Role of a glycocalyx on coronary arteriole permeability to proteins: evidence from enzyme treatments
- 1 April 2000
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Heart and Circulatory Physiology
- Vol. 278 (4) , H1177-H1185
- https://doi.org/10.1152/ajpheart.2000.278.4.h1177
Abstract
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, α-lactalbumin (α-lactalb) and porcine serum albumin (PSA), was determined in arterioles isolated from the hearts of 43 female Yucatan miniature swine. Pswas assessed in arterioles with an “intact” glycocalyx under control conditions and again after suffusion with adenosine (Ado, 10−5M, n = 42 arterioles, N = 29 pigs). In a second set of experiments ( n = 21 arterioles, N = 21 pigs) arteriolar Pswas determined before and after perfusion with enzyme (pronase or heparinase), which was used to digest the glycocalyx. Pswas assessed a third time on those microvessels after exposure to Ado. Consistent with the hypothesis, Psfor PSA ([Formula: see text]) and Psfor α-lactalb ([Formula: see text]) 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 [Formula: see text] in both untreated and enzyme-treated arterioles. Furthermore, in untreated arterioles, [Formula: see text] was unchanged by Ado suffusion, whereas Ado induced a pronounced reduction in[Formula: see text] 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.Keywords
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