Mechanism-based Small Molecule Probes for Labeling CD38 on Live Cells

Overview

Journal J Am Chem Soc

Publisher American Chemical Society

Specialty Chemistry

Date 2009 Feb 5

PMID 19191692

Citations 16

Authors

Hong Jiang

Johanna Congleton

Qun Liu

Paolomi Merchant

Fabio Malavasi

Hon Cheung Lee

Quan Hao

Andrew Yen

Hening Lin

Affiliations

Soon will be listed here.

Abstract

CD38 is a type II transmembrane glycoprotein with multiple functions. It acts as an ecto-enzyme as well as a receptor. The enzymatic activity catalyzes the formation of two potent Ca(2+) releasing agents: cyclic adenosine diphosphate ribose (cADPR) from nicotinamide adenine dinucleotide (NAD) and nicotinic acid adenine dinucleotide phosphate (NAADP) from NAD phosphate (NADP). The receptor function of CD38 leads to the phosphorylation of intracellular signaling proteins and the up-regulation of cytokine production in immune cells. These two functions of CD38 underlie its involvement in various biological processes, such as hormone secretion, immune cell differentiation, and immune responses. Clinically, CD38 is used as a negative prognosis marker for chronic lymphatic leukemia (CLL). However, a clear molecular understanding of CD38's role in physiology and pathology is still lacking. To facilitate the study of CD38 at cellular and molecular levels, here we report a mechanism-based method for fluorescently labeling CD38 on live cells. This labeling method does not interfere with the receptor function of CD38 and the downstream signaling. The labeling method is thus a useful tool to study the receptor function of CD38 in live cells. In addition, since the mechanism-based labeling also inhibits the enzymatic activity of CD38, it should be useful for dissecting the receptor function of CD38 without interference from its enzyme function in complicated biological processes.

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References

Deaglio S, Vaisitti T, Aydin S, Ferrero E, Malavasi F . In-tandem insight from basic science combined with clinical research: CD38 as both marker and key component of the pathogenetic network underlying chronic lymphocytic leukemia. Blood. 2006; 108(4):1135-44. DOI: 10.1182/blood-2006-01-013003. View

Howard M, Grimaldi J, Bazan J, Lund F, Santos-Argumedo L, Parkhouse R . Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science. 1993; 262(5136):1056-9. DOI: 10.1126/science.8235624. View

Yin J, Lin A, Buckett P, Wessling-Resnick M, Golan D, Walsh C . Single-cell FRET imaging of transferrin receptor trafficking dynamics by Sfp-catalyzed, site-specific protein labeling. Chem Biol. 2005; 12(9):999-1006. PMC: 2494879. DOI: 10.1016/j.chembiol.2005.07.006. View

Lee H . Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu Rev Pharmacol Toxicol. 2001; 41:317-45. DOI: 10.1146/annurev.pharmtox.41.1.317. View

Deaglio S, Vaisitti T, Billington R, Bergui L, Omede P, Genazzani A . CD38/CD19: a lipid raft-dependent signaling complex in human B cells. Blood. 2007; 109(12):5390-8. DOI: 10.1182/blood-2006-12-061812. View

Johnson J, Ford E, Bernal-Mizrachi E, Kusser K, Luciani D, Han Z . Suppressed insulin signaling and increased apoptosis in CD38-null islets. Diabetes. 2006; 55(10):2737-46. DOI: 10.2337/db05-1455. View

Kontani K, Nishina H, Ohoka Y, Takahashi K, Katada T . NAD glycohydrolase specifically induced by retinoic acid in human leukemic HL-60 cells. Identification of the NAD glycohydrolase as leukocyte cell surface antigen CD38. J Biol Chem. 1993; 268(23):16895-8. View

Munoz P, Mittelbrunn M, de la Fuente H, Perez-Martinez M, Garcia-Perez A, Ariza-Veguillas A . Antigen-induced clustering of surface CD38 and recruitment of intracellular CD38 to the immunologic synapse. Blood. 2008; 111(7):3653-64. DOI: 10.1182/blood-2007-07-101600. View

Dianzani U, Funaro A, Difranco D, Garbarino G, Bragardo M, Redoglia V . Interaction between endothelium and CD4+CD45RA+ lymphocytes. Role of the human CD38 molecule. J Immunol. 1994; 153(3):952-9. View

10.

Tornoe C, Christensen C, Meldal M . Peptidotriazoles on solid phase: [1,2,3]-triazoles by regiospecific copper(i)-catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J Org Chem. 2002; 67(9):3057-64. DOI: 10.1021/jo011148j. View

11.

Kato I, Yamamoto Y, Fujimura M, Noguchi N, Takasawa S, Okamoto H . CD38 disruption impairs glucose-induced increases in cyclic ADP-ribose, [Ca2+]i, and insulin secretion. J Biol Chem. 1999; 274(4):1869-72. DOI: 10.1074/jbc.274.4.1869. View

12.

Jin D, Liu H, Hirai H, Torashima T, Nagai T, Lopatina O . CD38 is critical for social behaviour by regulating oxytocin secretion. Nature. 2007; 446(7131):41-5. DOI: 10.1038/nature05526. View

13.

Zubiaur M, Fernandez O, Ferrero E, Salmeron J, Malissen B, Malavasi F . CD38 is associated with lipid rafts and upon receptor stimulation leads to Akt/protein kinase B and Erk activation in the absence of the CD3-zeta immune receptor tyrosine-based activation motifs. J Biol Chem. 2001; 277(1):13-22. DOI: 10.1074/jbc.M107474200. View

14.

Lamkin T, Chin V, Varvayanis S, Smith J, Sramkoski R, Jacobberger J . Retinoic acid-induced CD38 expression in HL-60 myeloblastic leukemia cells regulates cell differentiation or viability depending on expression levels. J Cell Biochem. 2005; 97(6):1328-38. DOI: 10.1002/jcb.20745. View

15.

Malavasi F, Deaglio S, Funaro A, Ferrero E, Horenstein A, Ortolan E . Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology. Physiol Rev. 2008; 88(3):841-86. DOI: 10.1152/physrev.00035.2007. View

16.

Ausiello C, Urbani F, Lande R, la Sala A, Di Carlo B, Baj G . Functional topography of discrete domains of human CD38. Tissue Antigens. 2001; 56(6):539-47. DOI: 10.1034/j.1399-0039.2000.560608.x. View

17.

Deaglio S, Morra M, Mallone R, Ausiello C, Prager E, Garbarino G . Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member. J Immunol. 1998; 160(1):395-402. View

18.

Chen I, Howarth M, Lin W, Ting A . Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat Methods. 2005; 2(2):99-104. DOI: 10.1038/nmeth735. View

19.

Matrai Z . CD38 as a prognostic marker in CLL. Hematology. 2005; 10(1):39-46. DOI: 10.1080/10245330400020470. View

20.

Rostovtsev V, Green L, Fokin V, Sharpless K . A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes. Angew Chem Int Ed Engl. 2002; 41(14):2596-9. DOI: 10.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-4. View