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Human endothelial cells synthesize, process, and secrete fibronectin
molecules bearing an alternatively spliced type III homology (ED1)
JH Peters, LA Sporn, MH Ginsberg and DD Wagner
Department of Immunology, Research Institute of Scripps Clinic, La Jolla.
Cellular fibronectin (Fn) bearing an alternatively spliced extra type III
structural repeat (ED1) is normally present at low concentrations in blood
plasma. The source of this material remains uncertain. In this study,
primary cultures of human umbilical vein endothelial cells (HUVEC) labeled
with 35S-methionine were observed to synthesize Fn monomers both with and
without this segment. Monomers isolated from cell lysates with antibodies
to the ED1 sequence comigrated in nonreduced sodium dodecyl sulfate
polyacrylamide gel electrophoresis with the slower (designated M1), but not
the faster (designated M2), of two major monomeric populations that were
recognized by antibodies raised to plasma-derived Fn. The differences
between M1 and M2 were not due to glycosylation, since they were also
observed between species of Fn monomer purified from cells grown in the
presence of tunicamycin. M1 and M2 were both observed to incorporate with a
similar rate into dimeric Fn, indicating that Fn monomers with and without
the ED1 site can dimerize with similar efficiency. Analysis of reduced
samples of Fn isolated from cells with anti-ED1 antibodies indicated the
presence of both M1-M1 and M1-M2 dimers. In addition to being incorporated
into extracellular matrix, ED1 + Fn was observed to be secreted in soluble
form into the medium, potentially reflecting intravascular release of this
protein by endothelial cells in vivo.
Volume 75,
Issue 9,
pp. 1801-1808,
05/01/1990
Copyright © 1990 by The American Society of Hematology
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