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    Biochem Biophys Res Commun. 1996 Nov 21;228(3):838-45.

    Human BST-1 expressed on myeloid cells functions as a receptor molecule.

    Okuyama Y, Ishihara K, Kimura N, Hirata Y, Sato K, Itoh M, Ok LB, Hirano T.

    Department of Molecular Oncology, Osaka University Medical School, Japan.

    We have previously identified and cloned BST-1 as a molecule which is overexpressed on the bone marrow stromal cell lines derived from patients with rheumatoid arthritis and which has the ability to support the pre-B cell growth. BST-1 is a glycosylphosphatidylinositol-anchored ectoenzyme having ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities. In this report, we demonstrate that human BST-1 was expressed on monocytes, granulocytes in the peripheral blood of healthy donors, and macrophages matured in vitro. Cross-linking of BST-1 with a polyclonal anti-BST-1 antibody induced tyrosine phosphorylation of a 130-kDa protein (p130) in the human myeloid cell lines U937 and THP-1. Cross-linking of BST-1 overexpressed on a transfectant induced tyrosine phosphorylation of p130, dephosphorylation of the 100-kDa protein, and growth inhibition. These results suggest that BST-1 can deliver signals into cells and function as a receptor.

    PMID: 8941363 [PubMed - indexed for MEDLINE]

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