Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation.

Jackson, D G; Bell, J I

doi:10.4049/jimmunol.144.7.2811

Cited by 345T-cell and B-cell ImmunologyMonoclonal and Polyclonal Antibodies ResearchCell Adhesion Molecules Research

Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation.

Jackson, D G, Bell, J I·1990·The Journal of Immunology

DOI 10.4049/jimmunol.144.7.2811

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Abstract

A cDNA clone encoding the human lymphocyte differentiation Ag CD38 was isolated from a mixture of four different lymphocyte CDNA libraries expressed transiently in COS cells and screened by panning with mAb. Transfected COS cells expressed a surface protein of Mr 46,000 that was similar to the native CD38 molecule expressed on the B cell line Daudi and the T cell leukemia HPB-ALL and which was recognized by each of the CD38 specific mAb HIT-2, T16, T168, HB7, 5D2, ICO-18, and ICO-20. The CD38 cDNA sequence predicts an unusual 30-kDa polypeptide with a short N-terminal cytoplasmic tail, and a carboxyl-terminal extracellular domain carrying the four potential N-linked glycosylation sites. The absence of significant homology with other known surface Ag including members of the Ig superfamily ruled out the possibility that CD38 was the human homologue of the murine Qa2 molecule as has been suggested previously. PvuII digests of human genomic DNA revealed a polymorphism linked to the CD38 gene.

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The human CD38 gene: polymorphism, CpG island, and linkage to the CD157 ( BST-1 ) gene
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“Human CD38 also displays genetic variability, as suggested in the original cDNA cloning report by Jackson and Bell (1990) who found differences in the gene among healthy individuals by Southern blot analysis of Pvu IIdigested DNA.”
Background
CD38: T Cell Immuno-Metabolic Modulator
Kar, A., Mehrotra, S., & Chatterjee, S. (2020) · Cells · doi:10.3390/cells9071716 · Cited by 91 · see citing works
Roles and mechanisms of the CD38/cyclic adenosine diphosphate ribose/Ca<sup>2+</sup>signaling pathway
Wei, W. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i1.58 · Cited by 89 · see citing works
CD38 Deficiency Protects the Heart from Ischemia/Reperfusion Injury through Activating SIRT1/FOXOs‐Mediated Antioxidative Stress Pathway
Guan, X., Liu, X., Hong, X., Zhao, N., Xiao, Y., Wang, L.-F., Tang, L., Jiang, K., Qian, Y., Deng, K., et al. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7410257 · Cited by 90 · see citing works
“As a membrane protein, CD38 contains a single transmembrane domain, a short N-terminal cytoplasmic tail, and a carboxyl-terminal extracellular domain [9].”
Background
Activation of the Aryl Hydrocarbon Receptor AhR Promotes Retinoic Acid–Induced Differentiation of Myeloblastic Leukemia Cells by Restricting Expression of the Stem Cell Transcription Factor Oct4
Bunaciu, R. P., & Yen, A. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2299 · Cited by 84 · see citing works
“CD38 is a type II transmembrane glycoprotein, expressed on several leukocytes and early hematopoietic precursor cells (25), that can signal through Raf and ERK activation (26).”
Background
Antigen-induced clustering of surface CD38 and recruitment of intracellular CD38 to the immunologic synapse
Muñoz, P., Mittelbrunn, M., de la Fuente, H., Pérez‐Martínez, M., García-Pérez, A., Ariza, A., Malavasi, F., Zubiaur, M., Sánchez‐Madrid, F., & Sancho, J. (2008) · Blood · doi:10.1182/blood-2007-07-101600 · Cited by 82 · see citing works
The CD38/cyclic ADP-ribose system: A topological paradox
FLORA, A. D., Guida, L., Franco, L., & Zocchi, E. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)00062-9 · Cited by 82 · see citing works
Localization of the Cyclic ADP-ribose-dependent Calcium Signaling Pathway in Hepatocyte Nucleus
Khoo, K. M., Han, M., Park, J. B., Chae, S., Kim, U., Lee, H. C., Bay, B., & Chang, C. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908231199 · Cited by 82 · see citing works
Engineered anti-CD38 monoclonal antibodies for immunotherapy of multiple myeloma
Ellis, J. H., Barber, K. A., Tutt, A. N. J., Hale, C., Lewis, A., Glennie, M. J., Stevenson, G. T., & Crowe, J. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.2.925 · Cited by 81 · see citing works
Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing
Nata, K., Takamura, T., Karasawa, T., Kumagai, T., Hashioka, W., Tohgo, A., Yonekura, H., Takasawa, S., Nakamura, S., & Okamoto, H. (1997) · Gene · doi:10.1016/s0378-1119(96)00723-8 · Cited by 81 · see citing works
CD38 gene polymorphism and chronic lymphocytic leukemia: a role in transformation to Richter syndrome?
Aydin, S., Rossi, D., Bergui, L., D'Arena, G. F., Ferrero, E., Bonello, L., Omedè, P., Novero, D., Morabito, F., Carbone, A., et al. (2008) · Blood · doi:10.1182/blood-2008-01-129726 · Cited by 80 · see citing works
Nicotinamide adenine dinucleotide: Biosynthesis, consumption and therapeutic role in cardiac diseases
Tannous, C., Booz, G. W., Altara, R., Muhieddine, D. H., Mericskay, M., Refaat, M. M., & Zouein, F. A. (2020) · Acta Physiologica · doi:10.1111/apha.13551 · Cited by 79 · see citing works
CD38 Signaling in T Cells Is Initiated within a Subset of Membrane Rafts Containing Lck and the CD3-ζ Subunit of the T Cell Antigen Receptor
Muñoz, P., Navarro, M.-D.-C., Pavón, E. J., Salmerón, J., Malavasi, F., Sancho, J., & Zubiaur, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308034200 · Cited by 79 · see citing works
The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38
Ferrero, E., & Malavasi, F. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.65.2.151 · Cited by 79 · see citing works
“In view of its immunological background, CD38 was studied in great detail in hematopoietic cells where its expression has been most appropriately termed ‘discontinuous’ [4].”
BackgroundInfluential
Resolving the topological enigma in Ca2+ signaling by cyclic ADP-ribose and NAADP
Lee, H. C., & Zhao, Y. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.009635 · Cited by 78 · see citing works
“CD38 is a single pass membrane protein consists of a short amino tail, a transmembrane segment and a C-domain (21).”
BackgroundInfluential
Human lymphocyte antigen CD38 catalyzes the production of cyclic ADP‐ribose
Summerhill, R. J., Jackson, D. G., & Galione, A. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80735-d · Cited by 78 · see citing works
Self-citation
Novel aspects of signaling and ion-homeostasis regulation in immunocytesThe TRPM ion channels and their potential role in modulating the immune response
Perraud, A. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2004.04.013 · Cited by 77 · see citing works
Review: NAD + : A modulator of immune functions
Grahnert, A., Grahnert, A., Klein, C., Schilling, E., Wehrhahn, J., & Hauschildt, S. (2010) · Innate Immunity · doi:10.1177/1753425910361989 · Cited by 76 · see citing works
CD38 ligation induces discrete cytokine mRNA expression in human cultured lymphocytes
Ausiello, C. M., Urbani, F., la Sala, A., Funaro, A., & Malavasi, F. (1995) · European Journal of Immunology · doi:10.1002/eji.1830250554 · Cited by 76 · see citing works
Extracellular cyclic ADP‐ribose increases intracellular free calcium concentration and stimulates proliferation of human hemopoietic progenitors
Podestà, M., Zocchi, E., Pitto, A., Usai, C., Franco, L., Bruzzone, S., Guida, L., Bacigalupo, A. P., Scadden, D. T., Walseth, T. F., et al. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.5.680 · Cited by 75 · see citing works
“Both mammalian cyclases are expressed in the bone marrow (BM): CD38 on hemopoietic cells (7, 18) and BST-1 on stromal cells (9); the presence of NAD(1) in plasma and interstitial fluids (16) could enable production of extracellular cADPR in the BM microenvironment.”
Background
Lack of NK cells in lupus patients with renal involvement
Erkeller-Yüksel, F., Lydyard, P. M., & Isenberg, D. A. (1997) · Lupus · doi:10.1177/096120339700600905 · Cited by 74 · see citing works
Accumulation of cyclic ADP‐ribose measured by a specific radioimmunoassay in differentiated human leukemic HL‐60 cells with all‐trans‐retinoic acid
Takahashi, K., Kukimoto, I., Tokita, K., Inageda, K., Inoue, S.-I., Kontani, K., Hoshino, S.-I., Nishina, H., Kanaho, Y., & Katada, T. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00914-u · Cited by 74 · see citing works
High Expression of a CD38-Like Molecule in Normal Prostatic Epithelium and its Differential Loss in Benign and Malignant Disease
Kramer, G., Steiner, G. E., Födinger, D., Fiebiger, E., Rappersberger, C., Binder, S., Hofbauer, J., & Marberger, M. (1995) · The Journal of Urology · doi:10.1016/s0022-5347(01)66733-8 · Cited by 72 · see citing works
A Single Residue at the Active Site of CD38 Determines Its NAD Cyclizing and Hydrolyzing Activities
Graeff, R. M., Munshi, C. B., Aarhus, R., Johns, M. E., & Lee, H. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011299200 · Cited by 71 · see citing works
CD38-mediated growth suppression of B-cell progenitors requires activation of phosphatidylinositol 3-kinase and involves its association with the protein product of the c-cbl proto-oncogene
Kitanaka, A., Ito, C., Nishigaki, H., & Campana, D. (1996) · Blood · doi:10.1182/blood.v88.2.590.bloodjournal882590 · Cited by 70 · see citing works
Glucocorticoid Regulation of Natural Cytotoxicity: Effects of Cortisol on the Phenotype and Function of a Cloned Human Natural Killer Cell Line
Zhou, J., Olsen, S., Moldovan, J. B., Fu, X., Sarkar, F. H., Moudgil, V. K., & Callewaert, D. M. (1997) · Cellular Immunology · doi:10.1006/cimm.1997.1138 · Cited by 69 · see citing works
Equilibrative and Concentrative Nucleoside Transporters Mediate Influx of Extracellular Cyclic ADP-Ribose into 3T3 Murine Fibroblasts
Guida, L., Bruzzone, S., Sturla, L., Franco, L., Zocchi, E., & FLORA, A. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207793200 · Cited by 68 · see citing works
Innate immunity is regulated by CD38, an ecto-enzyme with ADP-ribosyl cyclase activity
Partida‐Sánchez, S., Randall, T. D., & Lund, F. E. (2003) · Microbes and Infection · doi:10.1016/s1286-4579(02)00055-2 · Cited by 68 · see citing works
CD38 Functions Are Regulated Through an Internalization Step
Funaro, A., Reiniš, M., Trubiani, O., Santi, S., Primio, R. D., & Malavasi, F. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.5.2238 · Cited by 68 · see citing works
“Cloning and sequencing showed that CD38 has a very short cytoplasmic tail lacking conventional internalization signals and potential phosphorylation sites (38).”
Background

The murine homologue of the T lymphocyte antigen CD28. Molecular cloning and cell surface expression.
Gross, J. A., John, T. S., & Allison, J. P. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.8.3201 · Cited by 152 · see citing works
CD38: A multi-lineage cell activation molecule with a split personality
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Isolation of a cDNA encoding CD33, a differentiation antigen of myeloid progenitor cells.
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CD38 molecule: structural and biochemical analysis on human T lymphocytes, thymocytes, and plasma cells.
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Molecular cloning of a cDNA encoding CD34, a sialomucin of human hematopoietic stem cells
Simmons, D. L., Satterthwaite, A. B., Tenen, D. G., & Seed, B. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.1.267 · Cited by 239 · see citing works

Authors: Jackson, D. G., & Bell, J. I.
Affiliations: John Radcliffe Hospital (GB)
ORCID: Jackson, D G
Bell, J I
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 1990-04-01
Volume: 144
Issue: 7
Pages: 2811-2815
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.144.7.2811
OpenAlex: W1566643819
Cited by: 343
References: 0
Citations by year: 2026: 5 · 2025: 3 · 2024: 4 · 2023: 2 · 2022: 10 · 2021: 3 · 2020: 13 · 2019: 9 · 2018: 8 · 2017: 6 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 5 · 2012: 10
FWCI: 3.27
Type: journal article
Language: en
Open access: closed
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords: CD38, lymphocyte differentiation antigens, cDNA cloning, cell surface glycoproteins, lymphocyte differentiation, B cells, T cells, monoclonal antibodies, N-glycosylation, cytoplasmic tail, genetic polymorphism, Daudi cells
MeSH terms: Amino Acid Sequence, Antigens, Differentiation, Base Sequence, Cloning, Molecular, DNA, Genes, Humans, Lymphocytes, Membrane Glycoproteins, Molecular Sequence Data, Molecular Weight, Solubility, Transfection, Blotting, Southern, Antigens, CD, Gene Expression, ADP-ribosyl Cyclase, ADP-ribosyl Cyclase 1

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Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation.

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