Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38

Howard, Maureen; Grimaldi, J. Christopher; Bazán, J. Fernando; Lund, Frances E.; Santos‐Argumedo, Leopoldo; Parkhouse, R. M. E.; Walseth, Timothy F.; Lee, Hon Cheung

doi:10.1126/science.8235624

Cited by 726 publications

(555 citation statements)

References 24 publications

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“…Neither cADPR influx across the plasma membrane nor cADPR-initiated signal transduction in responsive cells has been demonstrated so far, although external cADPR has been reported to enhance the proliferation of activated murine B lymphocytes [4]. In addition, extracellular cADPR has been recently demonstrated to enhance the calcium response to depolarization in intact rat cerebellar granule cells [15].…”

Section: *Corresponding Author Fax: (39) (10) 354415mentioning

confidence: 99%

“…CD38 is also a bifunctional ectoenzyme that catalyzes, at the outer surface of many cell types [3], the sequential synthesis and degradation of cyclic ADP-ribose (cADPR) [4][5][6][7][8]: the two enzyme activities involved are an ADP-ribosyl cyclase (responsible for the conversion of NAD + to nicotinamide and cADPR) and a cADPR hydrolase that degrades cADPR to ADP-ribose (ADPR).…”

Section: Introductionmentioning

confidence: 99%

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NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

Zocchi¹,

Franco²,

Guida³

et al. 1996

FEBS Letters

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CD38 is a transmembrane glycoprotein involved as an orphan receptor in many physiological processes of lymphocytes. It is also a bifunctional enzyme that catalyzes at its ectocellular domain the synthesis from NAD + (cyclase) and the hydrolysis (hydrolase) of the calcium-mobilizing metabolite cyclic ADPribose (cADPR). A still unexplained paradox concerns the relationship between ectocellular localization of CD38 and intracellular calcium-releasing activity of its intermediate product cADPR. Incubation of CD38 + human Namalwa B cells with external NAD + elicited extensive membrane down-regulation of CD38 and its internalization in non-clathrin-coated vesicles. Since the internalized CD38 was demonstrated to be enzymatically active, this NAD+-dependent process is a hitherto unrecognized means for shifting cADPR metabolism from the cell surface to the intracellular environment.

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Section: *Corresponding Author Fax: (39) (10) 354415mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

Zocchi¹,

Franco²,

Guida³

et al. 1996

FEBS Letters

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“…Formal proof of the enzymatic activity of CD38 was first obtained by M. Howard et al using purified recombinant murine CD38 [56] and their findings were extended to human CD38 by various laboratories [57]. In both species, CD38 is a complex enzyme because it can convert (1) NAD ϩ directly to ADPR (glycohydrolase activity), (2) NAD ϩ to cADPR (cyclase activity), and (3) cADPR to ADPR (hydrolase activity), at least in the test tube.…”

Section: The Enzymatic Activity Of Cd38mentioning

confidence: 99%

The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38

Ferrero

Malavasi

1999

Journal of Leukocyte Biology

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Human CD38 is a 45-kDa type II membrane glycoprotein with an intricate pattern of expression in leukocytes, although evidence is accumulating of its quite widespread expression in cells of nonvascular origin. CD38 is a member of a nascent eukaryotic gene family encoding cytosolic and membrane-bound enzymes whose substrate is NAD, a coenzyme ubiquitously distributed in nature. Functionally, CD38 is an eclectic molecule with the ability not only to catalyze but also to signal, to mobilize calcium, and to adhere to itself, to hyaluronan, and to other ligands. Interaction with CD38 on various leukocyte subpopulations has profound though diverse consequences on their life-span, but these effects seem to be independent of the enzymatic activity of the molecule. CD38 challenges our expectations of a surface molecule and we must sift through its many guises to unmask its true nature. J. Leukoc. Biol. 65: 151-161; 1999.

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“…CD38 is an ectoenzyme that possesses both ADP ribosyl cyclase and cADP ribosyl hydrolase activities, which generate cADP ribose and ADP ribose from NAD ϩ (1)(2)(3)(4). A role for CD38 in regulation of B cell activation has been suggested by analysis using agonistic mAb to mouse CD38 (5)(6)(7)(8)(9).…”

mentioning

confidence: 99%

A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5

Yasue

Nishizumi

Aizawa

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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CD38 is an ectoenzyme that possesses both ADP ribosyl cyclase and cADP ribosyl hydrolase activities, which generate cADP ribose and ADP ribose from NAD ϩ (1-4). A role for CD38 in regulation of B cell activation has been suggested by analysis using agonistic mAb to mouse CD38 (5-9). We have reported that CD38 ligation on B cells by anti-mouse CD38 mAb induced proliferation, IgM secretion, and tyrosine phosphorylation of Bruton tyrosine kinase (Btk) in B cells from wild-type mice. B cells from X chromosome-linked immunodeficient (Xid) mice did not respond at all to anti-CD38 mAb although CD38 expression on these B cells was comparable to that on wild-type B cells (8, 9). We infer from these results that Btk activity is involved in B cell triggering after cross-linkage of CD38.Interleukin 5 (IL-5) induces proliferation and differentiation of B cells, eosinophils, and basophils (10, 11). IL-5 signals through the IL-5 receptor (IL-5R) complex, which is comprised of an ␣ chain (IL-5R␣) and a ␤ chain (12-18). Analysis of the synergistic effects of various cytokines with CD38 ligation of B cell activation revealed that IL-5 showed the most potent effect on B cell proliferation, Blimp-1 gene expression, and IgM production (9). Although neither CD38 nor IL-5R carries the catalytic domain for protein tyrosine kinases, CD38 ligation induces activation of Btk (9) Lyn and Fyn are expressed in a broad range of cell types and tissues (27). Lyn has been shown to be physically associated with a number of hematopoietic cell surface receptors, including the B cell antigen receptor (28-30), CD40 (31), the lipopolysaccharide (LPS) receptor (32), the high affinity Fc RI complex (33), the granulocyte-macrophage colonystimulating factor receptor (34), and IL-5R (11, 35). Furthermore, Lyn and Fyn were shown to be associated with Btk (36). Lyn is most likely the predominant src family kinase involved in activation of Btk in B cells (37). It is not clear, however, whether Fyn and Lyn are involved in the signaling cascade of CD38 ligation. In this study, using fyn-deficient (Fyn Ϫ͞Ϫ ), lyn-deficient (Lyn Ϫ͞Ϫ ), and fyn͞lyn double-deficient (Fyn͞ Lyn Ϫ͞Ϫ ) mice, we have examined the role of Fyn and Lyn in signaling through CD38 ligation and in the synergistic effect of CD38 ligation and IL-5 on B cell triggering. We describe that CD38 ligation and IL-5 induce IgG1 secretion, which is impaired in B cells from Lyn Ϫ͞Ϫ and Fyn͞Lyn Ϫ͞Ϫ mice.

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Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38

Cited by 726 publications

References 24 publications

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38

A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5

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Formation and Hydrolysis of Cyclic ADP-Ribose Catalyzed by Lymphocyte Antigen CD38

Cited by 726 publications

References 24 publications

NAD+‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD+‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38

A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5

Contact Info

Product

Resources

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NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells

NAD⁺‐dependent internalization of the transmembrane glycoprotein CD38 in human Namalwa B cells