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Blood, Vol. 95 No. 4 (February 15), 2000:
pp. 1350-1355
Circulating forms of intercellular adhesion molecule (ICAM)-1
in mice lacking membranous ICAM-1
Natasja K. van den Engel,
Edmund Heidenthal,
Antje Vinke,
Hubert Kolb, and
Stephan Martin
From the Clinical Department, Diabetes Research Institute at the
Heinrich Heine University, Düsseldorf, Germany
Mice deficient in intercellular adhesion molecule-1 (ICAM-1),
lacking membranous ICAM-1, show a normal development but abnormalities of inflammatory and immune functions. Although the membrane-bound form
of ICAM-1 is not detectable in the mutant strain, circulating ICAM-1
(cICAM) is present in serum from ICAM-1-deficient mice in similar
amounts as in serum from wild-type mice. These findings were confirmed
in vitro by flow cytometric analysis of lipopolysaccharide-stimulated spleen cells, and cICAM-enzyme-linked immunosorbent assay analysis of
supernatants of cultured spleen cells. To analyze for the source of
cICAM-1, spleen cell RNA was isolated and ICAM-1 RNA was amplified by
reverse transcriptase-polymerase chain reaction using primers binding
in the 5' and 3' untranslated regions. Different fragments were cloned and sequenced. In wild-type RNA the common 5 domain form of
ICAM-1 was identified. In RNA from ICAM-1 mutant mice only 3 smaller
fragments were found. Sequencing these fragments identified 3 alternatively spliced isoforms of ICAM-1, lacking 2 or 3 extracellular
domains. However, in all spliced fragments the transmembrane domain was
included. Therefore, we postulate that circulating forms of ICAM-1 are
generated by proteolytic cleavage of membranous ICAM-1. The data
indicate that the expression of membranous ICAM-1 and the appearance of
circulating forms in serum are independently regulated mechanisms.
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