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Blood, Vol. 96 No. 2 (July 15), 2000:
pp. 732-739
Molecular cloning and characterization of a human metalloprotease
disintegrin a novel marker for dendritic cell
differentiation
Jana Fritsche,
Markus Moser,
Stefan Faust,
Alice Peuker,
Reinhard Büttner,
Reinhard Andreesen, and
Marina Kreutz
From the Department of Hematology/Oncology and the Institute of
Pathology, University of Regensburg, Regensburg, Germany.
The 1 ,25-dihydroxyvitamin D3
(1,25- [OH]2VD3) modulates the
differentiation of monocytic cell lines and monocytes (MOs) in vitro.
Up to now several target genes of 1,25(OH)2VD3
have been described in monocytic cell lines; however, little is known
about target genes in primary MOs. With the Differential Display
technique, we found a transcript up-regulated by
1,25(OH)2VD3 in short-term cultured human blood
MOs, which we called MADDAM (metalloprotease and disintegrin dendritic
antigen marker; EMBL/GenBank/DDBJ accession no. Y13786). Northern blot
analysis confirmed this result and revealed a signal of MADDAM
messenger RNA (mRNA) at about 7.5 kilobases (kb). Long-term culture
(more than 20 hours) of MOs during macrophage (MAC) differentiation led
to a rapid and complete down-regulation of MADDAM
expression. In contrast, MADDAM expression was maintained in MOs
differentiated along the dendritic cell (DC) pathway and induced in
CD34+-derived DCs. In addition, in situ hybridization
revealed signals of MADDAM mRNA in follicles of human lymph nodes and
MADDAM mRNA was detected in freshly isolated human blood-DCs by reverse
transcription-polymerase chain reaction (RT-PCR). By means of a
database search, we found that MADDAM is a member of the ADAM (a
metalloprotease and disintegrin) family, the human homologue to murine
meltrin- (ADAM 19). From these data, we conclude that MADDAM is an
important marker for the differentiation and characterization of DCs
and the distinction between MACs and DCs.
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