ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST‐1

Yuichi Hirata(Mochida Pharmaceutical (Japan)), Naoki Kimura, Koh Sato, Yoshiyuki Ohsugi, Shin Takasawa(Tohoku University), Hiroshi Okamoto(Tohoku University), Jun Ishikawa(The University of Osaka), Tsuneyasu Kaisho(The University of Osaka), Katsuhiko Ishihara(The University of Osaka), Toshio Hirano(The University of Osaka)
FEBS Letters
December 19, 1994
Cited by 169Open Access
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Abstract

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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