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Vol. 295, Issue 2, 484-491, November 2000
Vascular Biology Laboratory, Dalton Cardiovascular Research Center,
and Department of Physiology, School of Medicine, University of
Missouri, Columbia, Missouri (B.J.F.H., B.R.W., M.S.); and Department
of Physiology, School of Medicine, East Carolina University,
Greenville, North Carolina (L.C.K.)
Arterial injury models for coronary artery disease have demonstrated an
enhanced expression and function of either the endothelinA or endothelinB (ETA or ETB)
receptor subtype. We hypothesized that organ culture would enhance the
physiological function of ET receptors in the porcine right coronary
artery. Arteries were either cold stored (4°C) or organ cultured
(37°C) for 4 days. After 4 days, the artery was either 1) sectioned
into rings to measure the ET-1-induced isometric tension response
(3 × 10
10-3 × 107 M), or 2)
enzymatically dispersed and the isolated smooth muscle cells imaged
using fura-2 to measure the myoplasmic calcium (Cam) response to 3 × 108 M ET-1 (~EC50).
Isometric tension and Cam to ET-1 were measured in the
absence and presence of bosentan (nonselective ETA or
ETB receptor antagonist), BQ788 (ETB-selective
antagonist), and BQ123 (ETA-selective antagonist). Compared
with cold storage, organ culture induced a 2-fold increase in tension
development (3 × 107 M ET-1) and Cam
(3 × 108 M ET-1), which was inhibited with
bosentan, thus confirming the enhanced responses to ET-1 were due to ET
receptor activation. BQ123 also inhibited the enhanced contraction and
Cam responses to ET-1. In contrast, BQ788 failed to inhibit
tension development and Cam responses to ET-1 in organ
culture and cold storage. Sarafotoxin 6C (ETB agonist)
failed to elicit an increased Cam response in organ culture
compared with cold storage. Our results indicate the increased tension
development and Cam responses to ET-1 in organ culture are
attributable to ETA receptors, and not ETB receptors.
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