Endothelin Receptors

Henry, Peter J.; Goldie, Roy G.

doi:10.1007/978-3-642-56899-2_4

Cited by 3 publications

(2 citation statements)

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“…The very first step for ET-1 to elicit the biological effects is through binding to its specific receptors (Sokolovsky 1995). Upregulation and (or) downregulation of endothelin receptors has been shown in tissues of patients with different diseases as well as in animal disease models (Henry and Goldie 2001). The purpose of this study was to investigate whether ET-1 binding to various tissues in SHRsp was altered when compared with normotensive Wistar-Kyoto rats (WKY).…”

Section: Introductionmentioning

confidence: 99%

Upregulation of endothelin-1 binding in tissues of salt-loaded stroke-prone spontaneously hypertensive rats

Savage¹,

Jeng²

2002

Can. J. Physiol. Pharmacol.

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Upon maintained on a 1% NaCl drinking solution beginning at 7 weeks of age, the stroke-prone spontaneously hypertensive rat (SHRsp) developed severe hypertension and stroke; most died by 16 weeks. The mechanism by which these diseases evolve remains unclear. Endothelin-1 (ET-1) is a potent, peptidic vasoconstrictor and is implicated in the pathogenesis of various cardiovascular, renal, and central nervous system diseases. The purpose of the present study was to compare the binding of [125I]ET-1 to the brain, heart, kidney, liver, and spleen membrane preparations of 16-week-old SHRsp and age-matched normotensive Wistar-Kyoto rats (WKY). The KD values for [125I]ET-1 binding to the corresponding tissues of the two strains were not significantly different, except in the brain (SHRsp: 17 +/- 1 pM; WKY: 24 +/- 1 pM). In contrast, the Bmax values measured in the brain, heart, kidney, and liver of SHRsp were 1.5- to 2.1-fold greater than those of their WKY counterparts. Competition of [125I]ET-1 binding to the membrane preparations by the specific ETA receptor antagonist BQ-123 or the specific ETB receptor agonist sarafotoxin S6c revealed a similar proportion of ETA and ETB receptor subtypes in the corresponding tissues of the two rat strains. These results indicate that ET-1 binding is upregulated in SHRsp and suggest that ET-1 may play a pathophysiological role in this animal model of genetic hypertension.

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Section: Introductionmentioning

confidence: 99%

Upregulation of endothelin-1 binding in tissues of salt-loaded stroke-prone spontaneously hypertensive rats

Savage¹,

Jeng²

2002

Can. J. Physiol. Pharmacol.

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“…In humans, there are three isoforms of ETs, namely ET-1, ET-2, and ET-3, that interact with two distinct G protein-coupled receptors, ET A and ET B , to exert their biological effects [2]. These vasoconstrictors are initially synthesized as inactive prepropeptides that are activated by sequential, post-translational processing to produce the mature peptides.…”

Section: Introductionmentioning

confidence: 99%

Expression, purification and characterization of the monomeric and dimeric forms of soluble bovine endothelin converting enzyme-1a

Kulathila¹,

Clark²,

Savage³

et al. 2002

Clinical Science

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In this study, the catalytic domain of bovine endothelin converting enzyme-1a (ECE-1a) was cloned into a baculovirus transfer vector behind the human alkaline phosphatase signal sequence. The recombinant baculovirus was then used to infect High Five(TM) insect cells in suspension culture. Both the monomeric (85 kDa) and dimeric (170 kDa) forms of soluble ECE-1a were purified to electrophoretic homogeneity from concentrated culture media following sequential concanavalin A, SP-Sepharose, Mono Q and gel filtration column chromatography. Typically, approximately 11 mg of ECE-1a monomer and 6 mg of dimer were obtained from l litre of culture medium. No interconversion of the two forms was detected after purification. Both forms of ECE-1a had a pH optimum of 7.0, were maximally stimulated by NaCl at a concentration of 500 mM, and were inhibited to the same extent by metalloprotease inhibitors such as phosphoramidon and EDTA. However, in kinetic studies using big endothelin-1 (ET-1) as a substrate, the K(m) and k(cat) values for the monomer were 2.2 microM and 1.6 min(-1) respectively, while those of the dimer were 1.4 microM and 4.9 min(-1) respectively. These results show that, although the two forms of ECE-1a behave similarly in many aspects, the dimeric enzyme is more efficient in catalysing the conversion of big ET-1 to ET-1. The present protocol can be utilized to prepare large quantities of both forms of ECE-1a for further biochemical and structural characterization.

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Hypertensive and Hypotensive Snake Venom Components

Bdolah

2010

Toxins and Hemostasis

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Endothelin Receptors

Cited by 3 publications

References 246 publications

Upregulation of endothelin-1 binding in tissues of salt-loaded stroke-prone spontaneously hypertensive rats

Upregulation of endothelin-1 binding in tissues of salt-loaded stroke-prone spontaneously hypertensive rats

Expression, purification and characterization of the monomeric and dimeric forms of soluble bovine endothelin converting enzyme-1a

Hypertensive and Hypotensive Snake Venom Components

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