Cloning and functional expression of the bovine natriuretic peptide receptor-B (natriuretic factor R1c subtype)

Fenrick, Randy; Babinski, K.; McNicoll, N.; Therrien, Marc; Drouin, Jacques; A, De Léan

doi:10.1007/bf00944079

Cited by 23 publications

(11 citation statements)

References 30 publications

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“…Interestingly, this order of potency to inhibit Na ϩ -dependent pH i recovery correlates with the NP ability to activate cGMP synthesis in NPE cells (10,31). This indicates that the NP type B receptor (NPR-B) is the primary receptor mediating NP cellular effects in NPE cells (10,13). The inhibitory effect of CNP on the rate of Na ϩ -dependent pH i recovery in NPE cells was dose dependent within the range of 10 pM to 100 nM (Fig.…”

Section: Ph I Recording Of Npe Cells In Ciliary Epitheliummentioning

confidence: 76%

Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Fidzinski¹,

Salvador‐Silva²,

Choritz³

et al. 2004

American Journal of Physiology-Cell Physiology

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The natriuretic peptides (NPs) atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP), and C-type natriuretic peptide (CNP) display hypotensive effects in the mammalian eye by lowering the intraocular pressure (IOP), a function that is mediated by the bilayer ocular ciliary epithelium (CE), in conjunction with the trabecular meshwork. ANP regulates Na(+)/H(+) exchanger (NHE) activity, and inhibitors of NHE have been shown to lower IOP. We examined whether NPs influence the NHE activity of the CE, which is comprised of pigmented (PE) and nonpigmented (NPE) epithelial cells, by directly recording the rate of intracellular pH (pH(i)) recovery from its inner NPE cell layer. NPs inhibited, in a dose-dependent manner (1-100 nM), the rate of pH(i) recovery with the order of potency CNP > ANP > BNP, indicative that this inhibition is mediated by the presence of NPR type B receptors. 8-Bromo-cGMP (8-BrcGMP), a nonhydrolyzable analog of cGMP, mimicked NPs in inhibiting the rate of Na(+)-dependent pH(i) recovery. In contrast, ethylisopropyl amiloride (EIPA, 100 nM) or amiloride (10 microM) completely abolished the pH(i) recovery by NHE. 18alpha-Glycyrrhetinic acid (18alpha-GA), a gap junction blocker, attenuated the inhibitory effect of CNP on the rate of pH(i) recovery, suggesting that NHE activity in both cell layers of the CE is coregulated. This interpretation was supported, in part, by the coexpression of NHE-1 isoform mRNA in both NPE and PE cells. The mechanism by which the inhibitory effect of NPs on NHE-1 activity might influence the net solute movement or fluid transport by the bilayer CE remains to be determined.

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Section: Ph I Recording Of Npe Cells In Ciliary Epitheliummentioning

confidence: 76%

Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Fidzinski¹,

Salvador‐Silva²,

Choritz³

et al. 2004

American Journal of Physiology-Cell Physiology

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“…7). The structural characteristics of these amino acids are likely to be critical for the function of this region, because the sequence RGSSYGSL is absolutely conserved in all the NPR-B molecules identified to date, including humans, rats, cows, and eels (15,16,38,39).…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of the Major Phosphorylation Sites of the B-type Natriuretic Peptide Receptor

Potter

Hunter²

1998

Journal of Biological Chemistry

116

120

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C-type natriuretic peptide (CNP) is a newly discovered factor that stimulates vasorelaxation and inhibits cell proliferation. Natriuretic peptide receptor-B (NPR-B) is the primary signaling molecule for CNP. Recently, the guanylyl cyclase activity of NPR-B was shown to correlate with its phosphorylation state, and it was suggested that receptor dephosphorylation is a mechanism of desensitization. We now report the identification and characterization of the major NPR-B phosphorylation sites. Mutagenesis and comigration studies using synthetic phosphopeptides were employed to identify five residues (Ser-513, Thr-516, Ser-518, Ser-523, and Ser-526) within the kinase homology domain that are phosphorylated when NPR-B is expressed in human 293 cells. Mutation of any of these residues to alanine reduced the receptor's phosphorylation state and CNP-dependent guanylyl cyclase activity. The reductions were not explained by decreases in receptor protein level as indicated by immunoblot analysis and determinations of cyclase activity in the absence of CNP or in the presence of detergent. Elimination of all of the phosphorylation sites resulted in a completely dephosphorylated receptor whose CNP-dependent cyclase activity was decreased by >90%. However, unlike NPR-A, the dephosphorylated receptor was not completely unresponsive to hormone. Finally, two additional residues (Gly-521 and Ser-522) were identified that when mutated to alanine reduced the overall phosphorylation state and hormone responsiveness of the receptor without abolishing the phosphorylation of a specific site. These data indicate that phosphorylation of the kinase homology domain is a critical event in the regulation of NPR-B.

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“…Also, peptides such as angiotensin II and vasopressin can act via tyrosine kinase pathways to cause contraction of certain types of smooth muscle (Hollenberg, 1994). A third possibility is that nociceptin exerts its effects via activation of membrane-bound guanylyl cyclase in the same way as atrial natriuretic factor (Fenrick et al, 1994). These and other possible mechanisms could be readily examined in future work; it may be that the preservation of a nociceptin response in the presence of GTP analogs and AlF 3 precludes a role for the direct activation of guanylyl cyclase.…”

Section: Discussionmentioning

confidence: 99%

Nociceptin Inhibits T-Type Ca²⁺Channel Current in Rat Sensory Neurons by a G-Protein-Independent Mechanism

1997

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Nociceptin (orphanin FQ) is a novel, opioid-like, heptadecapeptide that is an endogenous ligand for the opioid receptor-like (ORL 1 ) receptor. Unlike classical opioids, nociceptin can produce hyperalgesia when injected intracerebroventricularly into mice. Despite this, nociceptin has been reported to decrease transmitter release, activate an inwardly rectifying K ϩ conductance, and suppress high-voltage-activated Ca 2ϩ channel conductances (HVA g Ca ) in much the same way as -, ␦-, and -opioids. We report an action of nociceptin that is not shared by morphine: the suppression of low-voltage-activated, transient calcium (barium) current (I Ba,T ) in acutely dissociated rat dorsal root ganglion (DRG) neurons (EC 50 ϭ 100 nM). This effect was reflected as inhibition of bursts of action potentials that can be evoked in "medium-sized" DRG neurons. Experiments with GTP-␥-S (100 M), GDP-␤-S (2 mM), or aluminum fluoride (AlF 3 ) (100 M) in the patch pipette failed to provide evidence for G-protein involvement in nociceptin-induced I Ba,T suppression. By contrast, both morphine and nociceptin suppressed HVA g Ca , and the latter response was affected by intracellular GTP-␥-S, GDP-␤-S, and AlF 3 in ways that confirmed G-protein involvement. The selective effect of nociceptin on I Ba,T may therefore be relevant to understanding why its behavioral actions differ from those of other opioids. This G-proteinindependent effect of the action of nociceptin may reflect a new general mechanism of action for opioid peptides within the nervous system. Key words: LC132 receptor; neuropathic pain; sympathetic ganglion; orphan receptor; enkephalin; endorphin; spinal cord; afterdepolarization; anticonvulsantThe heptadecapeptide nociceptin (orphanin FQ) is an endogenous ligand for the opioid receptor-like (ORL 1 ) receptor (Meunier et al., 1995;Reinscheid et al., 1995;Nothacker et al., 1996). This substance has attracted considerable attention, because unlike conventional opioids it does not produce analgesia when injected intracerebroventricularly into mice; in fact, nociceptin produces hyperalgesia in a tail-flick assay (Meunier et al., 1995;Reinscheid et al., 1995). Despite this, the cellular actions of nociceptin appear similar to those of -, ␦-, and -opioids. Opioids suppress neurotransmitter release (Jessell and Iversen, 1977;MacDonald and Nelson, 1978; Cherubini and North, 1985;Hori et al., 1992;, and -, ␦-, or -opioids attenuate high-voltage-activated C a 2ϩ channel conductances (HVA g C a ) (Hescheler et al., 1987;Surprenant et al., 1990;Schroeder et al., 1991; Moises et al., 1994a,b;Womack and McC leskey, 1995) and activate an inwardly rectif ying K ϩ conductance ( g K IR ) (North et al., 1987;Williams et al., 1988;Grudt and Williams, 1993). Similarly, nociceptin suppresses transmitter release in the periaqueductal gray matter and in the superficial dorsal horn of neonatal rat spinal cord (Liebel et al., 1997). It also inhibits H VA g C a in hippocampal neurons (Knoflach et al., 1996) and in a neuroblastoma cell line (Connor e...

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Cloning and functional expression of the bovine natriuretic peptide receptor-B (natriuretic factor R1c subtype)

Cited by 23 publications

References 30 publications

Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Identification and Characterization of the Major Phosphorylation Sites of the B-type Natriuretic Peptide Receptor

Nociceptin Inhibits T-Type Ca²⁺Channel Current in Rat Sensory Neurons by a G-Protein-Independent Mechanism

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Cloning and functional expression of the bovine natriuretic peptide receptor-B (natriuretic factor R1c subtype)

Cited by 23 publications

References 30 publications

Inhibition of NHE-1 Na+/H+ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Inhibition of NHE-1 Na+/H+ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Identification and Characterization of the Major Phosphorylation Sites of the B-type Natriuretic Peptide Receptor

Nociceptin Inhibits T-Type Ca2+Channel Current in Rat Sensory Neurons by a G-Protein-Independent Mechanism

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Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Inhibition of NHE-1 Na⁺/H⁺ exchanger by natriuretic peptides in ocular nonpigmented ciliary epithelium

Nociceptin Inhibits T-Type Ca²⁺Channel Current in Rat Sensory Neurons by a G-Protein-Independent Mechanism