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

Yuichi Hirata, Naoki Kimura, Koh Sato, Yoshiyuki Ohsugi, Shin Takasawa, Hiroshi Okamoto, Jun Ishikawa, Tsuneyasu Kaisho, Katsuhiko Ishihara, Toshio Hirano

Research output: Contribution to journalArticle

142 Citations (Scopus)

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 cADPR hydrolase activities.

Original languageEnglish
Pages (from-to)244-248
Number of pages5
JournalFEBS Letters
Volume356
Issue number2-3
DOIs
Publication statusPublished - 1994 Dec 19

Keywords

  • ADP ribosyl cyclase
  • BST-1
  • CD38
  • cADPR hydrolase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Hirata, Y., Kimura, N., Sato, K., Ohsugi, Y., Takasawa, S., Okamoto, H., Ishikawa, J., Kaisho, T., Ishihara, K., & Hirano, T. (1994). ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST-1. FEBS Letters, 356(2-3), 244-248. https://doi.org/10.1016/0014-5793(94)01279-2