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Tetraspanin CD9 modulates ADAM17-mediated shedding of LR11 in leukocytes
Shokichi Tsukamoto,Masahiro Takeuchi,Takeharu Kawaguchi,Emi Togasaki,Atsuko Yamazaki,Yasumasa Sugita,Tomoya Muto,Shio Sakai,Yusuke Takeda,Chikako Ohwada,Emiko Sakaida,Naomi Shimizu,Keigo Nishii,Meizi 생화학분자생물학회 2014 Experimental and molecular medicine Vol.46 No.-
LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A shedding mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated shedding of tumor necrosis factor-a and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated shedding mechanism.
Induction of allergic contact dermatitis by astigmatid mite-derived monoterpene, α-acaridial
Toshio Sasai,Yunosuke Hirano,Sayaka Maeda,Isamu Matsunaga,Atsushi Otsuka,Daisuke Morita,Ritsuo Nishida,Hideo Nakayama,Yasumasa Kuwahara,Masahiko Sugita,Naoki Mori 한국응용곤충학회 2008 한국응용곤충학회 학술대회논문집 Vol.2008 No.10
α-Acaridial [2(E)-(4-methyl-3-pentenyl)butenedial] is a novel monoterpene secreted from the house dust mites. Because of its molecular nature of a highly reactive, small lipidic compound, we addressed whether α-acaridial might function as a haptenic allergen that induced allergic contact dermatitis. Mice sensitized with α-acaridial were challenged by the same antigen on the ear skin. After 2 days, significant ear swelling with a prominent infiltration of CD4+ T lymphocytes was observed. In vitro, α-acaridial exhibited an outstanding ability to quickly interact with and chemically modify a reference protein. Virtually all cysteine residues and a sizable fraction of lysine residues were found to be selectively modified, suggesting that α-acaridial could potentially interact with any proteins. Previously, numerous mite-derived proteinaceous allergens have been associated with contact dermatitis. Our study now emphasizes that small lipidic compounds released from mites comprise a new class of mite allergens, and therefore, is of significant medical implications.