A Regulatory Role for CD37 in T Cell Proliferation

Spriel, Annemiek B. van; Puls, Kirsten L.; Sofi, Mariam; Pouniotis, Dodie; Hochrein, Hubertus; Orinska, Zane; Knobeloch, Klaus–Peter; Plebanski, Magdalena; Wright, Mark D.

doi:10.4049/jimmunol.172.5.2953

Cited by 120 publications

(93 citation statements)

References 42 publications

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“…45 It is surprising that mice defective for the tetraspanin CD151, which also directly associates with a3b1 and a6b1 integrin, show normal fertility but decreased blood coagulation and hyperproliferative T lymphocytes. 43 This latter phenotype can also be observed in knockout mice for the tetraspanins CD37, 48 Tssc6 49 and CD81. 50 Taken together, these published results suggest that tetraspanin family members can have complementary or partially overlapping roles in different physiological processes or that they merely facilitate physiological processes by enabling the interaction between essential protein components.…”

Section: Discussionmentioning

confidence: 88%

Reduced body weight in male Tspan8-deficient mice

et al. 2010

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Objective: The gene TSPAN8 was recently identified in a genome-wide association study as the most likely causal gene in a locus that was correlated with the risk of type 2 diabetes (T2D) in northern European individuals. To assess whether Tspan8 is the actual T2D-causal gene in this locus, we ablated its expression in mice and determined the consequences of this ablation on a multitude of metabolic traits. Results: We found that genetic ablation of Tspan8 in mice results in a reduction (À15.6%) in the body weight of males fed a normal chow diet and that this deficiency results in a resistance to body weight gain (À13.7%) upon feeding a high fat and high carbohydrate diet. The differences in body weight could only be detected in male mice and were the consequence of both a decrease in fat deposition, and a decrease in lean body mass (16.9 and 11%, respectively). In spite of the significant body weight difference, no changes in fasting insulin and glucose levels could be detected in Tspan8 knockout mice, nor could we identify changes in the clearance of glucose or sensitivity to insulin in oral glucose tolerance test and intraperitoneal insulin sensitivity test studies, respectively. In addition, male Tspan8 knockout mice showed significantly lower bone mineral density and phosphorus levels (6.2 and 16.6%, respectively). Expression of Tspan8 in mouse was highest in digestive tissues, but virtually absent from the pancreas. In contrast, expression of human TSPAN8 was substantial in digestive tissues, as well as pancreatic cells. Conclusions: Our results argue for a role for Tspan8 in body-weight regulation in males, but do not show differences in T2D-associated traits that were anticipated from previous human genome-wide association studies. Differences in Tspan8 expression levels in mouse and human tissues suggest that Tspan8 could fulfill different or additional physiological functions in these organisms.

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Section: Discussionmentioning

confidence: 88%

Reduced body weight in male Tspan8-deficient mice

et al. 2010

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“…Overexpression of the Pointed-P1 transcript induced a significant increase in plasmatocyte numbers, whereas overexpression of a constitutive active form of the inhibitor Anterior open induces lamellocyte formation. Interestingly, in mice, knocking down tetraspanins has been shown to induce lymphocyte proliferation (22). Sinenko et al (23) showed that in Drosophila loss of at least one tetraspanin, tetraspanin68c (tsp68c), was sufficient to induce overproliferation of larval hemocytes.…”

Section: Hemopoiesis and Cell Differentiationmentioning

confidence: 99%

Drosophila Hemopoiesis and Cellular Immunity

Williams

2007

The Journal of Immunology

272

197

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In Drosophila melanogaster larvae, three classes of circulating cellular immune surveillance cells (hemocytes) can be identified: plasmatocytes, crystal cells, and lamellocytes. Plasmatocytes are professional phagocytes most similar to the mammalian monocyte/macrophage lineage and make up ∼95% of circulating hemocytes. The other ∼5% of circulating hemocytes consists of crystal cells, which secrete components necessary for the melanization of invading organisms, as well as for wound repair. A third cell type known as lamellocytes are rarely seen in healthy larvae and are involved in the encapsulation of invading pathogens. There are no obvious mammalian counterparts for crystal cells or lamellocytes, and there is no equivalent to the lymphoid lineage in insects. In this review, I will discuss what is currently known about Drosophila hemopoiesis and the cellular immune response and where possible compare it to vertebrate mechanisms.

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“…Moreover, CD37 is a target for novel immunotherapies to treat B cell malignancies (12)(13)(14)(15)(16)(17)(18). CD37 has also been shown to control functions in T cells and dendritic cells (19)(20)(21)(22). Notably, we recently demonstrated that CD37 promotes migration of dendritic cells (23).…”

mentioning

confidence: 99%

Tetraspanin CD37 Regulates β2 Integrin–Mediated Adhesion and Migration in Neutrophils

Wee

Schulze

Jones

et al. 2015

The Journal of Immunology

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Deciphering the molecular basis of leukocyte recruitment is critical to the understanding of inflammation. In this study, we investigated the contribution of the tetraspanin CD37 to this key process. CD37-deficient mice showed impaired neutrophil recruitment in a peritonitis model. Intravital microscopic analysis indicated that the absence of CD37 impaired the capacity of leukocytes to follow a CXCL1 chemotactic gradient accurately in the interstitium. Moreover, analysis of CXCL1-induced leukocyte-endothelial cell interactions in postcapillary venules revealed that CXCL1-induced neutrophil adhesion and transmigration were reduced in the absence of CD37, consistent with a reduced capacity to undergo β2 integrin–dependent adhesion. This result was supported by in vitro flow chamber experiments that demonstrated an impairment in adhesion of CD37-deficient neutrophils to the β2 integrin ligand, ICAM-1, despite the normal display of high-affinity β2 integrins. Superresolution microscopic assessment of localization of CD37 and CD18 in ICAM-1–adherent neutrophils demonstrated that these molecules do not significantly cocluster in the cell membrane, arguing against the possibility that CD37 regulates β2 integrin function via a direct molecular interaction. Moreover, CD37 ablation did not affect β2 integrin clustering. In contrast, the absence of CD37 in neutrophils impaired actin polymerization, cell spreading and polarization, dysregulated Rac-1 activation, and accelerated β2 integrin internalization. Together, these data indicate that CD37 promotes neutrophil adhesion and recruitment via the promotion of cytoskeletal function downstream of integrin-mediated adhesion.

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A Regulatory Role for CD37 in T Cell Proliferation

Cited by 120 publications

References 42 publications

Reduced body weight in male Tspan8-deficient mice

Reduced body weight in male Tspan8-deficient mice

Drosophila Hemopoiesis and Cellular Immunity

Tetraspanin CD37 Regulates β2 Integrin–Mediated Adhesion and Migration in Neutrophils

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