CD38: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''CD38''' ([[cluster of differentiation]] 38), also known as '''cyclic ADP ribose hydrolase''' is a  [[glycoprotein]]<ref name="pmid18759251">{{cite journal |vauthors=Orciani M, Trubiani O, Guarnieri S, Ferrero E, Di Primio R |title=CD38 is constitutively expressed in the nucleus of human hematopoietic cells |journal=J. Cell. Biochem. |volume=105 |issue=3 |pages=905–12 |date=October 2008 |pmid=18759251 |doi=10.1002/jcb.21887}}</ref> found on the surface of many immune cells ([[white blood cell]]s), including [[CD4]]<sup>+</sup>, [[CD8]]<sup>+</sup>, [[B lymphocyte]]s and [[natural killer cell]]s. CD38 also functions in [[cell adhesion]], [[signal transduction]] and [[calcium signaling]].<ref>{{cite web | title = Entrez Gene: CD38 CD38 molecule| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=952| accessdate = }}</ref>
'''CD38''' ([[cluster of differentiation]] 38), also known as '''cyclic ADP ribose hydrolase''' is a  [[glycoprotein]]<ref name="pmid18759251">{{cite journal | vauthors = Orciani M, Trubiani O, Guarnieri S, Ferrero E, Di Primio R | title = CD38 is constitutively expressed in the nucleus of human hematopoietic cells | journal = Journal of Cellular Biochemistry | volume = 105 | issue = 3 | pages = 905–12 | date = October 2008 | pmid = 18759251 | doi = 10.1002/jcb.21887 }}</ref> found on the surface of many immune cells ([[white blood cell]]s), including [[CD4]]<sup>+</sup>, [[CD8]]<sup>+</sup>, [[B lymphocyte]]s and [[natural killer cell]]s. CD38 also functions in [[cell adhesion]], [[signal transduction]] and [[calcium signaling]].<ref>{{cite web | title = Entrez Gene: CD38 CD38 molecule| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=952| access-date = }}</ref>


In humans, the CD38 protein is encoded by the CD38 [[gene]] which is located on [[chromosome 4 (human)|chromosome 4]].<ref name="pmid2319135">{{cite journal | vauthors = Jackson DG, Bell JI | title = Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation | journal = J. Immunol. | volume = 144 | issue = 7 | pages = 2811–5 |date=April 1990 | pmid = 2319135 | doi = | url = http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=2319135 }}</ref><ref name="pmid9074508">{{cite journal | vauthors = Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H | title = Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing | journal = Gene | volume = 186 | issue = 2 | pages = 285–92 |date=February 1997 | pmid = 9074508 | doi = 10.1016/S0378-1119(96)00723-8| url = http://linkinghub.elsevier.com/retrieve/pii/S0378-1119(96)00723-8 }}</ref>
In humans, the CD38 protein is encoded by the CD38 [[gene]] which is located on [[chromosome 4 (human)|chromosome 4]].<ref name="pmid2319135">{{cite journal | vauthors = Jackson DG, Bell JI | title = Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation | journal = Journal of Immunology | volume = 144 | issue = 7 | pages = 2811–5 | date = April 1990 | pmid = 2319135 | doi = | url = http://www.jimmunol.org/cgi/pmidlookup?view=long&pmid=2319135 }}</ref><ref name="pmid9074508">{{cite journal | vauthors = Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H | title = Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing | journal = Gene | volume = 186 | issue = 2 | pages = 285–92 | date = February 1997 | pmid = 9074508 | doi = 10.1016/S0378-1119(96)00723-8 }}</ref>


== Function ==
== Function ==


CD38 is a multifunctional [[ectonucleotidase|ectoenzyme]] that catalyzes the synthesis and hydrolysis of [[cyclic ADP-ribose]] (cADPR) from [[Nicotinamide adenine dinucleotide|NAD<sup>+</sup>]] to [[Adenosine diphosphate ribose|ADP-ribose]]. These reaction products are essential for the regulation of intracellular Ca<sup>2+</sup>.<ref name="pmid18626062">{{cite journal | vauthors = Malavasi F, Deaglio S, Funaro A, Ferrero E, Horenstein AL, Ortolan E, Vaisitti T, Aydin S | title = Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology | journal = Physiol. Rev. | volume = 88 | issue = 3 | pages = 841–86 |date=July 2008 | pmid = 18626062 | doi = 10.1152/physrev.00035.2007 | url =  }}</ref>
CD38 is a multifunctional [[ectonucleotidase|ectoenzyme]] that catalyzes the synthesis and hydrolysis of [[cyclic ADP-ribose]] (cADPR) from [[Nicotinamide adenine dinucleotide|NAD<sup>+</sup>]] to [[Adenosine diphosphate ribose|ADP-ribose]] in addition to synthesis of NAADP from NADP+.<ref>{{cite journal | vauthors = Chini EN, Chini CC, Kato I, Takasawa S, Okamoto H | title = CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues | journal = The Biochemical Journal | volume = 362 | issue = Pt 1 | pages = 125–30 | date = February 2002 | pmid = 11829748 | pmc = 1222368 }}</ref> These reaction products are essential for the regulation of intracellular Ca<sup>2+</sup>.<ref name="pmid18626062">{{cite journal | vauthors = Malavasi F, Deaglio S, Funaro A, Ferrero E, Horenstein AL, Ortolan E, Vaisitti T, Aydin S | title = Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology | journal = Physiological Reviews | volume = 88 | issue = 3 | pages = 841–86 | date = July 2008 | pmid = 18626062 | doi = 10.1152/physrev.00035.2007 }}</ref>


== Clinical significance ==
== Clinical significance ==


The loss of CD38 function is associated with impaired immune responses, metabolic disturbances, and behavioral modifications including social amnesia possibly related to autism.<ref name="pmid18626062"/><ref name="Higashida_2012">{{cite journal | vauthors = Higashida H, Yokoyama S, Huang JJ, Liu L, Ma WJ, Akther S, Higashida C, Kikuchi M, Minabe Y, Munesue T | title = Social memory, amnesia, and autism: brain oxytocin secretion is regulated by NAD+ metabolites and single nucleotide polymorphisms of CD38 | journal = Neurochem. Int. | volume = 61 | issue = 6 | pages = 828–38 |date=November 2012 | pmid = 22366648 | doi = 10.1016/j.neuint.2012.01.030 }}</ref>
The loss of CD38 function is associated with impaired immune responses, metabolic disturbances, and behavioral modifications including social amnesia possibly related to autism.<ref name="pmid18626062"/><ref name="Higashida_2012">{{cite journal | vauthors = Higashida H, Yokoyama S, Huang JJ, Liu L, Ma WJ, Akther S, Higashida C, Kikuchi M, Minabe Y, Munesue T | title = Social memory, amnesia, and autism: brain oxytocin secretion is regulated by NAD+ metabolites and single nucleotide polymorphisms of CD38 | journal = Neurochemistry International | volume = 61 | issue = 6 | pages = 828–38 | date = November 2012 | pmid = 22366648 | doi = 10.1016/j.neuint.2012.01.030 | url = https://kanazawa-u.repo.nii.ac.jp/?action=repository_uri&item_id=30999 | format = Submitted manuscript }}</ref>


The CD38 protein is a marker of cell activation. It has been connected to [[HIV]] infection, [[leukemia]]s, [[myeloma]]s, solid tumors, [[type II diabetes mellitus]] and bone metabolism, as well as some genetically determined conditions.
The CD38 protein is a marker of cell activation. It has been connected to [[HIV]] infection, [[leukemia]]s, [[myeloma]]s, solid tumors, [[type II diabetes mellitus]] and bone metabolism, as well as some genetically determined conditions.
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CD38 produces an enzyme which regulates the release of [[oxytocin]] within the central nervous system.<ref name="Higashida_2012"/>
CD38 produces an enzyme which regulates the release of [[oxytocin]] within the central nervous system.<ref name="Higashida_2012"/>


A gradual increase in CD38 has been implicated in the decline of [[NAD+]] with age.<ref>{{cite journal | vauthors=Camacho-Pereira J, Tarragó MG, Chini CC, Nin V, Escande C, Warner GM, Puranik AS, Schoon RA, Reid JM, Galina A, Chini EN | title=CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism. | journal = Cell Metab | volume=23 | issue=6 | pages=1127-1139 | doi = 10.1016/j.cmet.2016.05.006 }}</ref>,<ref>{{cite journal | vauthors=Schultz M, Sinclair D | title=Why NAD+ Declines during Aging: It’s Destroyed | journal = Cell Metab |
[[Daratumumab]] which targets CD38 has been used in treating [[multiple myeloma]].<ref name="pmid26729183">{{cite journal | vauthors = McKeage K | title = Daratumumab: First Global Approval | journal = Drugs | volume = 76 | issue = 2 | pages = 275–81 | date = February 2016 | pmid = 26729183 | doi = 10.1007/s40265-015-0536-1 }}</ref><ref name="pmid27910963">{{cite journal | vauthors = Xia C, Ribeiro M, Scott S, Lonial S | title = Daratumumab: monoclonal antibody therapy to treat multiple myeloma | journal = Drugs of Today | volume = 52 | issue = 10 | pages = 551–560 | date = October 2016 | pmid = 27910963 | doi = 10.1358/dot.2016.52.10.2543308 }}</ref>
volume=23 | issue = 6 | pages = 965-966 | doi = 10.1016/j.cmet.2016.05.022 }}</ref>


[[Daratumumab]] which targets CD38 has been used in treating [[multiple myeloma]].<ref name="pmid26729183">{{cite journal | vauthors = McKeage K | title = Daratumumab: First Global Approval | journal = Drugs | volume = 76 | issue = 2 | pages = 275–81 | year = 2016 | pmid = 26729183 | doi = 10.1007/s40265-015-0536-1 }}</ref><ref name="pmid27910963">{{cite journal | vauthors = Xia C, Ribeiro M, Scott S, Lonial S | title = Daratumumab: monoclonal antibody therapy to treat multiple myeloma | journal = Drugs of Today | volume = 52 | issue = 10 | pages = 551–560 | year = 2016 | pmid = 27910963 | doi = 10.1358/dot.2016.52.10.2543308 }}</ref>
Increased expression of CD 38 is an unfavourable diagnostic marker in [[chronic lymphocytic leukemia]] and is associated with increased disease progression.<ref name="pmid26853852">{{cite journal | vauthors = Burgler S | title = Role of CD38 Expression in Diagnosis and Pathogenesis of Chronic Lymphocytic Leukemia and Its Potential as Therapeutic Target | journal = Critical Reviews in Immunology | volume = 35 | issue = 5 | pages = 417–32 | year = 2015 | pmid = 26853852 | doi = 10.1615/CritRevImmunol.v35.i5.50 }}</ref>


Increased expression of CD 38 in [[chronic lymphocytic leukemia]] is a associated with shorter time to progression.<ref name="pmid26853852">{{cite journal | vauthors = Burgler S | title = Role of CD38 Expression in Diagnosis and Pathogenesis of Chronic Lymphocytic Leukemia and Its Potential as Therapeutic Target | journal = Critical Reviews in Immunology | volume = 35 | issue = 5 | pages = 417–32 | year = 2015 | pmid = 26853852 | doi = 10.1615/CritRevImmunol.v35.i5.50  }}</ref>
== Application ==


== Application ==
CD38 has been used as a prognostic marker in [[leukemia]].<ref name="pmid11137554">{{cite journal | vauthors = Deaglio S, Mehta K, Malavasi F | title = Human CD38: a (r)evolutionary story of enzymes and receptors | journal = Leukemia Research | volume = 25 | issue = 1 | pages = 1–12 | date = January 2001 | pmid = 11137554 | doi = 10.1016/S0145-2126(00)00093-X }}</ref> CD38 is also used as a target for [[daratumumab]] (Darzalex), a medicine that has been approved for the treatment of [[multiple myeloma]].
 
The use of Daratumumab can interfere with pre-[[Blood transfusion]] tests, as CD38 is weakly expressed on the surface of [[erythrocytes]]. Thus, a screening assay for irregular antibodies against red blood cell antigens or a direct immunoglobulin test can produce false-positive results.<ref name="pmid29781081">{{cite journal | vauthors = de Vooght KM, Lozano M, Bueno JL, Alarcon A, Romera I, Suzuki K, Zhiburt E, Holbro A, Infanti L, Buser A, Hustinx H, Deneys V, Frelik A, Thiry C, Murphy M, Staves J, Selleng K, Greinacher A, Kutner JM, Bonet Bub C, Castilho L, Kaufman R, Colling ME, Perseghin P, Incontri A, Dassi M, Brilhante D, Macedo A, Cserti-Gazdewich C, Pendergrast JM, Hawes J, Lundgren MN, Storry JR, Jain A, Marwaha N, Sharma RR | title = Vox Sanguinis International Forum on typing and matching strategies in patients on anti-CD38 monoclonal therapy: summary | journal = Vox Sanguinis | volume = 113 | issue = 5 | pages = 492-498 | date = May 2018 | pmid = 29781081 | doi = 10.1111/vox.12653 }}</ref> This can be sidelined by either pretreatment of the [[erythrocytes]] with [[dithiothreitol]] (DTT) or by using an anti-CD38 antibody neutralizing agent, e.g. DaraEx.


CD38 has been used as a prognostic marker in [[leukemia]].<ref name="pmid11137554">{{cite journal | vauthors = Deaglio S, Mehta K, Malavasi F | title = Human CD38: a (r)evolutionary story of enzymes and receptors | journal = Leuk. Res. | volume = 25 | issue = 1 | pages = 1–12 | year = 2001 | pmid = 11137554 | doi = 10.1016/S0145-2126(00)00093-X }}</ref> CD38 is also use as a target for [[Daratumumab]], a medicine that has been approved for the treatment of [[multiple myeloma]]
== Animal studies ==
A gradual increase in CD38 has been implicated in the decline of [[NAD+]] with age.<ref>{{cite journal | vauthors = Camacho-Pereira J, Tarragó MG, Chini CC, Nin V, Escande C, Warner GM, Puranik AS, Schoon RA, Reid JM, Galina A, Chini EN | title = CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism | journal = Cell Metabolism | volume = 23 | issue = 6 | pages = 1127–1139 | date = June 2016 | pmid = 27304511 | pmc = 4911708 | doi = 10.1016/j.cmet.2016.05.006 }}</ref><ref>{{cite journal | vauthors = Schultz MB, Sinclair DA | title = Why NAD(+) Declines during Aging: It's Destroyed | journal = Cell Metabolism | volume = 23 | issue = 6 | pages = 965–966 | date = June 2016 | pmid = 27304496 | pmc = 5088772 | doi = 10.1016/j.cmet.2016.05.022 }}</ref> Treatment of old mice with a specific CD38 inhibitor, 78c, prevents age-related NAD+ decline.<ref>{{cite journal | vauthors = Tarragó MG, Chini CC, Kanamori KS, Warner GM, Caride A, de Oliveira GC, Rud M, Samani A, Hein KZ, Huang R, Jurk D, Cho DS, Boslett JJ, Miller JD, Zweier JL, Passos JF, Doles JD, Becherer DJ, Chini EN | title = + Decline | journal = Cell Metabolism | volume = 27 | issue = 5 | pages = 1081–1095.e10 | date = May 2018 | pmid = 29719225 | pmc = 5935140 | doi = 10.1016/j.cmet.2018.03.016 }}</ref>


==References==
== References ==
{{Reflist|2}}
{{Reflist|2}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal | vauthors=States DJ, Walseth TF, Lee HC |title=Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38 |journal=Trends Biochem. Sci. |volume=17 |issue= 12 |pages= 495 |year= 1993 |pmid= 1471258 |doi=10.1016/0968-0004(92)90337-9 }}
* {{cite journal | vauthors = States DJ, Walseth TF, Lee HC | title = Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38 | journal = Trends in Biochemical Sciences | volume = 17 | issue = 12 | pages = 495 | date = December 1992 | pmid = 1471258 | doi = 10.1016/0968-0004(92)90337-9 }}
*{{cite journal | vauthors=Malavasi F, Funaro A, Roggero S |title=Human CD38: a glycoprotein in search of a function |journal=Immunol. Today |volume=15 |issue= 3 |pages= 95–7 |year= 1994 |pmid= 8172650 |doi=10.1016/0167-5699(94)90148-1 |display-authors=etal}}
* {{cite journal | vauthors = Malavasi F, Funaro A, Roggero S, Horenstein A, Calosso L, Mehta K | title = Human CD38: a glycoprotein in search of a function | journal = Immunology Today | volume = 15 | issue = 3 | pages = 95–7 | date = March 1994 | pmid = 8172650 | doi = 10.1016/0167-5699(94)90148-1 }}
*{{cite journal | author=Guse AH |title=Cyclic ADP-ribose: a novel Ca2+-mobilising second messenger |journal=Cell. Signal. |volume=11 |issue= 5 |pages= 309–16 |year= 1999 |pmid= 10376802 |doi=10.1016/S0898-6568(99)00004-2 }}
* {{cite journal | vauthors = Guse AH | title = Cyclic ADP-ribose: a novel Ca2+-mobilising second messenger | journal = Cellular Signalling | volume = 11 | issue = 5 | pages = 309–16 | date = May 1999 | pmid = 10376802 | doi = 10.1016/S0898-6568(99)00004-2 }}
*{{cite journal | vauthors=Funaro A, Malavasi F |title=Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker |journal=J. Biol. Regul. Homeost. Agents |volume=13 |issue= 1 |pages= 54–61 |year= 1999 |pmid= 10432444 |doi=  }}
* {{cite journal | vauthors = Funaro A, Malavasi F | title = Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker | journal = Journal of Biological Regulators and Homeostatic Agents | volume = 13 | issue = 1 | pages = 54–61 | year = 1999 | pmid = 10432444 | doi =  }}
*{{cite journal | vauthors=Mallone R, Perin PC |title=Anti-CD38 autoantibodies in type? diabetes |journal=Diabetes Metab. Res. Rev. |volume=22 |issue= 4 |pages= 284–94 |year= 2006 |pmid= 16544364 |doi= 10.1002/dmrr.626 | pmc=2763400 }}
* {{cite journal | vauthors = Mallone R, Perin PC | title = Anti-CD38 autoantibodies in type? diabetes | journal = Diabetes/Metabolism Research and Reviews | volume = 22 | issue = 4 | pages = 284–94 | year = 2006 | pmid = 16544364 | pmc = 2763400 | doi = 10.1002/dmrr.626 }}
*{{cite journal | vauthors=Partidá-Sánchez S, Rivero-Nava L, Shi G, Lund FE |title=CD38: an ecto-enzyme at the crossroads of innate and adaptive immune responses |journal=Adv. Exp. Med. Biol. |volume=590 |issue=  |pages= 171–83 |year= 2007 |pmid= 17191385 |doi=10.1007/978-0-387-34814-8_12 | series=Advances in Experimental Medicine and Biology  | isbn=978-0-387-34813-1 }}
* {{cite journal | vauthors = Partidá-Sánchez S, Rivero-Nava L, Shi G, Lund FE | title = CD38: an ecto-enzyme at the crossroads of innate and adaptive immune responses | journal = Advances in Experimental Medicine and Biology | volume = 590 | issue =  | pages = 171–83 | year = 2007 | pmid = 17191385 | doi = 10.1007/978-0-387-34814-8_12 | isbn = 978-0-387-34813-1 | series = Advances in Experimental Medicine and Biology }}
*{{cite journal | vauthors=Jackson DG, Bell JI |title=Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation |journal=J. Immunol. |volume=144 |issue= 7 |pages= 2811–5 |year= 1990 |pmid= 2319135 |doi=  }}
* {{cite journal | vauthors = Jackson DG, Bell JI | title = Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation | journal = Journal of Immunology | volume = 144 | issue = 7 | pages = 2811–5 | date = April 1990 | pmid = 2319135 | doi =  }}
*{{cite journal | vauthors=Dianzani U, Bragardo M, Buonfiglio D |title=Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120 |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1306–11 |year= 1995 |pmid= 7539755 |doi=10.1002/eji.1830250526 |display-authors=etal}}
* {{cite journal | vauthors = Dianzani U, Bragardo M, Buonfiglio D, Redoglia V, Funaro A, Portoles P, Rojo J, Malavasi F, Pileri A | title = Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120 | journal = European Journal of Immunology | volume = 25 | issue = 5 | pages = 1306–11 | date = May 1995 | pmid = 7539755 | doi = 10.1002/eji.1830250526 }}
*{{cite journal | vauthors=Nakagawara K, Mori M, Takasawa S |title=Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15 |journal=Cytogenet. Cell Genet. |volume=69 |issue= 1–2 |pages= 38–9 |year= 1995 |pmid= 7835083 |doi=10.1159/000133933 |display-authors=etal}}
* {{cite journal | vauthors = Nakagawara K, Mori M, Takasawa S, Nata K, Takamura T, Berlova A, Tohgo A, Karasawa T, Yonekura H, Takeuchi T | title = Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15 | journal = Cytogenetics and Cell Genetics | volume = 69 | issue = 1–2 | pages = 38–9 | year = 1995 | pmid = 7835083 | doi = 10.1159/000133933 }}
*{{cite journal | vauthors=Tohgo A, Takasawa S, Noguchi N |title=Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38 |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 28555–7 |year= 1994 |pmid= 7961800 |doi=  |display-authors=etal}}
* {{cite journal | vauthors = Tohgo A, Takasawa S, Noguchi N, Koguma T, Nata K, Sugimoto T, Furuya Y, Yonekura H, Okamoto H | title = Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38 | journal = The Journal of Biological Chemistry | volume = 269 | issue = 46 | pages = 28555–7 | date = November 1994 | pmid = 7961800 | doi =  }}
*{{cite journal | vauthors=Takasawa S, Tohgo A, Noguchi N |title=Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26052–4 |year= 1994 |pmid= 8253715 |doi=  |display-authors=etal}}
* {{cite journal | vauthors = Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, Yonekura H, Okamoto H | title = Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP | journal = The Journal of Biological Chemistry | volume = 268 | issue = 35 | pages = 26052–4 | date = December 1993 | pmid = 8253715 | doi =  }}
*{{cite journal | vauthors=Nata K, Takamura T, Karasawa T |title=Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing |journal=Gene |volume=186 |issue= 2 |pages= 285–92 |year= 1997 |pmid= 9074508 |doi=10.1016/S0378-1119(96)00723-8 |display-authors=etal}}
* {{cite journal | vauthors = Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H | title = Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing | journal = Gene | volume = 186 | issue = 2 | pages = 285–92 | date = February 1997 | pmid = 9074508 | doi = 10.1016/S0378-1119(96)00723-8 }}
*{{cite journal | vauthors=Feito MJ, Bragardo M, Buonfiglio D |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141–7 |year= 1997 |pmid= 9263011 |doi=10.1093/intimm/9.8.1141 |display-authors=etal}}
* {{cite journal | vauthors = Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U | title = gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules | journal = International Immunology | volume = 9 | issue = 8 | pages = 1141–7 | date = August 1997 | pmid = 9263011 | doi = 10.1093/intimm/9.8.1141 }}
*{{cite journal | vauthors=Ferrero E, Malavasi F |title=Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase |journal=J. Immunol. |volume=159 |issue= 8 |pages= 3858–65 |year= 1997 |pmid= 9378973 |doi=  }}
* {{cite journal | vauthors = Ferrero E, Malavasi F | title = Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase | journal = Journal of Immunology | volume = 159 | issue = 8 | pages = 3858–65 | date = October 1997 | pmid = 9378973 | doi =  }}
*{{cite journal | vauthors=Deaglio S, Morra M, Mallone R |title=Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member |journal=J. Immunol. |volume=160 |issue= 1 |pages= 395–402 |year= 1998 |pmid= 9551996 |doi=  |display-authors=etal}}
* {{cite journal | vauthors = Deaglio S, Morra M, Mallone R, Ausiello CM, Prager E, Garbarino G, Dianzani U, Stockinger H, Malavasi F | title = Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member | journal = Journal of Immunology | volume = 160 | issue = 1 | pages = 395–402 | date = January 1998 | pmid = 9551996 | doi =  }}
*{{cite journal | vauthors=Yagui K, Shimada F, Mimura M |title=A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro |journal=Diabetologia |volume=41 |issue= 9 |pages= 1024–8 |year= 1998 |pmid= 9754820 |doi=10.1007/s001250051026 |display-authors=etal}}
* {{cite journal | vauthors = Yagui K, Shimada F, Mimura M, Hashimoto N, Suzuki Y, Tokuyama Y, Nata K, Tohgo A, Ikehata F, Takasawa S, Okamoto H, Makino H, Saito Y, Kanatsuka A | title = A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro | journal = Diabetologia | volume = 41 | issue = 9 | pages = 1024–8 | date = September 1998 | pmid = 9754820 | doi = 10.1007/s001250051026 }}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|CD38+Antigens}}
* {{MeshName|CD38+Antigens}}
* {{UCSC gene info|CD38}}
* {{UCSC gene info|CD38}}
* GeneCard CD38 [http://www.genecards.org/cgi-bin/carddisp.pl?gene=CD38]
* GeneCard CD38 [https://www.genecards.org/cgi-bin/carddisp.pl?gene=CD38]


{{PDB Gallery|geneid=952}}
{{PDB Gallery|geneid=952}}

Latest revision as of 11:56, 10 January 2019

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
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CD38 (cluster of differentiation 38), also known as cyclic ADP ribose hydrolase is a glycoprotein[1] found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. CD38 also functions in cell adhesion, signal transduction and calcium signaling.[2]

In humans, the CD38 protein is encoded by the CD38 gene which is located on chromosome 4.[3][4]

Function

CD38 is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP-ribose in addition to synthesis of NAADP from NADP+.[5] These reaction products are essential for the regulation of intracellular Ca2+.[6]

Clinical significance

The loss of CD38 function is associated with impaired immune responses, metabolic disturbances, and behavioral modifications including social amnesia possibly related to autism.[6][7]

The CD38 protein is a marker of cell activation. It has been connected to HIV infection, leukemias, myelomas, solid tumors, type II diabetes mellitus and bone metabolism, as well as some genetically determined conditions.

CD38 produces an enzyme which regulates the release of oxytocin within the central nervous system.[7]

Daratumumab which targets CD38 has been used in treating multiple myeloma.[8][9]

Increased expression of CD 38 is an unfavourable diagnostic marker in chronic lymphocytic leukemia and is associated with increased disease progression.[10]

Application

CD38 has been used as a prognostic marker in leukemia.[11] CD38 is also used as a target for daratumumab (Darzalex), a medicine that has been approved for the treatment of multiple myeloma.

The use of Daratumumab can interfere with pre-Blood transfusion tests, as CD38 is weakly expressed on the surface of erythrocytes. Thus, a screening assay for irregular antibodies against red blood cell antigens or a direct immunoglobulin test can produce false-positive results.[12] This can be sidelined by either pretreatment of the erythrocytes with dithiothreitol (DTT) or by using an anti-CD38 antibody neutralizing agent, e.g. DaraEx.

Animal studies

A gradual increase in CD38 has been implicated in the decline of NAD+ with age.[13][14] Treatment of old mice with a specific CD38 inhibitor, 78c, prevents age-related NAD+ decline.[15]

References

  1. ↑ Orciani M, Trubiani O, Guarnieri S, Ferrero E, Di Primio R (October 2008). "CD38 is constitutively expressed in the nucleus of human hematopoietic cells". Journal of Cellular Biochemistry. 105 (3): 905–12. doi:10.1002/jcb.21887. PMID 18759251.
  2. ↑ "Entrez Gene: CD38 CD38 molecule".
  3. ↑ Jackson DG, Bell JI (April 1990). "Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation". Journal of Immunology. 144 (7): 2811–5. PMID 2319135.
  4. ↑ Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H (February 1997). "Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing". Gene. 186 (2): 285–92. doi:10.1016/S0378-1119(96)00723-8. PMID 9074508.
  5. ↑ Chini EN, Chini CC, Kato I, Takasawa S, Okamoto H (February 2002). "CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues". The Biochemical Journal. 362 (Pt 1): 125–30. PMC 1222368. PMID 11829748.
  6. ↑ 6.0 6.1 Malavasi F, Deaglio S, Funaro A, Ferrero E, Horenstein AL, Ortolan E, Vaisitti T, Aydin S (July 2008). "Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology". Physiological Reviews. 88 (3): 841–86. doi:10.1152/physrev.00035.2007. PMID 18626062.
  7. ↑ 7.0 7.1 Higashida H, Yokoyama S, Huang JJ, Liu L, Ma WJ, Akther S, Higashida C, Kikuchi M, Minabe Y, Munesue T (November 2012). "Social memory, amnesia, and autism: brain oxytocin secretion is regulated by NAD+ metabolites and single nucleotide polymorphisms of CD38" (Submitted manuscript). Neurochemistry International. 61 (6): 828–38. doi:10.1016/j.neuint.2012.01.030. PMID 22366648.
  8. ↑ McKeage K (February 2016). "Daratumumab: First Global Approval". Drugs. 76 (2): 275–81. doi:10.1007/s40265-015-0536-1. PMID 26729183.
  9. ↑ Xia C, Ribeiro M, Scott S, Lonial S (October 2016). "Daratumumab: monoclonal antibody therapy to treat multiple myeloma". Drugs of Today. 52 (10): 551–560. doi:10.1358/dot.2016.52.10.2543308. PMID 27910963.
  10. ↑ Burgler S (2015). "Role of CD38 Expression in Diagnosis and Pathogenesis of Chronic Lymphocytic Leukemia and Its Potential as Therapeutic Target". Critical Reviews in Immunology. 35 (5): 417–32. doi:10.1615/CritRevImmunol.v35.i5.50. PMID 26853852.
  11. ↑ Deaglio S, Mehta K, Malavasi F (January 2001). "Human CD38: a (r)evolutionary story of enzymes and receptors". Leukemia Research. 25 (1): 1–12. doi:10.1016/S0145-2126(00)00093-X. PMID 11137554.
  12. ↑ de Vooght KM, Lozano M, Bueno JL, Alarcon A, Romera I, Suzuki K, Zhiburt E, Holbro A, Infanti L, Buser A, Hustinx H, Deneys V, Frelik A, Thiry C, Murphy M, Staves J, Selleng K, Greinacher A, Kutner JM, Bonet Bub C, Castilho L, Kaufman R, Colling ME, Perseghin P, Incontri A, Dassi M, Brilhante D, Macedo A, Cserti-Gazdewich C, Pendergrast JM, Hawes J, Lundgren MN, Storry JR, Jain A, Marwaha N, Sharma RR (May 2018). "Vox Sanguinis International Forum on typing and matching strategies in patients on anti-CD38 monoclonal therapy: summary". Vox Sanguinis. 113 (5): 492–498. doi:10.1111/vox.12653. PMID 29781081.
  13. ↑ Camacho-Pereira J, Tarragó MG, Chini CC, Nin V, Escande C, Warner GM, Puranik AS, Schoon RA, Reid JM, Galina A, Chini EN (June 2016). "CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism". Cell Metabolism. 23 (6): 1127–1139. doi:10.1016/j.cmet.2016.05.006. PMC 4911708. PMID 27304511.
  14. ↑ Schultz MB, Sinclair DA (June 2016). "Why NAD(+) Declines during Aging: It's Destroyed". Cell Metabolism. 23 (6): 965–966. doi:10.1016/j.cmet.2016.05.022. PMC 5088772. PMID 27304496.
  15. ↑ Tarragó MG, Chini CC, Kanamori KS, Warner GM, Caride A, de Oliveira GC, Rud M, Samani A, Hein KZ, Huang R, Jurk D, Cho DS, Boslett JJ, Miller JD, Zweier JL, Passos JF, Doles JD, Becherer DJ, Chini EN (May 2018). "+ Decline". Cell Metabolism. 27 (5): 1081–1095.e10. doi:10.1016/j.cmet.2018.03.016. PMC 5935140. PMID 29719225.

Further reading

  • States DJ, Walseth TF, Lee HC (December 1992). "Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38". Trends in Biochemical Sciences. 17 (12): 495. doi:10.1016/0968-0004(92)90337-9. PMID 1471258.
  • Malavasi F, Funaro A, Roggero S, Horenstein A, Calosso L, Mehta K (March 1994). "Human CD38: a glycoprotein in search of a function". Immunology Today. 15 (3): 95–7. doi:10.1016/0167-5699(94)90148-1. PMID 8172650.
  • Guse AH (May 1999). "Cyclic ADP-ribose: a novel Ca2+-mobilising second messenger". Cellular Signalling. 11 (5): 309–16. doi:10.1016/S0898-6568(99)00004-2. PMID 10376802.
  • Funaro A, Malavasi F (1999). "Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker". Journal of Biological Regulators and Homeostatic Agents. 13 (1): 54–61. PMID 10432444.
  • Mallone R, Perin PC (2006). "Anti-CD38 autoantibodies in type? diabetes". Diabetes/Metabolism Research and Reviews. 22 (4): 284–94. doi:10.1002/dmrr.626. PMC 2763400. PMID 16544364.
  • Partidá-Sánchez S, Rivero-Nava L, Shi G, Lund FE (2007). "CD38: an ecto-enzyme at the crossroads of innate and adaptive immune responses". Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology. 590: 171–83. doi:10.1007/978-0-387-34814-8_12. ISBN 978-0-387-34813-1. PMID 17191385.
  • Jackson DG, Bell JI (April 1990). "Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation". Journal of Immunology. 144 (7): 2811–5. PMID 2319135.
  • Dianzani U, Bragardo M, Buonfiglio D, Redoglia V, Funaro A, Portoles P, Rojo J, Malavasi F, Pileri A (May 1995). "Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120". European Journal of Immunology. 25 (5): 1306–11. doi:10.1002/eji.1830250526. PMID 7539755.
  • Nakagawara K, Mori M, Takasawa S, Nata K, Takamura T, Berlova A, Tohgo A, Karasawa T, Yonekura H, Takeuchi T (1995). "Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15". Cytogenetics and Cell Genetics. 69 (1–2): 38–9. doi:10.1159/000133933. PMID 7835083.
  • Tohgo A, Takasawa S, Noguchi N, Koguma T, Nata K, Sugimoto T, Furuya Y, Yonekura H, Okamoto H (November 1994). "Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38". The Journal of Biological Chemistry. 269 (46): 28555–7. PMID 7961800.
  • Takasawa S, Tohgo A, Noguchi N, Koguma T, Nata K, Sugimoto T, Yonekura H, Okamoto H (December 1993). "Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP". The Journal of Biological Chemistry. 268 (35): 26052–4. PMID 8253715.
  • Nata K, Takamura T, Karasawa T, Kumagai T, Hashioka W, Tohgo A, Yonekura H, Takasawa S, Nakamura S, Okamoto H (February 1997). "Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing". Gene. 186 (2): 285–92. doi:10.1016/S0378-1119(96)00723-8. PMID 9074508.
  • Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U (August 1997). "gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules". International Immunology. 9 (8): 1141–7. doi:10.1093/intimm/9.8.1141. PMID 9263011.
  • Ferrero E, Malavasi F (October 1997). "Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase". Journal of Immunology. 159 (8): 3858–65. PMID 9378973.
  • Deaglio S, Morra M, Mallone R, Ausiello CM, Prager E, Garbarino G, Dianzani U, Stockinger H, Malavasi F (January 1998). "Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member". Journal of Immunology. 160 (1): 395–402. PMID 9551996.
  • Yagui K, Shimada F, Mimura M, Hashimoto N, Suzuki Y, Tokuyama Y, Nata K, Tohgo A, Ikehata F, Takasawa S, Okamoto H, Makino H, Saito Y, Kanatsuka A (September 1998). "A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro". Diabetologia. 41 (9): 1024–8. doi:10.1007/s001250051026. PMID 9754820.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=CD38&oldid=1526103"