Human and bovine endothelial cell monolayers are differentially activated for neutrophil transmigration by human plasma.
Endothelial cells used in transendothelial migration assays have been derived from different sources including human umbilical vein and bovine pulmonary artery. As plasma-induced activation of endothelial cells for enhanced transmigration of leukocytes may be pathophysiologically relevant, the role of species differences between plasma and endothelial cells was studied. The effects of human plasma on human umbilical vein and bovine pulmonary artery endothelial cells with regard to transmigration of neutrophils were compared. Transendothelial migration of neutrophils was tested employing endothelial cell-covered Transwell cell culture chamber inserts with micropore filters of 5 microns pore size. Results showed that human plasma induces neutrophil transmigration of both human umbilical vein and bovine pulmonary artery endothelial cell monolayers. Plasma samples from 50 to 69 year old men with and without carotid arteriosclerosis (N = 152) stimulated endothelial cells of human origin significantly stronger for transmigration of neutrophils than endothelial cells of bovine origin. Analyses of limits of agreement and of correlation of the two methods indicated that bovine pulmonary artery and human umbilical vein endothelial cells cannot replace each other in assays of plasma-induced activation of transmigration. Plasma levels of soluble adhesion molecule P-selectin, which are elevated in patients with arteriosclerotic diseases, are inversely related to plasma-induced activation of neutrophil transmigration of endothelial monolayers of human origin but not of bovine origin (N = 65). As rates of transmigration that were induced by plasma from subjects without carotid arteriosclerosis (N = 73) were significantly related between human and bovine endothelium, elevated plasma levels of soluble P-selectin may thus affect results of assays for plasma-induced activation of neutrophil transmigration of endothelial monolayers in a species-specific manner.
Department of Internal Medicine, University of Innsbruck, Austria.
C J
CJ
Wiedermann
P
P
Schratzberger
S
S
Dunzendorfer
S
S
Kiechl
N
N
Reinisch
C M
CM
Kähler
J
J
Willeit
D000328:Adult; D000368:Aged; D000818:Animals; D016632:Apolipoprotein A-I / Q000097:blood; D001055:Apolipoproteins B / Q000097:blood; D002417:Cattle; D002463:Cell Membrane Permeability; D002478:Cells, Cultured; D002634:Chemotaxis, Leukocyte; D019040:E-Selectin / Q000097:blood; D004730:Endothelium, Vascular / Q000166:cytology / Q000502:physiology*; D005260:Female; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000097:blood; D008075:Lipoproteins, HDL / Q000097:blood; D008297:Male; D008875:Middle Aged; D009504:Neutrophils / Q000502:physiology*; D019007:P-Selectin / Q000097:blood; D010949:Plasma / Q000502:physiology*; D011651:Pulmonary Artery; D011994:Recombinant Proteins / Q000494:pharmacology; D012044:Regression Analysis; D013045:Species Specificity; D014280:Triglycerides / Q000097:blood; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology; D014471:Umbilical Veins; D019010:Vascular Cell Adhesion Molecule-1 / Q000097:blood
D016632:Apolipoprotein A-I; D001055:Apolipoproteins B; D019040:E-Selectin; D008075:Lipoproteins, HDL; D019007:P-Selectin; D011994:Recombinant Proteins; D014280:Triglycerides; D014409:Tumor Necrosis Factor-alpha; D019010:Vascular Cell Adhesion Molecule-1; D018799:Intercellular Adhesion Molecule-1