TAILIEUCHUNG - Báo cáo khoa học: Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25)

Insulin-like growth factor (IGF) binding protein-related protein-1 (IGFBP-rP1) modulates cellular adhesion and growth in an IGF⁄insulin-dependent or independent manner. It also shows tumor-suppressive activity in vivo. We recently found that a single-chain IGFB-rP1 is proteolytically cleaved to a two-chain form by a trypsin-like, endogenous serine protein-ase, changing its biological activities. | ềFEBS Journal Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 IGFBP-rP1 angiomodulin mac25 Sanjida Ahmed1 2 Xinlian Jin1 Motoki Yagi1 2 Chie Yasuda1 Yuichiro Sato1 2 Shouichi Higashi1 Chen-Yong Lin3 Robert B. Dickson3 and Kaoru Miyazaki1 2 1 Division of CellBiology Kihara Institute for BiologicalResearch Yokohama City University Japan 2 Graduate Schoolof Integrated Sciences Yokohama City University Japan 3 Lombardi Comprehensive Cancer Center Georgetown University MedicalCenter Washington DC USA Keywords angiomodulin insulin-like growth factor insulin-like growth factor binding protein-related protein-1 matriptase proteolytic processing Correspondence K. Miyazaki Division of Cell Biology Kihara Institute for BiologicalResearch Yokohama City University 641-12 Maioka-cho Totsuka-ku Yokohama 244-0813 Japan Fax 81 458201901 Tel 81 458201905 E-mail miyazaki@ Received 25 August 2005 revised 15 November 2005 accepted 8 December 2005 doi Insulin-like growth factor IGF binding protein-related protein-1 IGFBP-rPl modulates cellular adhesion and growth in an IGF insulin-dependent or independent manner. It also shows tumor-suppressive activity in vivo. We recently found that a single-chain IGFB-rP1 is proteolytically cleaved to a two-chain form by a trypsin-like endogenous serine proteinase changing its biological activities. In this study we attempted to identify the IGFBP-rP1-processing enzyme. Of nine human cell lines tested seven cell lines secreted IGFBP-rP1 at high levels and two of them ovarian clear cell adenocarcinoma OVISE and gastric carcinoma MKN-45 highly produced the cleaved IGFBP-rP1. Serine proteinase inhibitors effectively blocked the IGFBP-rP1 cleavage in the OVISE cell culture. The conditioned medium of OVISE cells did not cleave purified IGFBP-rP1 but their membrane fraction had an IGFBP-rP1-cleaving activity.

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