What question did this study set out to answer?

To determine the cellular localization, secretory pathway, and enzymatic substrate specificity of human CD39-L4.

CD39-L4 Is a Secreted Human Apyrase, Specific for the Hydrolysis of Nucleoside Diphosphates

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In vitro study demonstrates that CD39-L4 is a secreted apyrase in human cells, suggesting a regulatory role in platelet aggregation and hemostasis.

To determine the cellular localization, secretory pathway, and enzymatic substrate specificity of human CD39-L4.
Transfected COS-7 cells with a CD39-L4 construct harboring its native leader peptide and evaluated extracellular protein release with or without brefeldin A treatment.
Assessed CD39-L4 mRNA expression in human macrophages and characterized its enzymatic dependence on divalent cations and selectivity for nucleoside substrates.
CD39-L4 is released extracellularly via standard mammalian secretory pathways, with secretion completely inhibited by brefeldin A.
CD39-L4 message is expressed in macrophages, indicating that the protein circulates in human blood.
The enzyme functions as a calcium- and magnesium-dependent E-type apyrase displaying high substrate specificity for nucleoside diphosphates over nucleoside triphosphates.

Mulero et al. (1999) studied this question.

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In vitro study demonstrates that CD39-L4 is a secreted apyrase in human cells, suggesting a regulatory role in platelet aggregation and hemostasis.