptors (KOR) in human placenta and FLAG (DYKDDDDK)-tagged human KOR (FLAG-hKOR) expressed in Chinese hamster ovary (CHO) cells are localized in lipid rafts and whether changes in cholesterol contents affect hKOR properties and signaling. Lipid rafts were prepared from placenta membranes and CHO cells expressing FLAG-hKOR using the Na 2 CO 3 method and fractionation through a sucrose density gradient. The majority of the KOR in the placenta and FLAG-hKOR in CHO cells, determined by [ 3 H]diprenorphine binding and/or immunoblotting with an anti-FLAG antibody, was present in low-density fractions, coinciding with high levels of caveolin-1 and cholesterol, markers of lipid rafts, which indicated that the KOR is localized in lipid rafts. Pretreatment with 2% methyl ␤-cyclodextrin (MCD) reduced cholesterol content by ϳ48% and changed the cells from spindle-shaped to spherical. MCD treatment disrupted lipid rafts, shifted caveolin-1 and FLAG-hKOR to higher density fractions, increased the affinity of (Ϫ)-(trans)-3,4-dichloro-N-methyl-N-[2-(1-pyrrolidinyl)cyclohexyl]benzeneacetamide (U50,488H) for the hKOR, and greatly increased U50,488H-induced [35 S]guanosine 5Ј-O-(3-thio)triphosphate binding and p42/44 mitogen-activated protein kinase phosphorylation. Cholesterol replenishment reversed all the MCD effects. Caveolin-1 immunoprecipitated with G␣ i proteins and MCD treatment reduced caveolin-1 associated with G␣ i proteins, which may contribute to the enhanced agonist-induced G protein activation. Caveolin-1 also immunoprecipitated with FLAG-hKOR, but MCD treatment had no effect on the association. Thus, the KOR is located in lipid rafts and its localization in the microdomains greatly affects coupling to G proteins.Plasma membranes were traditionally viewed as uniform lipid bilayers and G protein-coupled receptors (GPCRs), G proteins, and membrane-bound effectors were randomly distributed in plasma membranes. In recent years, the concept that lipid rafts function as microdomains in plasma membranes to concentrate signaling molecules for regulated activation by related receptors has gained increasing acceptance (Pike, 2003;Chini and Parenti, 2004;Cohen et al., 2004). Lipid rafts are microdomains of cell membranes highly enriched in cholesterol and sphingolipids in the outer layer. Brown and Rose (1992) proposed the following operational definition of lipid rafts: when cell membranes were solubilized with ice-cold nonionic detergents such as Triton X-100 (1% for 1 h at 4°C) followed by sucrose density gradient centrifugation; lipid rafts are resistant to detergent solubilization and float in the lighter fractions, whereas the bulk of the solubilized cellular lipids and proteins are in the high-density fractions (Brown and Rose, 1992). There are two types of lipid rafts: planar lipid rafts and caveolae. Caveolae, a specialized subtype of lipid rafts, are flask-shaped invagi...

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Opioid receptors in rat cardiac sarcolemma: effect of phenylephrine and isoproterenol

Cited by 127 publications

References 38 publications

G-protein-coupled Receptor Signaling Components Localize in Both Sarcolemmal and Intracellular Caveolin-3-associated Microdomains in Adult Cardiac Myocytes

G-protein-coupled Receptor Signaling Components Localize in Both Sarcolemmal and Intracellular Caveolin-3-associated Microdomains in Adult Cardiac Myocytes

A highly potent peptide analgesic that protects against ischemia-reperfusion-induced myocardial stunning

Localization of the κ Opioid Receptor in Lipid Rafts

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