{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T23:45:49Z","timestamp":1783208749990,"version":"3.54.6"},"reference-count":55,"publisher":"Rockefeller University Press","issue":"5","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1999,9,6]]},"abstract":"<jats:p>The multifunctional ADP-ribosyl cyclase, CD38, catalyzes the cyclization of NAD+ to cyclic ADP-ribose (cADPr). The latter gates Ca2+ release through microsomal membrane-resident ryanodine receptors (RyRs). We first cloned and sequenced full-length CD38 cDNA from a rabbit osteoclast cDNA library. The predicted amino acid sequence displayed 59, 59, and 50% similarity, respectively, to the mouse, rat, and human CD38. In situ RT-PCR revealed intense cytoplasmic staining of osteoclasts, confirming CD38 mRNA expression. Both confocal microscopy and Western blotting confirmed the plasma membrane localization of the CD38 protein. The ADP-ribosyl cyclase activity of osteoclastic CD38 was next demonstrated by its ability to cyclize the NAD+ surrogate, NGD+, to its fluorescent derivative cGDP-ribose. We then examined the effects of CD38 on osteoclast function. CD38 activation by an agonist antibody (A10) in the presence of substrate (NAD+) triggered a cytosolic Ca2+ signal. Both ryanodine receptor modulators, ryanodine, and caffeine, markedly attenuated this cytosolic Ca2+ change. Furthermore, the anti-CD38 agonist antibody expectedly inhibited bone resorption in the pit assay and elevated interleukin-6 (IL-6) secretion. IL-6, in turn, enhanced CD38 mRNA expression. Taken together, the results provide compelling evidence for a new role for CD38\/ADP-ribosyl cyclase in the control of bone resorption, most likely exerted via cADPr.<\/jats:p>","DOI":"10.1083\/jcb.146.5.1161","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T12:46:23Z","timestamp":1027687583000},"page":"1161-1172","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":73,"title":["Cd38\/Adp-Ribosyl Cyclase"],"prefix":"10.1083","volume":"146","author":[{"given":"Li","family":"Sun","sequence":"first","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olugbenga A.","family":"Adebanjo","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baljit S.","family":"Moonga","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susanne","family":"Corisdeo","sequence":"additional","affiliation":[{"name":"bLankanau Medical Research Center, Merion, Pennsylvania 19066"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hindupur K.","family":"Anandatheerthavarada","sequence":"additional","affiliation":[{"name":"cSchool of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gopa","family":"Biswas","sequence":"additional","affiliation":[{"name":"cSchool of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toshiya","family":"Arakawa","sequence":"additional","affiliation":[{"name":"eMekai University, Saitama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshiyuki","family":"Hakeda","sequence":"additional","affiliation":[{"name":"eMekai University, Saitama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antoliy","family":"Koval","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bali","family":"Sodam","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.R.","family":"Bevis","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A. James","family":"Moser","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F. Anthony","family":"Lai","sequence":"additional","affiliation":[{"name":"dDepartment of Medicine, University of Cardiff, Cardiff, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Solomon","family":"Epstein","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce R.","family":"Troen","sequence":"additional","affiliation":[{"name":"bLankanau Medical Research Center, Merion, Pennsylvania 19066"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masayoshi","family":"Kumegawa","sequence":"additional","affiliation":[{"name":"eMekai University, Saitama, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mone","family":"Zaidi","sequence":"additional","affiliation":[{"name":"aCenter for Osteoporosis and Skeletal Aging, Department of Medicine, Medical College of Pennsylvania and Veterans Affairs Medical Center, Philadelphia, Pennsylvania 19104"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[1999,9,6]]},"reference":[{"key":"2023072901533213900_Adebanjoetal1994","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1006\/bbrc.1994.1291","article-title":"Modulation of the osteoclast Ca2+ receptor by extracellular protons. 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Cell Biol."},{"key":"2023072901533213900_Ausielloetal1996","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1006\/cimm.1996.0267","article-title":"Secretion of IFN-\u03b3, IL-6, granulocyte-macrophage colony-stimulating factor and IL-10 cytokines after activation of human purified T lymphocytes upon CD38 ligation","volume":"173","author":"Ausiello","year":"1996","journal-title":"Cell. Immunol."},{"key":"2023072901533213900_Berthelieretal1998","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1042\/bj3301383","article-title":"Human CD38 is an authentic NAD(P)+ glycohydrolase","volume":"330","author":"Berthelier","year":"1998","journal-title":"Biochem. J."},{"key":"2023072901533213900_Boydeetal1984","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1038\/sj.bdj.4805313","article-title":"Resorption of dentine by isolated osteoclasts in vitro","volume":"156","author":"Boyde","year":"1984","journal-title":"Brit. 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Metab."},{"key":"2023072901533213900_Kamedaetal1997","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1084\/jem.186.4.489","article-title":"Estrogen inhibits bone resorption by directly inducing apoptosis of bone resorbing osteoclasts","volume":"186","author":"Kameda","year":"1997","journal-title":"J. Exp. Med."},{"key":"2023072901533213900_Kamedaetal1998","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1006\/bbrc.1998.8448","article-title":"Calcium-sensing receptor in mature osteoclasts, which are bone resorbing cells","volume":"245","author":"Kameda","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023072901533213900_Katoetal1999","doi-asserted-by":"crossref","first-page":"1869","DOI":"10.1074\/jbc.274.4.1869","article-title":"CD38 disruption impairs glucose-induced increases in cyclic ADP-ribose, [Ca2+]i, and insulin secretion","volume":"274","author":"Kato","year":"1999","journal-title":"J. Biol. 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Chem."},{"key":"2023072901533213900_Mehtaetal1996","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1096\/fasebj.10.12.8903511","article-title":"Human CD38, a cell surface protein with multiple functions","volume":"10","author":"Mehta","year":"1996","journal-title":"FASEB J."},{"key":"2023072901533213900_Miyauchietal1990","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1083\/jcb.111.6.2543","article-title":"Osteoclast cytosolic calcium, regulated by voltage-gated calcium channels, extracellular calcium, controls podosome assembly and bone resorption","volume":"111","author":"Miyauchi","year":"1990","journal-title":"J. Cell Biol."},{"key":"2023072901533213900_Moongaetal1990","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1113\/jphysiol.1990.sp018242","article-title":"Intracellular regulation of enzyme secretion from rat osteoclasts and evidence for a functional role in bone resorption","volume":"42","author":"Moonga","year":"1990","journal-title":"J. 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