ADAM family proteins in the immune system

Yamamoto, Shunsuke; Higuchi, Yasunori; Yoshiyama, Kazuhiro; Shimizu, Eiichi; Kataoka, Masashi; Hijiya, Naoki; Matsuura, Keiko

doi:10.1016/s0167-5699(99)01464-4

Cited by 127 publications

(103 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Adamdec1 is a novel member of the ADAM superfamily of metalloprotease genes [18]. Members of this family are involved in the immune response besides other biological processes [19]. Spi-C is a transcription factor that is temporarily expressed in developing B cells as well as in macrophages [20].…”

Section: Resultsmentioning

confidence: 99%

B‐1a cells are imprinted by the microenvironment in spleen and peritoneum

et al. 2007

View full text Add to dashboard Cite

B‐1a cells are found mainly in the peritoneal cavity of mice but are also present in the spleen. Gene expression profiling defined many genes differentially expressed in B‐1a cells from these two sites. To see whether this gene expression pattern was imprinted by the particular microenvironment, peritoneal or spleen cells from recombinant L2 mice mainly consisting of B‐1a cells were adoptively transferred into Rag1–/– mice. Re‐isolated peritoneal and splenic B‐1a cells were analyzed for expression of three indicator genes – vcam‐1, adamdec1 and spi‐c. The expression of these genes was up‐regulated in splenic and down‐regulated in peritoneal cells. This particular pattern was observed for peritoneal or splenic donor cells transferred either intraperitoneally or intravenously. Similar results were obtained when levels of surface IgM or frequencies of Mac‐1+ B‐1 cells were compared after transfer. This suggests that the environment induces the particular genetic program of B‐1a cells and argues against an independent ontogeny.

show abstract

Section: Resultsmentioning

confidence: 99%

B‐1a cells are imprinted by the microenvironment in spleen and peritoneum

et al. 2007

View full text Add to dashboard Cite

show abstract

“…MMPs, such as gelatinase B and collagenase, are mainly stored in the specific granules, whereas serine proteinases, such as elastase, proteinase 3 and cathepsin G, are located in azurophilic granules. Members of MMP family termed 'a disintegrin and metalloprotease' (ADAM) contain a large number of transmembrane proteins such as ADAM8 (CD156a), ADAM17 (CD156b; TNF-a-converting enzyme) and membrane type 4 MMPs [32,33]. Many members of the ADAM gene family have protease activity (called sheddase or secretase); other members may lack MMP activity and function as cell-adhesion proteins or fertilins [33].…”

Section: Discussionmentioning

confidence: 99%

Interaction of Human Immunoglobulin G with CD16 on Natural Killer Cells: Ligand Clearance, FcγRIIIA Turnover and Effects of Metalloproteinases on FcγRIIIA‐Mediated Binding, Signal Transduction and Killing‡

Moţa¹,

Moldovan²,

Călugăru³

et al. 2004

Scand J Immunol

View full text Add to dashboard Cite

Human natural killer (NK) cells express low-affinity Fc immunoglobulin G (IgG) receptor (FcgRIIIA/CD16). The binding of monomeric IgG (mIgG) and F(ab 0 ) 2 fragments of 3G8 anti-CD16 monoclonal antibody (mAb) to FcgRIIIA was investigated by flow cytometry. Over 90% of NK cells bound endogenous IgG, and during incubation at 37 C, the FcgRIIIA occupancy decreased slowly. Approximately 90% of NK cells bind mIgG or F(ab 0 ) 2 fragments of 3G8 anti-CD16 mAb. The calculated half-time (T 1/2 ) of in vitro mIgG dissociation from FcgRIIIA was 130 min. By cross-linking the mIgG ligand with F(ab 0 ) 2 fragments of anti-human IgG antibody, the T 1/2 decreases to 85 min. In kinetics study, it has been shown that 125 I-mIgG bound to FcgRIIIA is slowly released in the culture supernatant, maybe eluted at acid pH, or partially internalized and degraded. The binding of IgG to FcgRIIIA was increased by 53.8% on cells cultured in the presence of RU36156, a matrix metalloproteinase (MMP) inhibitor. Furthermore, an increase in phosphorylation of Lyn tyrosine kinase, after cross-linking of mIgG-FcgRIIIA complex, was observed on NK cells treated with RU36156. When the FcgRIIIA was occupied by mIgG, the capacity of NK cells to kill K562 target cells was decreased by RU36156, because the MMP inhibitor protects CD16 from proteolysis. Our data demonstrate that binding of mIgG to human NK cells is followed by ligand dissociation and/or internalization, enzymatic degradation and exocytosis. The RU36156 MMP inhibitor protects FcgRIIIA from cleavage, augments NK-cell activation and may interfere in their killing capacity.

show abstract

“…Unfortunately, CD62L is rapidly shed from the cell surface following TCR stimulation through cleavage by the TNF-␣-converting enzyme, thereby making analysis of stimulated populations of bulk or CD44 high CD8 ϩ T cells difficult (45)(46)(47). Therefore, CFSE-labeled CD8 ϩ T cells from LCMV-immune C57BL/6 mice were sorted into naive, T CM , or T EM populations based on CD8␣, CD44, and CD62L expression to Ͼ95% purity (Fig.…”

Section: Differential Responsiveness Of T CM and T Em Cd8 ϩ T Cells Tmentioning

confidence: 99%

IL-15 Transpresentation Augments CD8+ T Cell Activation and Is Required for Optimal Recall Responses by Central Memory CD8+ T Cells

Kokaji

Hockley

Kane

2008

The Journal of Immunology

View full text Add to dashboard Cite

Although the adaptive immune system has a remarkable ability to mount rapid recall responses to previously encountered pathogens, the cellular and molecular signals necessary for memory CD8+ T cell reactivation are poorly defined. IL-15 plays a critical role in memory CD8+ T cell survival; however, whether IL-15 is also involved in memory CD8+ T cell reactivation is presently unclear. Using artificial Ag-presenting surfaces prepared on cell-sized microspheres, we specifically addressed the role of IL-15 transpresentation on mouse CD8+ T cell activation in the complete absence of additional stimulatory signals. In this study we demonstrate that transpresented IL-15 is significantly more effective than soluble IL-15 in augmenting anti-CD3ε-induced proliferation and effector molecule expression by CD8+ T cells. Importantly, IL-15 transpresentation and TCR ligation by anti-CD3ε or peptide MHC complexes exhibited synergism in stimulating CD8+ T cell responses. In agreement with previous studies, we found that transpresented IL-15 preferentially stimulated memory phenotype CD8+ T cells; however, in pursuing this further, we found that central memory (TCM) and effector memory (TEM) CD8+ T cells responded differentially to transpresented IL-15. TCM CD8+ T cells undergo Ag-independent proliferation in response to transpresented IL-15 alone, whereas TEM CD8+ T cells are relatively unresponsive to transpresented IL-15. Furthermore, upon Ag-specific stimulation, TCM CD8+ T cell responses are enhanced by IL-15 transpresentation, whereas TEM CD8+ T cell responses are only slightly affected, both in vitro and in vivo. Thus, our findings distinguish the role of IL-15 transpresentation in the stimulation of distinct memory CD8+ T cell subsets, and they also have implications for ex vivo reactivation and expansion of Ag-experienced CD8+ T cells for immunotherapeutic approaches.

show abstract

ADAM family proteins in the immune system

Cited by 127 publications

References 50 publications

B‐1a cells are imprinted by the microenvironment in spleen and peritoneum

B‐1a cells are imprinted by the microenvironment in spleen and peritoneum

Interaction of Human Immunoglobulin G with CD16 on Natural Killer Cells: Ligand Clearance, FcγRIIIA Turnover and Effects of Metalloproteinases on FcγRIIIA‐Mediated Binding, Signal Transduction and Killing‡

IL-15 Transpresentation Augments CD8+ T Cell Activation and Is Required for Optimal Recall Responses by Central Memory CD8+ T Cells

Contact Info

Product

Resources

About