TAILIEUCHUNG - Báo cáo khoa học: Activation of hepatocyte growth factor activator zymogen (pro-HGFA) by human kallikrein 1-related peptidases

Hepatocyte growth factor activator (HGFA) is a serine protease and a potent activator of prohepatocyte growth factor⁄scatter factor (pro-HGF⁄SF), a multifunctional growth factor that is critically involved in tis-sue morphogenesis, regeneration, and tumor progression. | ỊFEBS Journal Activation of hepatocyte growth factor activator zymogen pro-HGFA by human kallikrein 1-related peptidases Shoichiro Mukai1 2 Tsuyoshi Fukushima1 Daiji Naka3 Hiroyuki Tanaka1 Yukio Osada2 and Hiroaki Kataoka1 1 Section of Oncopathology and Regenerative Biology Department of Pathology Faculty of Medicine University of Miyazaki Japan 2 Department of Urology Faculty of Medicine University of Miyazaki Japan 3 Mitsubishi ChemicalMedience Corporation R D and Business Development Segment Tokyo Japan Keywords hepatocyte growth factor HGF activator KLK4 KLK5 tissue kallikrein Correspondence H. Kataoka Section of Oncopathology and Regenerative Biology Department of Pathology Faculty of Medicine University of Miyazaki 5200 Kihara Kiyotake Miyazaki 889-1692 Japan Fax 81 985 85 6003 Tel 81 985 85 2809 E-mail mejina@ Received 9 December 2007 revised 29 December 2007 accepted 2 January 2008 doi Hepatocyte growth factor activator HGFA is a serine protease and a potent activator of prohepatocyte growth factor scatter factor pro-HGF SF a multifunctional growth factor that is critically involved in tissue morphogenesis regeneration and tumor progression. HGFA circulates as a zymogen pro-HGFA and is activated in response to tissue injury. Although thrombin is considered to be an activator of pro-HGFA alternative pro-HGFA activation pathways in tumor microenvironments remain to be identified. In this study we examined the effects of kallikrein 1-related peptidases KLKs a family of extracellular serine proteases on the activation of pro-HGFA. Among the KLKs examined KLK2 KLK3 KLK4 and KLK5 we identified KLK4 and KLK5 as novel activators of pro-HGFA. Using N-terminal sequencing the cleavage site was identified as the normal processing site Arg407-Ile408. The activation of pro-HGFA by KLK5 required a negatively charged substance such as dextran sulfate whereas KLK4 could process pro-HGFA without dextran sulfate. KLK5 .

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