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Department of Physiology, University of Missouri School of Medicine, Columbia, Missouri 65212
Whereas the glycocalyx of endothelial cells has been
shown to influence solute flux from capillary microvessels, little is known about its contribution to the movement of macromolecules across
the walls of other microvessels. We evaluated the hypothesis that a
glycocalyx contributes resistance to protein flux measured in coronary
arterioles. Apparent solute permeability (Ps) to
two proteins of different size and similar charge, 
-lactalbumin
(-lactalb) and porcine serum albumin (PSA), was determined in
arterioles isolated from the hearts of 43 female Yucatan miniature
swine. Ps was assessed in arterioles with an
"intact" glycocalyx under control conditions and again after
suffusion with adenosine (Ado, 10
5 M,
n = 42 arterioles, N = 29 pigs). In a second set of
experiments (n = 21 arterioles, N = 21 pigs) arteriolar
Ps was determined before and after perfusion with
enzyme (pronase or heparinase), which was used to digest the
glycocalyx. Ps was assessed a third time on those
microvessels after exposure to Ado. Consistent with the hypothesis,
Ps for PSA
(PPSAs) and Ps for -lactalb
(P
-lactalbs) increased from basal levels following enzyme treatment. Subsequent suffusion with
Ado, a significant metabolite known to alter coronary vascular smooth
muscle tone and permeability, resulted in a significant reduction of
basal P-lactalbs in both untreated and enzyme-treated arterioles. Furthermore, in untreated arterioles, PPSAs was unchanged by
Ado suffusion, whereas Ado induced a pronounced reduction in
PPSAs of enzyme-treated vessels.
These data demonstrate that in intact coronary arterioles an
enzyme-sensitive layer, most likely at the endothelial cell surface,
contributes significantly to net barrier resistance to solute flux.
porcine serum albumin; -lactalbumin; microspectrofluorometry; microcirculation; endothelium; Yucatan miniature swine; protease; heparinase
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