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The ADAM15 ectodomain is shed from secretory exosomes
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  • Journal title : BMB Reports
  • Volume 48, Issue 5,  2015, pp.277-282
  • Publisher : Korean Society for Biochemistry and Molecular Biology
  • DOI : 10.5483/BMBRep.2015.48.5.161
 Title & Authors
The ADAM15 ectodomain is shed from secretory exosomes
Lee, Hee Doo; Kim, Yeon Hyang; Koo, Bon-Hun; Kim, Doo-Sik;
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 Abstract
We demonstrated previously that a disintegrin and metalloproteinase 15 (ADAM15) is released into the extracellular space as an exosomal component, and that ADAM15-rich exosomes have tumor suppressive functions. However, the suppressive mechanism of ADAM15-rich exosomes remains unclear. In this study, we show that the ADAM15 ectodomain is cleaved from released exosomes. This shedding process of the ADAM15 ectodomain was dramatically enhanced in conditioned ovarian cancer cell medium. Proteolytic cleavage was completely blocked by phenylmethylsulfonyl fluoride, indicating that a serine protease is responsible for exosomal ADAM15 shedding. Experimental evidence indicates that the ADAM15 ectodomain itself has comparable functions with those of ADAM15-rich exosomes, which effectively inhibit vitronectininduced cancer cell migration and activation of the MEK/extracellular regulated kinase signaling pathway. We present a tumor suppressive mechanism for ADAM15 exosomes and provide insight into the functional significance of exosomes that generate tumor-inhibitory factors. [BMB Reports 2015; 48(5): 277-282]
 Keywords
ADAM15;Ectodomain shedding;Exosomes;MEK/ERK signaling;Tumor suppression;
 Language
English
 Cited by
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Glycosyl-Phosphatidyl-Inositol (GPI)-Anchors and Metalloproteases: Their Roles in the Regulation of Exosome Composition and NKG2D-Mediated Immune Recognition, Frontiers in Cell and Developmental Biology, 2016, 4  crossref(new windwow)
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