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Contribution of the Actin Cytoskeleton to the Viscoelastic Characteristics of Inwardly Remodeled Arterioles
Author(s) -
CastorenaGonzalez Jorge Augusto,
Staiculescu Marius Catalin,
Zhao Guiling,
MartinezLemus Luis A.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.902.4
Subject(s) - vasoconstriction , dithiothreitol , chemistry , arteriole , actin , cytoskeleton , filamin , biophysics , actin cytoskeleton , microbiology and biotechnology , medicine , endocrinology , biochemistry , microcirculation , biology , enzyme , cell
In hypertension, one of the most important structural changes in the vasculature is the inward remodeling of arterioles, which is characterized by a reduction in passive luminal diameter. In arterioles, prolonged exposure to vasoconstrictor agonists or the reducing agent Dithiothreitol (DTT) induces inward remodeling. Therefore, we hypothesized that DTT induces inward remodeling via prolonged vasoconstriction and remodeling of the actin cytoskeleton. In rat cremaster isolated arterioles, acute exposure to DTT induced a concentration‐dependent constriction. A 4‐hour exposure to 200μM DTT caused prolonged vasoconstriction and induced an 11±4% reduction in passive diameter, with an increase in media‐to‐lumen ratio from 0.14±0.01 to 0.20±0.02. All this was inhibited in the presence of Cytochalasin‐D (500nM). Passive pressure‐diameter curves were obtained for control and remodeled arterioles before and after a 1‐hour incubation with the actin depolymerization agent Mycalolide‐B (2μM). The elasticity of control arterioles was not affected by Mycalolide‐B, but was increased by 21% in remodeled arterioles. These results indicate that DTT induces inward remodeling via prolonged vasoconstriction and that the change in viscoelastic characteristics of inwardly remodeled arterioles, namely increased stiffness, is partially dependent on the F‐actin components of the cytoskeleton. NIH HL‐088105 to LAM