Contraction of reptile, amphibian, and fish blood vessels by endothelin-1

1991 ◽  
Vol 69 (2) ◽  
pp. 215-217 ◽  
Author(s):  
Thomas C. Poder ◽  
Shai D. Silberberg ◽  
David Rampe
Keyword(s):  
Blood Vessels ◽  
Isometric Force ◽  
Mammalian Species ◽  
Cardinal Vein ◽  
Endothelin 1 ◽  
Systemic Arch ◽  
Fish Blood ◽  
Porcine Endothelial Cells ◽  
Arteries And Veins ◽  
Nanomolar Range

Endothelin-1, a 21 aminio acid peptide originally isolated from porcine endothelial cells, has been reported to contract arteries and veins from several mammalian species. We studied the effect of endothelin-1 on blood vessels removed from turtle (Pseudymes scripta), frog (Rana pipiens), and catfish (Amiurus melas). The vessels were suspended for isometric recording in thermally controlled organ baths and were exposed cumulatively to endothelin-1 (0.5–100 nM). All vessels showed a concentration-dependent increase in isometric force. The half-maximal concentrations (EC50) of endothelin-1 were all in the nanomolar range: turtle left systemic arch (17.9 ± 1.2 nM), frog systemic arch (5.5 ± 1.1 nM), catfish mesenteric artery (6.3 ± 1.3 nM), and catfish posterior cardinal vein (2.5 ± 1.4 nM). Vessels from frog and catfish developed more tension when exposed to 100 nM endomelin-1 than to 80 mM KCl (ET/KCl tension ratio). Our observations that endothelin-1 potently contracts blood vessels from reptiles, amphibians, and fish suggest that endothelin-1 may be a vertebrate peptide mat has been conserved during evolution.Key words: endothelium-derived contracting factor, vascular smooth muscle, vasoactive peptide.

Pharmacological Characterization of Postjunctional α-Adrenoceptors in Human Nasal Mucosa

2005 ◽  
Vol 19 (5) ◽  
pp. 495-502 ◽  
Author(s):  
Michel R. Corboz ◽  
Maria A. Rivelli ◽  
Lori Varty ◽  
Jennifer Mutter ◽  
Mark Cartwright ◽  
...  
Keyword(s):  
Nasal Mucosa ◽  
Isometric Force ◽  
Ringer Solution ◽  
Predominant Role ◽  
Pharmacological Characterization ◽  
Human Nasal Mucosa ◽  
Force Transducers ◽  
Arteries And Veins

Background Functional α1- and α2-adrenoreceptor subtype pharmacology was characterized in an in vitro human nasal mucosa contractile bioassay. Methods Nasal mucosa was obtained from 49 donor patients and mucosal strips were placed in chambers filled with Krebs–Ringer solution and attached to isometric force transducers. Results Nonselective α-adrenoreceptor agonists epinephrine, norepinephrine, and oxymetazoline produced concentration-dependent contractions of isolated human nasal mucosa (pD2= 5.2, 4.9, and 6.5, respectively). The α2-adrenoreceptor agonist BHT-920 (10 μM)–induced contractions were blocked by yohimbine (0.01–1 μM) and prazosin (0.01–1 μM) inhibited the contractile response to the α1-adrenoreceptor agonist phenylephrine (10 μM). Histological analysis showed that phenylephrine and BHT-920 differentially contracted the arteries and veins of human nasal mucosa, respectively. Conclusion Our results indicate that functional α1- and α2-adrenoceptors are present and functional in human nasal mucosa. The a 2-adrenoceptors display a predominant role in contracting the veins and the α1-adrenoceptors appear to preferentially constrict the human nasal arteries.

Heterogeneity in role of endothelium-derived NO in pulmonary arteries and veins of full-term fetal lambs

1995 ◽  
Vol 268 (4) ◽  
pp. H1586-H1592 ◽  
Author(s):  
Y. Gao ◽  
H. Zhou ◽  
J. U. Raj
Keyword(s):  
Nitric Oxide ◽  
Isometric Force ◽  
Pulmonary Veins ◽  
Pulmonary Arteries ◽  
Full Term ◽  
Fourth Generation ◽  
Cyclic Monophosphate ◽  
Arteries And Veins ◽  
Endothelium Dependent Relaxation

Endothelium-derived nitric oxide (EDNO) modulates fetal pulmonary vasoactivity. The role of EDNO in regulation of vasomotor tone in fetal pulmonary arteries vs. that in veins is not known. We have investigated the role of EDNO in the responses of pulmonary arteries and veins of full-term fetal lambs. Fourth-generation pulmonary arterial and venous rings were suspended in organ chambers filled with modified Krebs-Ringer bicarbonate solution (95% O2-5% CO2 at 37 degrees C), and their isometric force was measured. N omega-nitro-L-arginine had no effect on the resting tension of pulmonary arteries with endothelium but caused contraction of pulmonary veins with endothelium. The basal level of intracellular guanosine 3',5'-cyclic monophosphate (cGMP) of pulmonary veins with endothelium was higher than that of arteries with endothelium. In pulmonary arteries, bradykinin, but not acetylcholine, induced endothelium-dependent relaxation and an increase in cGMP content. In pulmonary veins, acetylcholine, but not bradykinin, induced endothelium-dependent relaxation and an increase in cGMP content. Agonist-induced maximal relaxation and increases in cGMP content were smaller in pulmonary arteries than in veins. All these endothelium-dependent responses were abolished by N omega-nitro-L-arginine. In tissues without endothelium, nitric oxide induced significantly less relaxation and less increase in cGMP content in pulmonary arteries than in pulmonary veins. All vessels relaxed similarly to 8-bromoguanosine 3',5'-cyclic monophosphate. Our data suggest that the role of EDNO in modulating tone differs between pulmonary arteries and veins in full-term fetal lambs.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals H2O2 mediates Ca2+- and MLC20phosphorylation-independent contraction in intact and permeabilized vascular muscle

2000 ◽  
Vol 279 (3) ◽  
pp. H1185-H1193 ◽  
Author(s):  
Nancy J. Pelaez ◽  
Tracey R. Braun ◽  
Richard J. Paul ◽  
Richard A. Meiss ◽  
C. Subah Packer
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Kinase Inhibitor ◽  
Isometric Force ◽  
Mesenteric Arteries ◽  
Regulatory Myosin Light Chain ◽  
Pulmonary Arterial ◽  
Dose Dependent ◽  
Arteries And Veins ◽  
Permeabilized Muscle

One purpose of the current study was to establish whether vasoconstriction occurs in all vessel types in response to H2O2. Isometric force was measured in pulmonary venous and arterial rings, and isobaric contractions were measured in mesenteric arteries and veins in response to H2O2. A second purpose was to determine whether H2O2-induced contraction is calcium independent. The addition of H2O2 to calcium-depleted (using the Ca2+ ionophore ionomycin in zero calcium EGTA buffer) muscle caused contraction. Furthermore, permeabilized muscle contracted in response to H2O2 even in zero Ca2+. The final purpose was to determine whether the 20-kDa regulatory myosin light chain (MLC20) phosphorylation plays a role in H2O2-induced contraction. Pulmonary arterial strips were freeze-clamped at various time points during H2O2-induced contractions, and the relative amounts of phosphorylated MLC20 were measured. H2O2 caused dose-dependent contractions that were independent of MLC20 phosphorylation. ML-9, a myosin light chain kinase inhibitor, had no effect on the H2O2 contractile response. In conclusion, H2O2 induces Ca2+- and MLC20 phosphorylation-independent contraction in pulmonary and systemic arterial and venous smooth muscle.

Mechanism of relaxations to C-type natriuretic peptide in veins

1996 ◽  
Vol 271 (5) ◽  
pp. H1907-H1911 ◽  
Author(s):  
M. Banks ◽  
C. M. Wei ◽  
C. H. Kim ◽  
J. C. Burnett ◽  
V. M. Miller
Keyword(s):  
Methylene Blue ◽  
Natriuretic Peptide ◽  
Soluble Guanylate Cyclase ◽  
Isometric Force ◽  
Muscle Membrane ◽  
Channel Blockers ◽  
Response Curves ◽  
Endothelin 1 ◽  
Prostaglandin F2 Alpha ◽  
Smooth Muscle Membrane

C-type natriuretic peptide (CNP) is an endothelium-derived peptide that shares structural homology with atrial natriuretic peptide (ANP). CNP causes greater endothelium-independent relaxations in veins compared with arteries. Relaxations to CNP in porcine coronary arteries are mediated by hyperpolarization of the smooth muscle membrane. Experiments were designed to investigate the mechanism(s) by which CNP causes relaxation in canine femoral veins. Rings of canine femoral veins without endothelium were suspended for measurement of isometric force in organ chambers. Concentration-response curves to CNP were obtained in veins contracted with either endothelin-1 (10(-8) M), KCl (40 mM), phenylephrine (10(-6) M) or prostaglandin F2 alpha (2 x 10(-6) M) in the absence and presence of BQ-123 (10(-6) M), NG-monomenthyl-L-arginine (L-NMMA; 10(-4) M), HS-142-1 (10(-5) M), methylene blue (10(-5) M), or potassium channel blockers, tetraethylammonium chloride (TEA; 10(-3) M), charybdotoxin (10(-7) M), glibenclamide (10(-7) M), or apamin (10(-7) M). Relaxations to CNP were significantly attenuated when the tissue was contracted with KCl and endothelin-1. During contraction to either phenylephrine or prostaglandin F2 alpha, relaxations to CNP were inhibited by HS-142-1, methylene blue, TEA, and charybdotoxin, but not by L-NMMA, glibenclamide, or apamin. In separate experiments, guanosine 3',5'-cyclic monophosphate increased twofold within 10-60 s after the addition of CNP (10(-8) M). These data suggest that CNP mediates relaxation of canine femoral veins through activation of large-conduction, calcium-activated potassium channels and activation of particulate and soluble guanylate cyclase.

Endothelin-1 conversion and receptor characterization in human placental arteries

1994 ◽  
Vol 267 (2) ◽  
pp. E242-E249
Author(s):  
B. M. Wilkes ◽  
C. M. Macica ◽  
P. F. Mento
Keyword(s):  
Blood Vessels ◽  
Competitive Inhibition ◽  
Polyacrylamide Gel Electrophoresis ◽  
Receptor Subtype ◽  
Scatchard Analysis ◽  
Binding Studies ◽  
Single Class ◽  
Endothelin 1 ◽  
Active Peptide ◽  
Receptor Sites

Endothelin-1-(1-21), a potent pressor peptide, is transcribed as big endothelin-(1-38) and converted to active peptide by endothelin-converting enzyme. The current investigation tested the hypothesis that human fetoplacental blood vessels convert big endothelin-1 to active peptide and that fetoplacental blood vessels respond to endothelin-1 by binding of the peptide to specific receptor sites. In the isolated perfused placental cotyledon the addition of big endothelin-1 to the perfusate caused a time-dependent increase in perfusion pressure that corresponded to the appearance of endothelin-1 in the perfusate. The properties of human placental endothelin-1 receptors were defined in binding studies performed on a plasma membrane fraction of small arteries (<1.0 mm) dissected from the placenta. Binding was saturable, reached steady state by 3 h at 25 degrees C, and was linear with protein concentration. Scatchard analysis of binding data indicated a single class of high-affinity binding sites with a dissociation constant of 27.6 +/- 2.3 pM and a density of 856 +/- 119 fmol/mg protein (n = 5). The potency order for competitive inhibition of the binding of 125I-labeled endothelin-1 [endothelin-1 = endothelin-2 > endothelin-3 = sarafotoxin S6b >> big endothelin-1 (human) = big endothelin-1 (porcine)] is most consistent with a type A endothelin receptor subtype. Phenylephrine, bradykinin, norepinephrine, atrial natriuretic factor, diltiazem, U-46619, and angiotensin II did not displace 125I-endothelin-1 binding. Endothelin receptors were shown to have an approximate molecular weight of 36,600 by polyacrylamide gel electrophoresis.(ABSTRACT TRUNCATED AT 250 WORDS)

Localization of Endothelin-1 Binding Sites in Mammalian Blood Vessels Using in vitro Autoradiography

2015 ◽  
pp. 135-142
Author(s):  
R. F. Power ◽  
J. Wharton ◽  
R. A. Rutherford ◽  
M. Ghatei ◽  
S. R. Bloom ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Binding Sites ◽  
Endothelin 1 ◽  
In Vitro Autoradiography ◽  
Mammalian Blood

Human chromostatin inhibits endothelin-1-induced contractures in human blood vessels

1993 ◽  
Vol 47 (1) ◽  
pp. 25-32 ◽  
Author(s):  
S. Aardal ◽  
E. Galindo ◽  
D. Aunis ◽  
K.B. Helle
Keyword(s):  
Blood Vessels ◽  
Human Blood ◽  
Endothelin 1
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