Enkephalin Dipeptidyl Carboxypeptidase (Enkephalinase) Activity: Selective Radioassay, Properties, and Regional Distribution in Human Brain

Llorens, C.; Malfroy, Bernard; Gacel, G.; Roques, Bernárd P.; Roy, Jean; Morgat, Jean‐Louis; Javoy‐Agid, F.; Agid, Yves

doi:10.1111/j.1471-4159.1982.tb11500.x

Cited by 98 publications

(39 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1), The significance of these differences is not clear. However, the fact that rat and human enkephalinase have been shown to be identical with respect to a number of properties, including optimal pH, sensitivity to inhibitors and kinetic parameters for the hydrolysis of a number of substrates [12,13,15,16], suggests that these differences do not affect the enzymatic activity of the enzyme.…”

Section: Methodsmentioning

confidence: 99%

“…Enkephalinase activity has been detected in several human tissues including brain [12], neutrophils [ 13,14], kidney [15] and placenta [ 16]. We now report the isolation and characterization of a full-length cDNA clone encoding human enkephalinase, constructed from placenta mRNA, and present a comparison of the human, rat and rabbit enzymes.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)

Malfroy¹,

Kuang²,

Seeburg³

et al. 1988

FEBS Letters

205

View full text Add to dashboard Cite

We have isolated a cDNA clone encoding human enkephalinase (neutral endopeptidase, EC 3.4.24.11) in a ).gt 10 library from human placenta, and present the complete 742 amino acid sequence of human enkephalinase. The human enzyme displays a high homology with rat and rabbit enkephalinase. Like the rat and rabbit enzyme, human enkephalinase contains a single N-terminal transmembrane region and is likely to be inserted through cell membranes with the majority of protein, including its carboxy-terminus, located extracellularly.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)

Malfroy¹,

Kuang²,

Seeburg³

et al. 1988

FEBS Letters

205

View full text Add to dashboard Cite

show abstract

“…The NEP activity was measured using a modification of the procedure of LLORENS et al [19]. Briefly, the tracheae from sensitized and nonsensitized rats were minced and homogenized.…”

Section: Measurement Of Neutral Endopeptidase Activitymentioning

confidence: 99%

Effect of cromolyn on adenosine-induced airway microvascular leakage in sensitized rats

Tamaoki¹,

Yamawaki²,

Taira³

et al. 1999

Eur Respir J

View full text Add to dashboard Cite

Inhalation of adenosine causes bronchoconstriction in asthmatic subjects, but the effect of this purine nucleotide on airway vascular permeability is unknown.In order to determine whether adenosine produces airway microvascular leakage and, if so, to examine the effect of cromolyn (sodium cromoglycate (SCG)) on this extravasation of Evans blue was measured in the airways of ovalbumin-sensitized Brown Norway rats.Inhaled adenosine caused microvascular leakage in sensitized but not in nonsensitized rats, and the response was abolished by capsaicin pretreatment or the tachykinin neurokinin-1 receptor antagonist FK888. Adenosine-induced vascular leakage became apparent in nonsensitized rats when treated with phosphoramidon, and airway neutral endopeptidase activity was lower in sensitized than in nonsensitized animals. The extravasation induced by adenosine in sensitized rats was dose dependently inhibited by SCG aerosols. SCG likewise inhibited microvascular responses to substance P, but had no effect on those to platelet-activating factor.These results suggest that: 1) adenosine induces airway microvascular leakage in sensitized rats through stimulation of neurokinin-1 receptors; 2) this effect is associated with a sensitization-induced decrease in neutral endopeptidase activity; and 3) sodium cromoglycate inhibits adenosine-induced extravasation, presumably via functional antagonism of tachykinins. Eur Respir J 1999; 14: 1082±1087. Adenosine is a naturally occurring purine nucleotide formed by the cleavage of adenosine 5'-monophosphate by 5'-nucleotidase or by the catabolism of S-adenosylhomocysteine. Based on the findings that adenosine can be released from mast cells in both early-and late-phase asthmatic responses via antigen/immunoglobulin E (IgE) interaction after allergen bronchoprovocation [1] and that inhaled adenosine causes bronchoconstriction in asthmatics but not in normal subjects [2], this purine nucleotide is thought to play a role in the pathophysiology of asthma. Increased microvascular permeability and plasma protein extravasation in the airways might contribute to mucosal oedema, inflammatory cell infiltration and epithelial cell desquamation, which are characteristic features of asthma [3]. Previous studies have shown that adenosine induces plasma extravasation in rat skin [4] and hamster cheek pouch [5], but its effect on airway microvascular permeability is unknown.Cromolyn (sodium cromoglycate (SCG)) is an antiallergic drug and has been widely used in the treatment of asthma [6,7]. Although SCG has long been recognized as a mast cell-stabilizing agent [8], its mechanism of action in asthma is still unclear. CROSSMAN et al. [9] showed that oedema formation in the human skin produced by substance P was reduced by SCG, suggesting that SCG may modify tachykinin actions. Therefore, the purposes of the present study were: 1) to determine whether adenosine produces airway vascular leakage; 2) to elucidate the possible involvement of tachykinins in the effect of adenosine; and 3) to deter...

show abstract

“…The data were expressed as the number of inflammatory cells per 100 epithelial cells in the same fields. NEP activity was measured using a modification of the procedure of Llorens et al (1982 …”

Section: Methodsmentioning

confidence: 99%

Airway hyper-responsiveness to neurokinin A and bradykinin following Mycoplasma pneumoniae infection associated with reduced epithelial neutral endopeptidase

Tamaoki¹,

Chiyotani²,

Tagaya³

et al. 1998

Microbiology

View full text Add to dashboard Cite

T o determine whether mycoplasma infection produces airway hyperresponsiveness to tachykinins and bradykinin and, if so, to elucidate the role of neutral endopeptidase (NEP), isolated hamster tracheal segments were studied under isometric conditions in vitro. Nasal inoculation with Mycoplasma pneumoniae potentiated contractile responses to neurokinin A and bradykinin, causing a leftward shift of the dose-response curves to a lower concentration by 1 log unit for each agonist, whereas there was no response with acetylcholine. Pretreatment of tissues with the NEP inhibitor phosphoramidon augmented neurokinin A-and bradykinin-induced contractions in salinetreated control tissues, but did not further potentiate the responsiveness in M. pneumoniae-infected tissues. NEP activity in the tracheal epithelium, but not in epithelium-denuded tissues, was decreased in infected animals. These results suggest that M. pneumoniae infection causes airway bronchoconstrictor hyper-responsiveness to neurokinin A and bradykinin and that this effect may be associated with an inhibition of epithelial NEP activity.

show abstract

Enkephalin Dipeptidyl Carboxypeptidase (Enkephalinase) Activity: Selective Radioassay, Properties, and Regional Distribution in Human Brain

Cited by 98 publications

References 31 publications

Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)

Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)

Effect of cromolyn on adenosine-induced airway microvascular leakage in sensitized rats

Airway hyper-responsiveness to neurokinin A and bradykinin following Mycoplasma pneumoniae infection associated with reduced epithelial neutral endopeptidase

Contact Info

Product

Resources

About