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

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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.

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

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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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Crossref · 10.4049/jimmunol.144.7.2811

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Background
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Background
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Background
ADP-Ribosyl Cyclase
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Background
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Background
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Background
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Inhibitor peptide SNP‐1 binds to a soluble form of BST‐1/CD157 at a 2 : 2 stoichiometry
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Background
Characterization and phylogenetic epitope mapping of CD38 ADPR cyclase in the cynomolgus macaque
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“This consists of a short intracytoplasmic (IC) tail, a transmembrane domain and a major extracellular domain (ECD) formed by 256 of the 300 constituent amino acids of the CD38 polypeptide [7].”
Background
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Background
The role of CD38 in ischemia reperfusion injury in cardiopulmonary bypass and thoracic transplantation: a narrative review
Gouchoe, D. A., Vijayakumar, A., Aly, A. H., Cui, E. Y., Essandoh, M. K., Gumina, R. J., Black, S. M., & Whitson, B. A. (2023) · Journal of Thoracic Disease · doi:10.21037/jtd-23-725 · Cited by 7
“CD38 has traditionally been characterized as a glycosylated cell surface protein (type II) protein with an extracellular catalytic domain (25).”
Background
Stimulation of natural killer cells with small molecule inhibitors of CD38 for the treatment of neuroblastoma
Mills, C. M., Benton, T. Z., Piña, I. C., Francis, M. J., Reyes, L., Dolloff, N. G., Peterson, Y. K., & Woster, P. M. (2023) · Chemical Science · doi:10.1039/d2sc05749b · Cited by 6
Identification of a major enzyme for the synthesis and hydrolysis of cyclic ADP-ribose in amphibian cells and evolutional conservation of the enzyme from human to invertebrate
Ikeda, T., Takasawa, S., Noguchi, N., Nata, K., Yamauchi, A., Takahashi, I., Yoshikawa, T., Sugawara, A., Yonekura, H., & Okamoto, H. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1284-0 · Cited by 6
Alteration of enzymatic properties of cell-surface antigen CD38 by agonistic anti-CD38 antibodies that prolong B cell survival and induce activation
Hara‐Yokoyama, M., Kimura, T., Kaku, H., Wakiyama, M., Kaitsu, Y., Inoue, M., Kusano, S., Shirouzu, M., Yokoyama, S., Katada, T., et al. (2007) · International Immunopharmacology · doi:10.1016/j.intimp.2007.10.010 · Cited by 6
Enzymic and Signal Transduction Properties of CD38/NADase and PC-1/Phosphodiesterase
Katada, T., Kontani, K., Wada, T., Hosoda, N., Hoshino, S.-I., & Nishina, H. (2000) · KARGER eBooks · doi:10.1159/000058762 · Cited by 6
CD38 gene-modified dendritic cells inhibit murine asthma development by increasing IL-12 production and promoting Th1 cell differentiation
Wang, J., Zhu, W., Chen, Y., Lin, Z., & Ma, S. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5756 · Cited by 6
“CD38, which consists of 304 amino acids, is a single chain type 2 transmembrane glycoprotein that belongs to the multifunctional ectoenzyme family (17,18).”
Hemin‐dependent induction and internalization of CD38 in K562 cells
Yalçıntepe, L., Erçelen, Ş., Çınar, S., Badur, S., Tiryaki, D., & Bermek, E. (2003) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10637 · Cited by 6
Signal Transduction Via the CD38/NAD+ Glycohydrolase
Kontani, K., Kukimoto, I., Kanda, Y., Inoue, S., Kishimoto, H., Hoshino, S.-I., Nishina, H., Takahashi, K., Hazeki, O., & Katada, T. (1997) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-8632-0_54 · Cited by 5
ADP-Ribosyl Cyclase in Rat Salivary Glands
Masuda, W., & Noguchi, T. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2450 · Cited by 5
ADP-Ribosyl Cyclases - A Family of cADPR and NAADP Metabolizing Enzymes
Lee, H. C., Munshi, C. B., & Graeff, R. M. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0269-2_2 · Cited by 5
CD38/ADP-ribosyl cyclase in the rat sublingual gland: Subcellular localization under resting and saliva-secreting conditions
Masuda, W., & Jimi, E. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.07.006 · Cited by 4
Dual Roles of CD38 in Autophagy
Wang, X., Song, J., Wu, Z., Fan, B., & Mode, X. (2017) · Yangtze Medicine · doi:10.4236/ym.2017.11002 · Cited by 4
“CD38 is a type II membrane protein, originally identified as a cell surface differentiation marker in B lymphocytes, and later found to be expressed ubiquitously [1] [2].”
Background
Exploiting CD38-mediated endocytosis for immunoliposome internalization
Orciani, M., Cavaletti, G., Fino, V., Mattioli‐Belmonte, M., Tredici, G., Bruni, P., & Primio, R. D. (2008) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e3282ffd673 · Cited by 4
Subpoblaciones de células T CD8+ en niños asintomáticos infectados verticalmente por el VIH-1
Resino, S., Bellón, J. M., Pérez, A., Gutiérrez, M. D. G., & Muñoz‐Fernández, M. Á. (2004) · Medicina Clínica · doi:10.1016/s0025-7753(04)74125-1 · Cited by 4
CD8 blockade promotes the expansion of antigen-specific CD4+ FOXP3+ regulatory T cells in vivo
Wang, Z., & Davies, J. D. (2006) · International Immunopharmacology · doi:10.1016/j.intimp.2006.10.012 · Cited by 4
“-PA Author M anuscript N IH -PA Author M anuscript N IH -PA Author M anuscript CD4+ regulatory T cells can also express CD38, a high density of CD62L (CD62Lhigh) and a low density of CD45RB (CD45RBlow).”
BackgroundInfluential
Regulation of Immune Responses by CD38 and cADPR
Lund, F. E., Randall, T. D., & Partida‐Sánchez, S. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0269-2_11 · Cited by 4
“CD38 was identified more than 20 years ago as a cell surface protein expressed on leukocyte subsets [1, 2].”
Background
Evolving understandings for the roles of CD38 protein in autoimmunity and autoimmune disease
Ye, X., Zhang, J., Song, M., Wang, P., Arés, I., López-Torres, B., Martínez, M., Martínez‐Larrañaga, M., Maximiliano, J.-E., Anadón, A., et al. (2026) · Clinical & Experimental Immunology · doi:10.1093/cei/uxag014 · Cited by 3
The ecto-enzyme CD38 modulates CD4T cell immunometabolic responses and participates in HIV pathogenesis
Díaz-Basilio, F., Vergara‐Mendoza, M., Romero-Rodríguez, J., Hernández-Rizo, S., Escobedo‐Calvario, A., Leon-Fuentes, L., Pérez-Patrigeón, S., Murakami-Ogasawara, A., Gómez-Palacio, M., Reyes‐Terán, G., et al. (2024) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiae060 · Cited by 4
Serum proteins with NAD+ glycohydrolase activity and anti-CD38 reactivity – elevated levels in serum of tumour patients
Korkut, Ç., Yalçıntepe, L., Kiremit-Korkut, N., Gocmen, S. U., Öztürk, S. İ., Gümüşel, F., Tiryaki, D., & Bermek, E. (1998) · Cancer Letters · doi:10.1016/s0304-3835(97)00531-4 · Cited by 3
Pathophysiological Implications of Altered Redox Balance in HIV/AIDS Infection: Diagnosis and Counteract Interventions
del Valle, L. G. (2011) · ACS symposium series · doi:10.1021/bk-2011-1083.ch002 · Cited by 3
Retinoid-Mediated Signaling and CD38 Expression
Mehta, K. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0269-2_20 · Cited by 3
Surface molecules involved in B lymphocyte function
Möller, P., Eichelmann, A., & Moldenhauer, G. (1991) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf01605069 · Cited by 3
Long-term high-protein diet intake accelerates adipocyte senescence through macrophage CD38-mediated NAD+ depletion
Yang, X., Hua, L., Gao, D., Wu, Y., Yang, Y., Jin, X., Jiang, X., Jin, C., Feng, B., Che, L., et al. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102306 · Cited by 3
“Considering that CD38 is predominantly expressed in immune cells and endothelial cells [52,53], we analyzed the snRNA-seq datasets to identify the cell populations responsible for CD38-mediated NAD + depletion.”
B cell antigens: A key to optimizing CAR-T cell therapy
Khodke, P., Hasurkar, D., Upadhyay, A., Shedge, A., Sippy, R., & Kumbhar, B. V. (2025) · International Reviews of Immunology · doi:10.1080/08830185.2025.2515839 · Cited by 3
“Cluster of differentiation 38 (CD38) also known as ADP-ribosyl cyclase or cyclic ADP-ribose hydrolase 1 [208] is a glycosylated membrane antigen, with a transmembrane domain close to its N-terminus as shown in Figure 5B [209].”
Distribution of plasma cell markers and intracellular IgE in cell line U266
Lagging, E., van Hage, M., Härfast, B., & Halldén, G. (1996) · Immunology Letters · doi:10.1016/0165-2478(95)02483-2 · Cited by 2

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
Life Sciences › Immunology and Microbiology › Immunology › 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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