CD156 Transgenic Mice

Abstract

CD156 (ADAM8) is part of the ADAM family of proteins with the catalytic site consensus sequence of metalloprotease and disintegrins. To examine the role of CD156 in vivo, we generated mutant CD156 (eCD156) transgenic mice expressing the ectodomain of CD156 under the control of the α1-antitrypsin (AT) promoter. One of the transgenic mice designated ATMS2-TG18 expressed a 1.84 kb mRNA which was predicted to be a truncated CD156. The expression of the transgenic CD156 mRNA in ATMS2-TG18 mice was abundant in the liver and slight in kidney. Turpentine oil (TO) and lipopolysaccharide (LPS) markedly upregulated the expression. Soluble CD156 (sCD156) was produced constitutively, and increased after the treatment with TO. Casein-induced peritoneal leukocyte infiltration was significantly less extensive in ATMS2-TG18 than non-transgenic mice. The expression of L-selectin in neutrophils (PMN) from peripheral blood leukocytes (PBL) was more strongly downregulated in ATMS2-TG18 than non-transgenic mice, suggesting that L-selectin in PMN from ATMS2-TG18 mice was shed by sCD156. In contrast, oxazolone (Ox)-induced contact hypersensitivity reactions (CHR) were more marked in ATMS2-TG18 than non-transgenic mice. The expression of E-selectin mRNA was detected in inflammatory skin sites from ATMS2-TG18, but not non-transgenic mice, suggesting that sCD156 may activate the endothelial cells and lead to the upregulation of E-selectin. These results suggest that CD156 regulates leukocyte infiltration directly or indirectly.

Gingival Crevicular Fluid Zinc- and Aspartyl-Binding Protease Profile of Individuals with Moderate/Severe Atopic Dermatitis

“…Regarding the other zinc-binding proteases downregulated in the GCF of AD patients, disintegrin and metalloproteinase ADAM8 and 9 act as inducing inflammation or anti-inflammation responses, under specific conditions. ADAM8 and 9 have not been previously studied in AD [22,23]. In line with our results, a previous study reported a higher ADAM9 expression in normal mucosa compared to the inflamed gastric mucosa, suggesting that the decreased ADAM9 may predispose to chronic mucosal inflammation [23].…”

“…This was also true for the expression of L-selectin in PMN from peripheral blood samples. These results suggest that ADAM8 might activate endothelial cells and lead to the upregulation of E-selectin, thus regulating leukocyte infiltration directly or indirectly [22]. Therefore, it could be expected that ADAM8 and 9 would be detectable in the GCF samples of healthy controls, regulating leukocyte infiltration as a defensive mechanism of periodontal tissues [22].…”

Generation of hematopoietic repopulating cells from human embryonic stem cells independent of ectopicHOXB4expression

“…Reduction of CD44 by HAS1 expression may negatively regulate normal in vivo migratory properties of HSCs ( 23 ). In contrast with hESC-derived cells, somatic cells expressed substantially higher levels of CXCR4, CD44, and l-selectin, which are involved in appropriate homing and engraftment behavior of candidate human HSCs ( 24 , 25 ), as well as matrix metalloproteinases, ADAM8 ( 26 ) and ADAM17 ( 27 ) that are involved in establishing HSC residence within the BM niche.…”

ADAM9 Is a Novel Product of Polymorphonuclear Neutrophils: Regulation of Expression and Contributions to Extracellular Matrix Protein Degradation during Acute Lung Injury

“…We showed that Adam9 was not essential for PMNs (or macrophages) to accumulate in the lungs during LPS- or bleomycin-mediated ALI in mice suggesting that neither the MP nor the disintegrin domain of PMN or monocytes/macrophage-derived ADAM9 regulate inflammatory cell recruitment into the lung. In contrast, the MP domains of PMN-derived Adam-8 and -17 regulate inflammatory responses in tissues by shedding L-selectin, TNF-α, and TNF receptors from PMN surfaces (66–68). During LPS- and bleomycin-mediated ALI, Adam9 promoted lung injury and reduced lung compliance without altering lung inflammatory cell counts in mice.…”