Document Detail


Big ET-1 processing into vasoactive peptides in arteries and veins.
MedLine Citation:
PMID:  17904426     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The endothelin (ET) peptides are more potent in contracting veins than arteries. The precursor big ET-1 is metabolized by endothelin converting enzyme [ECE; to ET-1 (1-21)], matrix metalloproteases [MMPs; to ET-1 (1-32)] and chymase [to ET-1(1-31)]. We hypothesized that arteries and veins were differently dependent in conversion of big ET-1 to vasoconstrictors. Immunohistochemical, western, zymographic and isometric contractile assays in rat aorta and vena cava were used. Big ET-1 contracted aorta [60+/-17% phenylephrine contraction] but was more efficacious in vena cava [478+/-61% norepinephrine contraction]. ECE and its product ET-1(1-21) were detected in aorta and vena cava, and the ECE inhibitors phosphoramidon and CGS-26393 reduced big ET-1-induced contraction. ET-1 (1-32) contracted aorta and vena cava but inhibition of MMPs with minocycline or GM6001 did not reduce big ET-1-induced contraction; zymography confirmed active tissue MMPs. Aorta and vena cava contracted to the product of chymase, ET-1 (1-31). Chymase was detected in aorta and only weakly in vena cava. Inhibition of chymase (chymostatin, 100 muM) reduced arterial (19% control) but not venous constriction to big ET-1. These results suggest at least one potential significant difference - the role of chymase - in in vitro enzymatic processing of big ET-1 in arteries and veins.
Authors:
Stephanie W Watts; Keshari Thakali; Chuck Smark; Catherine Rondelli; Gregory D Fink
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, N.I.H., Extramural     Date:  2007-09-07
Journal Detail:
Title:  Vascular pharmacology     Volume:  47     ISSN:  1537-1891     ISO Abbreviation:  Vascul. Pharmacol.     Publication Date:    2007 Nov-Dec
Date Detail:
Created Date:  2007-11-05     Completed Date:  2008-08-21     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  101130615     Medline TA:  Vascul Pharmacol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  302-12     Citation Subset:  IM    
Affiliation:
Department of Pharmacology and Toxicology, Michigan State University, East Lansing, MI 48824-1317, USA. wattss@msu.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Aorta, Thoracic / drug effects,  physiology*
Aspartic Acid Endopeptidases / antagonists & inhibitors
Chymases / antagonists & inhibitors,  metabolism
Dipeptides / pharmacology
Endothelin-1 / analogs & derivatives,  metabolism*,  pharmacology
Glycopeptides / pharmacology
Isometric Contraction
Male
Matrix Metalloproteinases / metabolism
Metalloendopeptidases / antagonists & inhibitors
Minocycline / pharmacology
Muscle, Smooth, Vascular / drug effects,  physiology
Organophosphonates / pharmacology
Peptide Fragments / metabolism*,  pharmacology
Protease Inhibitors / pharmacology
Rats
Rats, Sprague-Dawley
Tetrazoles / pharmacology
Vena Cava, Inferior / drug effects,  physiology*
Grant Support
ID/Acronym/Agency:
P01 HL070687-020004/HL/NHLBI NIH HHS; P01 HL70687/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Dipeptides; 0/Endothelin-1; 0/Glycopeptides; 0/N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide; 0/Organophosphonates; 0/Peptide Fragments; 0/Protease Inhibitors; 0/Tetrazoles; 0/endothelin-1 (1-21); 0/endothelin-1 (1-31); 10118-90-8/Minocycline; 154116-34-4/CGS 26393; 36357-77-4/phosphoramidon; EC 3.4.21.39/Chymases; EC 3.4.23.-/Aspartic Acid Endopeptidases; EC 3.4.24.-/Matrix Metalloproteinases; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.71/endothelin-converting enzyme
Comments/Corrections

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