Polymorphism R62W results in resistance of CD23 to enzymatic cleavage in cultured cells

Jf, Meng; McFall, Chris; Lj, Rosenwasser

doi:10.1038/sj.gene.6364376

Cited by 19 publications

(27 citation statements)

References 40 publications

(44 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…An additional mutation that may reduce the cleavage of CD23 (R64W) has been reported recently in the human system [48]. This mutation has been associated with enhanced T-cell responses to antigen in allergic subjects.…”

Section: Mutations In Cd23mentioning

confidence: 98%

CD23: An overlooked regulator of allergic disease

Conrad

Ford²,

Sturgill³

et al. 2007

Curr Allergy Asthma Rep

View full text Add to dashboard Cite

Given the importance of immunoglobulin (Ig) E in mediating type I hypersensitivity, inhibiting IgE production would be a general way of controlling allergic disease. The low-affinity IgE receptor (FceRII or CD23) has long been proposed to be a natural regulator of IgE synthesis. In vivo research supporting this concept includes the observation that mice lacking CD23 have increased IgE production whereas mice overexpressing CD23 show strongly suppressed IgE responses. In addition, the finding that mice injected with monoclonal antibody directed against the coiled-coil stalk of CD23 have enhanced soluble CD23 release and increased IgE production demonstrates that full-length, trimeric CD23 is responsible for initiating an IgE inhibitory signal. The recent identification of ADAM10 (a disintegrin and metalloprotease) as the CD23 metalloprotease provides an alternative approach for designing therapies to combat allergic disease. Current data suggest that stabilizing cell-surface CD23 would be a natural means to decrease IgE synthesis and thus control type I hypersensitivity.

show abstract

Section: Mutations In Cd23mentioning

confidence: 98%

CD23: An overlooked regulator of allergic disease

Conrad

Ford²,

Sturgill³

et al. 2007

Curr Allergy Asthma Rep

View full text Add to dashboard Cite

show abstract

“…We also briefly discuss the roles of two other well-studied ADAMs: ADAM19, which is implicated in, amongst other processes, heart development and remyelination processes in the peripheral nervous system; and ADAM33, which is implicated in airway inflammation. Buxbaum et al, 1998;Peschon et al, 1998;Brou et al, 2000;Hansen et al, 2000;Reddy et al, 2000;Franzke et al, 2002;Contin et al, 2003;Garton et al, 2003;Nagano et al, 2004;Sahin et al, 2004;Fabre-Lafay et al, 2005;Horiuchi et al, 2005;Lambert et al, 2005;Maretzky et al, 2005b;Bech-Serra et al, 2006;Tsakadze et al, 2006;Chalaris et al, 2007;Dyczynska et al, 2007;Li et al, 2007;Sahin and Blobel, 2007 CD23, Kit ligand-1 (Zou et al, 2005;Meng et al, 2007) …”

Section: Revealing the Role Of Adam Proteases In Nonmammalian Modelsmentioning

confidence: 99%

“…However, genetic studies in human patients led to contradictory results (Raby et al, 2004; Blakey et al, 2009; Jie et al, 2011;Miyake et al, 2012) and ADAM33-deficient mice did not display phenotypical differences when assessed in established models of airway inflammation (Chen et al, 2006). Nevertheless, cellbased studies revealed a putative role for ADAM33 as an ectodomain sheddase for the IgE receptor CD23, which is a key player during allergic reactions (Weskamp et al, 2006;Meng et al, 2007). Transgenic ADAM33 mice might be useful for solving this question in the future.…”

mentioning

confidence: 99%

Ectodomain shedding and ADAMs in development

Weber¹,

2012

View full text Add to dashboard Cite

SummaryProteolytic enzymes belonging to the A Disintegin And Metalloproteinase (ADAM) family are able to cleave transmembrane proteins close to the cell surface, in a process referred to as ectodomain shedding. Substrates for ADAMs include growth factors, cytokines, chemokines and adhesion molecules, and, as such, many ADAM proteins play crucial roles in cell-cell adhesion, extracellular and intracellular signaling, cell differentiation and cell proliferation. In this Review, we summarize the fascinating roles of ADAMs in embryonic and adult tissue development in both vertebrates and invertebrates. Key words: ADAM, Notch, Ectodomain shedding, Cell fate determination, DifferentiationIntroduction Proteins belonging to the 'A Disintegrin And Metalloproteinase' (ADAM) family are membrane-anchored proteases that are able to cleave the extracellular domains of membrane-bound proteins in a process known as 'ectodomain shedding'. Typical substrates of ADAM proteases are growth factors, cytokines, chemokines and their receptors, as well as cell adhesion molecules and differentiation factors (Reiss and Saftig, 2009). ADAMs were initially discovered as novel type I transmembrane proteins with homology to snake venom integrin ligands and that played a functional role during guinea-pig sperm-egg fusion (Blobel et al., 1992). Subsequently, approximately half of the ADAM family members were predicted and then shown to possess zinc-dependent protease activity related to that exhibited by adamalysins metallopeptidases (Wolfsberg et al., 1993; Huxley-Jones et al., 2007). These active 'sheddases ' (ADAM8, 9, 10, 12, 15, 17, 19, 20, 21, 28, 30 and 33) share a typical consensus sequence (HEXGHXXGXXHD) that is present in zinc-binding proteases (Bode et al., 1993). So far, 40 family members have been identified in the mammalian genome (Puente and Lopez-Otin, 2004; Edwards et al., 2008), of which 37 are expressed in mice (most of them in a testis-specific manner) and 22 are thought to be expressed in humans (Table 1). In both mouse and human, intronless coding sequences probably representing pseudogenes (e.g. human ADAM5P and ADAM6) have also been described. The expression of ADAM or ADAM-related proteins has also been described in many different species, including the yeast Schizosaccharomyces pombe, the nematode worm Caenorhabditis elegans, the frog Xenopus laevis, the zebrafish Danio rerio and the fruitfly Drosophila melanogaster (Alfandari et al., 1997;Nakamura et al., 2004; Huxley-Jones et al., 2007; Iida et al., 2010). It was quickly realized that ADAMs are widely expressed and play fundamental roles during developmental processes, by regulating cell-cell and cell-matrix interactions and by modulating differentiation, migration, receptor-ligand signaling or repulsion (Becherer and Blobel, 2003).Following studies of the catalytically active ADAMs, ectodomain shedding emerged as a central biological event. This proteolytic process primarily affects type I and type II transmembrane proteins, although glycosylphosphatidylinisot...

show abstract

“…7 It is made up of a full-length molecule of 813 amino acids including 7 domains: pro-, metalloprotease, disintegrin, cysteine-rich, epidermal growth factor, transmembrane, and cytoplasmic, serving the functions of activation, proteolysis, adhesion, fusion, and signaling. 1 Since its discovery in 2002, ADAM33 has been extensively characterized at molecular and structural levels, [8][9][10][11][12] but its biological role and its contribution to asthma pathogenesis have remained elusive.…”

mentioning

confidence: 99%