Human BST-1, a bone marrow stromal cell surface molecule, is a
GPI-anchored protein that facilitates the growth of pre-B cells. The
deduced amino acid sequences of human and mouse BST-1 show around 30%
homology with those of CD38 and Aplysia ADP ribosyl cyclase.
Therefore, like CD38, BST-1 might possess ADP ribosyl cyclase
activity. Here, we report the establishment of a stable transformant
CHO cell line, which secretes truncated human soluble BST-1, and show
that purified soluble BST-1 displays both ADP ribosyl cyclase and
cADPR hydrolase activities.
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