Identification of a B2 bradykinin receptor expressed by PC12 pheochromocytoma cells.

Nardone, Julie; Gerald, Christophe; Rimawi, Lama; Song, Lucy; Hogan, Patrick G.

doi:10.1073/pnas.91.10.4412

Cited by 30 publications

(19 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This conclusion is supported by the evidence that in PC12 pheochromocytoma cells, LEV reduced, in a concentrationdependent manner, the [Ca 2ϩ ] i increase elicited by BK and ATP, two neurotransmitters that, in these cells, trigger IP 3 generation via the G q -coupled B 2 (Nardone et al, 1994) and P 2Y (Moskvina et al, 2003) receptors. Actually, several arguments sustain the hypothesis that, under our experimental conditions, these responses depended on IP 3 -triggered Ca 2ϩ store depletion rather than on Ca 2ϩ influx from the extracellular space or Ca 2ϩ release from the Rya stores.…”

Section: Discussionsupporting

confidence: 71%

“…[ 3 H]BK binding to BK plasma membrane receptors in PC12 cells and the potential interference of LEV with this binding reaction were studied using the experimental approach reported by Nardone et al (1994). Briefly, PC12 cells were plated onto 12-well plastic dishes at the density of 1 ϫ 10 6 cells/well.…”

Section: Methodsmentioning

confidence: 99%

“…1, A-D). (Nardone et al, 1994;Moskvina et al, 2003). ATP and BK were delivered to PC12 cells in a nominally Ca 2ϩ -free Krebs' solution obtained by omitting Ca 2ϩ ions and by adding 1.5 mM EGTA.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells

Cataldi¹,

Lariccia

Secondo

et al. 2005

J Pharmacol Exp Ther

View full text Add to dashboard Cite

The present study explores the hypothesis that the new antiepileptic drug levetiracetam (LEV) could interfere with the inositol 1,4,5-trisphosphate (IP 3 )-dependent release of intracellular Ca 2ϩ initiated by G q -coupled receptor activation, a process that plays a role in triggering and maintaining seizures. We assessed the effect of LEV on the amplitude of [Ca 2ϩ ] i response to bradykinin (BK) and ATP in single Fura-2/acetoxymethyl ester-loaded PC12 rat pheochromocytoma cells, which express very high levels of LEV binding sites. LEV dose-dependently reduced the [Ca 2ϩ ] i increase, elicited either by 1 M BK or by 100 M ATP (IC 50 , 0.39 Ϯ 0.01 M for BK and 0.20 Ϯ 0.01 M for ATP; Hill coefficients, 1.33 Ϯ 0.04 for BK and 1.38 Ϯ 0.06 for ATP). Interestingly, although the discharge of ryanodine stores by a process of calcium-induced calcium release also took place as part of the [Ca 2ϩ ] i response to BK, LEV inhibitory effect was mainly exerted on the IP 3 -dependent stores. In fact, the drug was still effective after the pharmacological blockade of ryanodine receptors. Furthermore, LEV did not affect Ca 2ϩ stored in the intracellular deposits since it did not reduce the amplitude of [Ca 2ϩ ] i response either to thapsigargin or to ionomycin. In conclusion, LEV inhibits Ca 2ϩ release from the IP 3 -sensitive stores without reducing Ca 2ϩ storage into these deposits. Because of the relevant implications of IP 3 -dependent Ca 2ϩ release in neuron excitability and epileptogenesis, this novel effect of LEV could provide a useful insight into the mechanisms underlying its antiepileptic properties.

show abstract

Section: Discussionsupporting

confidence: 71%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells

Cataldi¹,

Lariccia

Secondo

et al. 2005

J Pharmacol Exp Ther

View full text Add to dashboard Cite

show abstract

“…I. Engel (National Institutes of Health, Bethesda, MD). EcoRI fragments containing A␣ d and A␤ d cDNA were subcloned into the polylinker EcoRI site of the expression plasmid pLGP-3, kindly provided by Dr. P. Hogan (Harvard Medical School, Boston, MA), which is derived from the plasmid pCD and contains an SV40 promotor for transient expression of cDNA in COS cells and fd to generate single-stranded templates for mutagenesis (39). Site-directed mutagenesis was carried out on uracil-labeled, single-stranded templates, as described previously (27), using oligonucleotides listed in Table I to generate variants.…”

Section: Methodsmentioning

confidence: 99%

An Ion Pair in Class II Major Histocompatibility Complex Heterodimers Critical for Surface Expression and Peptide Presentation

Nalefski

Shaw

Rao

1995

Journal of Biological Chemistry

View full text Add to dashboard Cite

In this report we demonstrate that the ion pair Arg-80␣ and Asp-57␤, located in the peptide-binding site of nearly all class II major histocompatibility complex (MHC) proteins, is important for surface expression and function of the murine class II heterodimer I-A d . Charge reversal at either of these two residues by site-directed mutagenesis generated mutant class II molecules that failed to appear at the cell surface. This defect in surface expression was partially reversed when the invariant chain was present or when the mutants were paired with the corresponding charge-reversed variant of the opposite chain. Surprisingly, surface expression was restored when cells expressing the single-site mutants were cultured at reduced temperature. In addition, the substitution of Asp-57␤ with residues found in alleles of class II molecules associated with diabetes resulted in heterodimers that were inefficiently expressed at the cell surface and presented foreign peptide poorly. Together, these results demonstrate that the formation of a salt-bridge between Arg-80␣ and Asp-57␤ is required for efficient surface expression of class II MHC molecules, therefore representing an important step in the assembly and transport of functional class II heterodimers to the cell surface.

show abstract

“…In mammals two principal types of kinin receptors, B1 and B2, with distinct pharmacological properties have been cloned and characterized (1)(2)(3)(4). Their ligands are derived from bradykinin, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg.…”

mentioning

confidence: 99%

Cloning and Functional Characterization of the Ornithokinin Receptor

Schröeder

Beug

Müller‐Esterl

1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

Kinins are proinflammatory peptides that dilate vessels, increase vascular permeability, contract smooth muscles, and provoke pain. In mammals two principal types of kinin receptors, B1 and B2, with distinct pharmacological properties have been cloned and characterized (1-4). Their ligands are derived from bradykinin, Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg. Expression of the B1 receptor is induced under pathophysiological conditions such as injury, infection, or chronic inflammation where it mediates hyperalgesia and sensitization (5, 6). The B2 receptor is constitutively expressed in fibroblasts and in epithelial, endothelial, neuronal, and smooth muscle cells (7,8 (11,12). HOE140, a synthetic peptide derived from the bradykinin sequence, is a selective and tightly binding B2 receptor antagonist (13, 14) that lacks partial agonistic activity in most physiological settings (15).Kinins are well conserved peptides that have been identified in invertebrates, e.g. in the wasp (16). In fact the non-mammalian kinins are identical to their human counterpart including a 4-hydroxylation of a proline residue at position 3 (16). Kinins are present in all the major vertebrate classes including reptiles, amphibia, fish, and birds (8). The avian kinin, first described in 1967 (17), and aptly named ornithokinin, differs from the human bradykinin in two positions: Thr substitutes for Ser at position 6, and Leu for Phe at position 8. Ornithokinin, i.e. [Ser 6 ,Leu 8 ]bradykinin, induces transient hypotension in the chicken and contracts smooth muscle cells of the oviduct (17, 18), two physiological activities reminiscent of the kinin effects in mammals. To date the receptor underlying ornithokinin's effects has not been defined. Unlike most of the insect kinins ornithokinin has no effect on the human kinin system, and vice versa (18). The differential binding profiles are likely to reflect distinct structures of the ligand-binding sites of the corresponding receptors, however, the lack of non-mammalian kinin receptor sequences has precluded such comparisons.Here we describe the cloning of an avian kinin receptor using a PCR 1 -based strategy. Expression of the biologically active chicken ornithokinin receptor revealed the unexpected finding that HOE140, the principal antagonist of the mammalian B2 receptors, is a full agonist of the avian receptor as is ornithokinin, whereas bradykinin and [des-Arg 9 ]bradykinin have no effect. Sequence analyses indicate that avian and mammalian kinin receptors are only distantly related. Our results suggest that the ornithokinin receptor is the first member of a novel type of kinin receptors. More importantly, having available a receptor in which HOE140 acts as a full agonist will make the ornithokinin receptor a unique tool to study ligand binding and receptor function at the molecular level. EXPERIMENTAL PROCEDURESSources of Reagents-The pCDNA3, pVL-1392 vectors, and the Liposome Kit were from Invitrogen; oligonucleotides from MWG-Biotech;

show abstract

Identification of a B2 bradykinin receptor expressed by PC12 pheochromocytoma cells.

Cited by 30 publications

References 39 publications

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells

An Ion Pair in Class II Major Histocompatibility Complex Heterodimers Critical for Surface Expression and Peptide Presentation

Cloning and Functional Characterization of the Ornithokinin Receptor

Contact Info

Product

Resources

About

Identification of a B2 bradykinin receptor expressed by PC12 pheochromocytoma cells.

Cited by 30 publications

References 39 publications

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca2+]iIncrease Induced by ATP and Bradykinin in PC12 Cells

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca2+]iIncrease Induced by ATP and Bradykinin in PC12 Cells

An Ion Pair in Class II Major Histocompatibility Complex Heterodimers Critical for Surface Expression and Peptide Presentation

Cloning and Functional Characterization of the Ornithokinin Receptor

Contact Info

Product

Resources

About

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells

The Antiepileptic Drug Levetiracetam Decreases the Inositol 1,4,5-Trisphosphate-Dependent [Ca²⁺]_iIncrease Induced by ATP and Bradykinin in PC12 Cells