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

Hirata, Yoshihiro; Kimura, Naoki; Sato, Keita; Ohsugi, Yoshiyuki; Takasawa, Shin; Okamoto, Hiroshi; Ishikawa, Jun; Kaisho, Tsuneyasu; Ishihara, Katsuhiko; Hirano, Toshio

doi:10.1016/0014-5793(94)01279-2

Cited by 153 publications

(121 citation statements)

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“…Furthermore, BST-1 shows 30% homology with CD38 and Aplysiu ADP-ribosyl cyclase, which can synthesize cADP-ribose (15,16). In fact, sBST-1 has cyclase activity (18), and cADP-ribose is a second messenger that induces intracellular Ca++ release through the ryanodine receptor independently of the IP,-mediated pathway (19). Therefore, BST-1 is considered to affect cell growth, differentiation, and apoptosis, via Ca++ mobilization.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, deduced amino acid sequences of both human and murine BST-1 showed -30% homology with CD38 and Aplysia ADP-ribosyl cyclase (15,16). Indeed, BST-1 has both ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities (18) which suggests that it affects cell growth, differentiation, and apoptosis by inducing intracellular Ca+ + mobilization, because c ADP-ribose is thought to be a second messenger that acts on the ryanodine receptor (19).…”

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confidence: 99%

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Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Lee

Ishihara

et al. 1996

Arthritis & Rheumatism

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Objective. Bone marrow stromal cell antigen 1 (BST‐1) is a novel glycosyl phosphatidylinositol–anchored ectoenzyme, which is overexpressed on bone marrow stromal and synovial cell lines derived from patients with rheumatoid arthritis (RA). To investigate the pathophysiologic roles of BST‐1 in RA, we established an enzyme‐linked immunosorbent assay (ELISA) system to detect the soluble form of BST‐1 (sBST‐1) and examined levels of sBST‐1 in the sera of RA patients. Methods. Concentrations of sBST‐1 in sera from healthy donors and from patients with RA, osteoarthritis, Sjögren's syndrome, and systemic lupus erythematosus were measured with the ELISA. Results. In 7% of the RA patient samples (10 of 143), concentrations of serum sBST‐1 were higher (∼30–50‐fold) than in non‐RA samples. Serum sBST‐1 concentrations showed no correlation with age, C‐reactive protein level, or rheumatoid factor level. All RA patients with high concentrations of serum sBST‐1 had severe disease with involvement of several large joints. Conclusion. We believe the measurement of serum sBST‐1 may have prognostic value, but further analysis is necessary to clarify the clinical significance of elevated sBST‐1 in RA.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Lee

Ishihara

et al. 1996

Arthritis & Rheumatism

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“…In mammalian cells, the best known ADP-ribosyl cyclases are CD38, a type II transmembrane 48 kDa glycoprotein (10,11) and BST-1, a glycosylphosphatidylinositol-anchored protein (12,13). Both CD38 and BST-1, sharing significant sequence identity, feature two important properties (9).…”

Section: H]nitrobenzylthioinosine (Nbmpr) To Intact Cells and Influxmentioning

confidence: 99%

Concentrative Influx of Functionally Active Cyclic ADP-ribose in Dimethyl Sulfoxide-differentiated HL-60 Cells

Guida

Franco

Bruzzone

et al. 2004

Journal of Biological Chemistry

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“…On the other hand, human BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B cell growth, has recently been reported to have an amino acid sequence similar to CD38 [18]. BST-1 protein expressed in Chinese hamster ovary cells displayed the enzyme activities of ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase in the presence of metal ions such as Zn2+ and Mn2+ [19]. In the present study, we produced the recombinant CD38 fused with a maltose-binding protein (MBP-CD38) in Escherichia coli and investigated the effects of various metal ions on its enzyme properties, together with that of the native membrane-bound CD38 in HL-60 cells.…”

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Stimulation of ADP‐Ribosyl Cyclase Activity of the Cell Surface Antigen CD38 by Zinc Ions Resulting from Inhibition of Its NAD⁺ Glycohydrolase Activity

Kukimoto

Hoshino

Kontani

et al. 1996

European Journal of Biochemistry

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The lymphocyte cell surface antigen, CD38, which has an amino acid sequence similar to Aplysia ADP-ribosyl cyclase, catalyzes not only the hydrolysis of NAD' and l-(S-phospho-P-D-ribosyl)adenosine 5'-phosphate cyclic anhydride (cyclic ADP-ribose) but also the formation of cyclic ADP-ribose from NAD'. To characterize the bifunctional enzyme properties, we produced the recombinant CD38 fused with a maltose-binding protein (MBP-CD38). Zinc ions stimulated the ADP-ribosyl cyclase activity of MBP-CD38, but inversely inhibited its NAD' glycohydrolase activity which was approximately 100-fold dominant to the cyclase activity in the absence of Zn'+. Such dual effects of Zn'+ were also observed in the native membrane-bound CD38 of HL-60 cells which had been caused to differentiate by retinoic acid. Zinc ions inhibited the NAD' glycohydrolase reaction catalyzed by MBP-CD38 in an uncompetitive manner, whereas they enhanced the ADP-ribosyl cyclase reaction without affecting the K,, value for NAD'. There was an increase in the fluorescence intensity of a hydrophobic fluorescent probe, 8-anilino-1 -naphthalenesulfonate, in the presence of MBP-CD38. The fluorescence increase was further enhanced by the addition of Zn2+ with a shift in the maximum emission wavelength from 484nm to 470nm, suggesting that Zn" caused conformational changes of MBP-CD38. These results indicate that Zn2+ directly interacts with CD38 to stimulate its ADP-ribosyl cyclase with inhibition of its NAD' glycohydrolase, probably due to prevention of the access of water molecule to an intermediate of the enzymesubstrate complex.Keywords: CD38 ; cyclic ADP-ribose ; zinc ; NAD' glycohydrolase ; ADP-ribosyl cyclase.The cell-surface antigen, CD38, is a 46-kDa type-I1 singletransmembrane glycoprotein with a short N-terminal cytoplasmic domain and a long C-terminal extracellular domain [I, 21. The expression of CD38 is widely used as a phenotypic marker of the differentiation or activation of T and B lymphocytes [3-51, though its function has not been fully elucidated. We previously reported that an ecto-enzyme activity of NAD' glycohydrolase induced by retinoic acid in HL-60 cells is attributed to the molecule of CD38 [6] and that it has an ability to bind to hyaluronate [7]. Interestingly, CD38 has an amino acid sequence similar to Aplysia ADP-ribosyl cyclase which catalyzes the formation of 1 -(S-phospho-P-D-ribosyl)adenosine 5'-phosphate cyclic anhydride (cyclic ADP-ribose) from NAD' [8 -101 ; there are especially 10 cysteine residues conserved between CD38 and Aplysia ADP-ribosyl cyclase [ll]. Cyclic ADP-ribose has been considered as a new mediator of Ca'+ release from intracellular stores [12, 131.It has been reported that CD38 catalyzes not only the hydrolysis of NAD' but also the formation and hydrolysis of cyclic ADP-ribose [14-161. However, the ADP-ribosyl cyclase activity of CD38 is quite low compared to its NAD' glycohydrolase activity ; the ratio of the two specific activities is approximately 1 : 100 [17]. In this respect, the ADP-ribosyl cyclase acti...

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

Cited by 153 publications

References 27 publications

Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Concentrative Influx of Functionally Active Cyclic ADP-ribose in Dimethyl Sulfoxide-differentiated HL-60 Cells

Stimulation of ADP‐Ribosyl Cyclase Activity of the Cell Surface Antigen CD38 by Zinc Ions Resulting from Inhibition of Its NAD⁺ Glycohydrolase Activity

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

Cited by 153 publications

References 27 publications

Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Elevated levels of the soluble form of bone marrow stromal cell antigen 1 in the sera of patients with severe rheumatoid arthritis

Concentrative Influx of Functionally Active Cyclic ADP-ribose in Dimethyl Sulfoxide-differentiated HL-60 Cells

Stimulation of ADP‐Ribosyl Cyclase Activity of the Cell Surface Antigen CD38 by Zinc Ions Resulting from Inhibition of Its NAD+ Glycohydrolase Activity

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Stimulation of ADP‐Ribosyl Cyclase Activity of the Cell Surface Antigen CD38 by Zinc Ions Resulting from Inhibition of Its NAD⁺ Glycohydrolase Activity