Monocyte adhesion to subendothelial components
JW Tobias, MM Bern, PA Netland and BR Zetter
Human monocytes have been shown to penetrate the endothelial layer of large
blood vessels and to adhere to the subendothelial basement membrane. To
determine the active components of this process, we have studied the
ability of monocytes to adhere to isolated components of the subendothelial
matrix. Using a quantitative dot-blot adhesion assay, we find that
monocytes adhere preferentially to immobilized laminin and elastin. The
monocytes adhere less well to fibronectin and bind poorly or not at all to
collagen types I and IV, or to heparan sulfate. Monocyte binding to elastin
requires an intact, crosslinked molecule as no binding was observed to
soluble, acid-alcohol elastin extracts, to pepsin or elastase digests of
elastin, to tropoelastin monomer, or to desmosine/isodesmosine crosslinks.
Similar binding profiles to elastin, laminin, and fibronectin were seen
with the established human leukocyte cell line U937. The promyelocytic cell
line HL60 adhered equally well to laminin but showed slightly reduced
adhesion to elastin when compared with the fresh monocytes or U937 cells.
Freshly isolated human erythrocytes did not demonstrate significant
adhesion to fibronectin, laminin, or elastin.
Volume 69,
Issue 4,
pp. 1265-1268,
04/01/1987
Copyright © 1987 by The American Society of Hematology
