Human BST-1 Expressed on Myeloid Cells Functions as a Receptor Molecule

Okuyama, Yoshiki; Ishihara, Katsuhiko; Kimura, Naoki; Hirata, Yoshihiro; Sato, Keita; Itoh, Motoyuki; Ok, Lee Byung; Hirano, Toshio

doi:10.1006/bbrc.1996.1741

Cited by 50 publications

(48 citation statements)

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“…These effects can be attributed to the ability of CD157 to act as a receptor (29,33,34). However, the nature of the physiological interaction(s) implementing these multiple biological activities remained an unresolved issue.…”

Section: Discussionmentioning

confidence: 99%

“…Signals-In addition to its activity in promoting cell adhesion and migration (8), CD157 cross-linking by specific mAbs has been shown to elicit a signaling cascade that involves the phosphorylation of FAK (14,29,30). Moreover, CD157 is part of the integrin-driven molecular machinery that regulates fundamental functions in neutrophils and monocytes through the activation of a complex signaling network (10,11).…”

Section: Cd157-fibronectin Interaction Modulates the Transduction Of mentioning

confidence: 99%

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Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

Morone¹,

Augeri²,

Cuccioloni

et al. 2014

Journal of Biological Chemistry

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Background: Surface CD157 modulates leukocyte and ovarian cancer cell adhesion and migration through the interaction with an unknown ligand. Results: CD157 binds heparin-binding domains of numerous extracellular matrix proteins with high affinity. Conclusion:The interaction of CD157 with extracellular matrix proteins is instrumental in the regulation of cell adhesion. Significance: These findings provide valuable insights into the biological mechanism responsible for the nonenzymatic functions of CD157.

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Section: Discussionmentioning

confidence: 99%

Section: Cd157-fibronectin Interaction Modulates the Transduction Of mentioning

confidence: 99%

Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

Morone¹,

Augeri²,

Cuccioloni

et al. 2014

Journal of Biological Chemistry

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“…12,13 Such negative characteristics are even more evident in CD157, the other member of the protein family, whose signaling features are known, notwithstanding a glycophosphatidylinositol linkage to the cell membrane. 14,15 Some clues can be extrapolated from cocapping experiments, which show that CD38 associates on the cell membrane with professional signaling receptors such as the T-cell receptor (TCR)-CD3 complex in T cells, the B-cell receptor (BCR) in B cells, and CD16 in NK cells. 16 A hypothesis to explain the signaling properties of CD38 is that the molecule exploits the signaling machinery of professional receptors to deliver its own independent signals.…”

Section: Introductionmentioning

confidence: 99%

Human CD38 and CD16 are functionally dependent and physically associated in natural killer cells

Deaglio

Zubiaur²,

Gregorini³

et al. 2002

Blood

105

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IntroductionHuman CD38 is the prototype of a family of proteins that share structural similarities and ectoenzymatic activities involved in the production of calcium-mobilizing compounds. [1][2][3] Aside from its ectoenzymatic activities and, apparently with independent modalities, CD38 may perform as a receptor, ruling adhesion and signaling in T 4 and B lymphocytes, 5 monocytes, 6 and natural killer (NK) cells. 7,8 The receptor functions of CD38 are regulated through interaction with a counterreceptor, identified as CD31. 9 The signaling events initiated by interactions between CD38 and CD31 (and fully mimicked by agonistic anti-CD38 monoclonal antibodies [mAbs]) were initially studied in the dynamic context of circulating CD38 ϩ T lymphocytes adhering to CD31 ϩ endothelial cells. 10 Use of this model allowed definition of some of the events that take place after the interaction and that include calcium (Ca ϩϩ ) mobilization from cytosolic stores, tyrosine phosphorylation of selected substrates, activation of nuclear factors, and secretion of cytokines. 11 It is generally agreed that CD38 controls a specific signaling pathway in T cells, B cells, NK cells, and monocytes. In spite of this evidence, the modalities through which the signal is initiated remain elusive. The molecule has neither the canonical structure of a receptor nor the hallmark domains. Indeed, the cytoplasmic tail is short and lacks docking sites and it is not tyrosine phosphorylated on activation. 12,13 Such negative characteristics are even more evident in CD157, the other member of the protein family, whose signaling features are known, notwithstanding a glycophosphatidylinositol linkage to the cell membrane. 14,15 Some clues can be extrapolated from cocapping experiments, which show that CD38 associates on the cell membrane with professional signaling receptors such as the T-cell receptor (TCR)-CD3 complex in T cells, the B-cell receptor (BCR) in B cells, and CD16 in NK cells. 16 A hypothesis to explain the signaling properties of CD38 is that the molecule exploits the signaling machinery of professional receptors to deliver its own independent signals. This idea was first supported by experiments using CD38 ϩ T-cell lines deficient in components of the signaling apparatus of the TCR-CD3 complex. 17,18 The inability of CD38 to signal in these cells was overcome by reconstituting a complete TCR-CD3 complex, thereby indicating that CD38 signaling depends on the presence of a functional TCR. These observations were recently expanded by studies using T lymphocytes purified from the intestinal The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked ''advertisement'' in accordance with 18 U.S.C. section 1734. For personal use only. on May 11, 2018. by guest www.bloodjournal.org From lamina propria as a model in which the TCR complex is physiologically impaired. 19 A comparative analysis of circulating versus residential T lymphocytes from the s...

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“…1 The CD157 and CD38 molecules are pleiotropic in function, acting both as ectoenzymes and receptors. [2][3][4] CD157 is abundantly expressed by myeloid lineage from precursors to differentiated stages 5 by bone marrow stromal cells, synovial cells, endothelial cells, and other cell types. 6 Functional analysis by means of agonistic monoclonal antibodies (mAbs) mimicking natural ligand(s) suggested that CD157 could act as a receptor with signal transduction capacity.…”

mentioning

confidence: 99%

CD157 is an important mediator of neutrophil adhesion and migration

Funaro¹,

Ortolan²,

Ferranti³

et al. 2004

Blood

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CD157, a glycosylphosphatidylinositol (GPI)-anchored protein encoded by a member of the CD38 NADase/ADP-ribosyl cyclase gene family, is expressed on the surface of most human circulating neutrophils. This work demonstrates that CD157 is a receptor that induces reorganization of the cytoskeleton and significant changes in cell shape, and that signals mediated by CD157 act through modulation of cytosolic Ca 2؉ concentration. These signals are independent of the products of CD157's enzymatic activities (ie, cyclic adenosine diphosphate [ADP]-ribose and ADP-ribose). Indeed, the enzymatic activities of CD157 in circulating neutrophils as well as in dimethyl sulfoxide (DMSO)-differentiated (CD157 ؉ / CD38 ؊ ) HL-60 cells, are hardly detectable. This work also shows that the receptorial activity relies on cross-talk between CD157 and ␤ 2 integrin. CD157 localizes in GM1-enriched lipid rafts and, upon activation, it migrates to the uropod, a structure specialized in motility and adhesive functions. Indeed, CD157 is involved in adhesion to extracellular matrix proteins and in chemotaxis induced in vitro by formylmethionyl-leucyl-phenylalanine (fMLP). These findings were consistent with the results obtained in neutrophils from patients with paroxysmal nocturnal hemoglobinuria (PNH), in which CD157 is deficient. These neutrophils showed constant defects in adhesion and migration. Our data attribute specific and crucial roles to CD157 in the regulation of innate immunity during inflammation. IntroductionHuman CD157 is a glycosylphosphatidylinositol (GPI)-linked glycoprotein encoded by a member of the NADase/adenosine diphosphate (ADP)-ribosyl cyclase gene family, which also includes CD38. 1 The CD157 and CD38 molecules are pleiotropic in function, acting both as ectoenzymes and receptors. [2][3][4] CD157 is abundantly expressed by myeloid lineage from precursors to differentiated stages 5 by bone marrow stromal cells, synovial cells, endothelial cells, and other cell types. 6 Functional analysis by means of agonistic monoclonal antibodies (mAbs) mimicking natural ligand(s) suggested that CD157 could act as a receptor with signal transduction capacity. However, as CD157 lacks a cytoplasmic domain, it must associate with some "conventional" receptor(s) to transduce signals; much in the same way as CD38, which has a short intracellular domain, CD157 acts as a parasite on specific receptors to compensate for its structural ineptitude to exert receptorial functions. 7,8 In concert with monocytes and tissue macrophages, neutrophils carry out many of the major functional responses of the innate immune system. They participate in inflammatory responses, such as host resistance to infection, and in detrimental host inflammatory reactions, including arthritis, septic shock, stroke, and transplantation rejection. The regulation of neutrophil recruitment into the inflammatory sites and neutrophil clearance are critical processes assuring effective host defense without tissue injury. Neutrophil extravasation is a multistep process depe...

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Human BST-1 Expressed on Myeloid Cells Functions as a Receptor Molecule

Cited by 50 publications

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Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

Binding of CD157 Protein to Fibronectin Regulates Cell Adhesion and Spreading

Human CD38 and CD16 are functionally dependent and physically associated in natural killer cells

CD157 is an important mediator of neutrophil adhesion and migration

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