Details

Autor(en) / Beteiligte

• Lee, H.D., Yonsei University, Seoul, Republic of Korea
• Kim, Y.H., Korea Polytechnics, Nonsan, Republic of Korea
• Koo, B.H., Yonsei University, Seoul, Republic of Korea
• Kim, D.S., Yonsei University, Seoul, Republic of Korea

Titel

The ADAM15 ectodomain is shed from secretory exosomes

Ist Teil von

• BMB Reports, 2015, 48(5), , pp.277-282

Ort / Verlag

Korea (South): Korean Society for Biochemistry and Molecular Biology

Erscheinungsjahr

2015

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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.