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Modulation of endothelial cell functions by different molecular species of
interleukin 1
E Dejana, F Breviario, A Erroi, F Bussolino, L Mussoni, M Gramse, G Pintucci, B Casali, CA Dinarello and J Van Damme
Different molecular species of interleukin 1 (IL 1) were examined for the
spectrum of responses elicited in human endothelial cells (HEC), including
synthesis of prostacyclin (PGI2), tissue-type procoagulant activity (PCA),
platelet activating factor (PAF), and plasminogen activator inhibitor
(PA-I). The IL 1 preparations utilized for the present study included a
natural, partially purified IL 1, a preparation purified to homogeneity
with extensive homology with the derived aminoacid IL 1 beta (pI7) sequence
denominated "22K factor," murine recombinant IL 1 alpha, human recombinant
IL 1 alpha (pI5) and beta (pI7). Natural, partially purified IL 1, a
mixture of alpha and beta species, induced the entire spectrum of responses
in HEC. Production of PA-I was elicited by all forms of IL 1 tested. PGI2
and PCA were elicited by "22K factor" and by human recombinant IL 1 beta
and alpha but not by murine recombinant IL 1 alpha. PAF synthesis was
stimulated by murine and human recombinant IL 1 alpha but not by human
recombinant IL 1 beta and 22K factor. Thus the available different
molecular forms of IL 1 elicit largely but not completely overlapping
patterns of responses in HEC. The IL 1 pathway of regulation of HEC
functions might provide a basis for novel strategies in therapeutically
oriented research on vessel wall disorders.
Volume 69,
Issue 2,
pp. 695-699,
02/01/1987
Copyright © 1987 by The American Society of Hematology
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