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J Biol Chem, Vol. 274, Issue 29, 20064-20067, July 16, 1999
From the Functional Genomics Department, Hyseq Inc.,
Sunnyvale, California 94086
The human ecto-apyrase gene family consists of
five reported members (CD39, CD39-L1,
CD39-L2, CD39-L3, and CD39-L4). The
family can be subdivided into two groups by conservation of proposed structural domains. The CD39, CD39-L1, and
CD39-L3 genes all encode hydrophobic portions in their
carboxy and amino termini, serving as transmembrane domains for CD39
and potentially for the other two members. CD39-L2 and
CD39-L4 genes encode hydrophobic portions in their amino
termini, suggesting that they might encode secreted apyrases. We
demonstrate that the CD39-L4 gene encodes the first reported human secreted ecto-apyrase. COS-7 cells transfected with a
CD39-L4 expression construct utilizing the naturally occurring leader
peptide express recombinant protein outside of the cells. This
expression can be blocked by brefeldin A, a chemical that inhibits a
step in mammalian secretory pathways. We also demonstrate expression of
CD39-L4 message in macrophages, suggesting that the protein is present
in the circulation. Furthermore, we show that CD39-L4 is an E-type
apyrase, is dependent on calcium and magnesium cations, and has high
degree of specificity for NDPs over NTPs as enzymatic substrates. A
potential physiological role in hemostasis and platelet aggregation is presented.
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