Multiphasic studies on mechamistic asrects of Biocompatiblity of Materials used far Cardiouascular Devices

Research Project

Project/Area Number	61480303
Research Category	Grant-in-Aid for General Scientific Research (B)
Allocation Type	Single-year Grants
Research Field	Thoracic surgery
Research Institution	National cardiovascular Center
Principal Investigator	MATSUDA Takehisa National Cardiovascular Center, 人工臓器部医用材料研究室, 室長 (60142189)
Co-Investigator(Kenkyū-buntansha)	SAKAKIBARA Izumi National Cardiovascular Center, 実験治療開発部, 研究員 (90153866) HAYASHI Ryosuke National Cardiovascular Center, 実験治療開発部, 研究員 (00173047) IWATA Hiroo National Cardiovascular Center, 人工臓器部医用材料研究室, 研究員 (30160120) NIIHOBE Michio Osaka University, 蛋白質研究所・機能制御部門, 助手 (80135748) KATOH Hisao National Cardiovascular Center, 血栓研究室, 室長 (80029959)
Project Period (FY)	1986 – 1987
Project Status	Completed (Fiscal Year 1987)
Budget Amount *help	¥6,000,000 (Direct Cost: ¥6,000,000) Fiscal Year 1987: ¥2,000,000 (Direct Cost: ¥2,000,000) Fiscal Year 1986: ¥4,000,000 (Direct Cost: ¥4,000,000)
Keywords	Biocanpatiblility / Coagulation / Camplement Platelet / Blood / 生体応答性
Research Abstract	This study aims to assess the bicompatibility of blood-contacting surfaces used for cardiovascular artificial devices. Due to the complex nature of body defense mechanisms involving in the thrombus formation, a multiphasic study was conduced to determine the nature and magnitude of the biological responses at blood/material interfaces. Newly-developed quantitative assay method determining the degree of contact activation clearly differentiated the coagulation-promoting surfaces and innert surfaces. The studies using reconstituted systems using purified coagulation and complement factors showed that the molecular events at the initial states of activation of both biological systems were clearly understood at molecular level. On the other hand, the platelet adhesion mediated via adsorbed polasma proteins were inhibited in a dose-dependent manner by using synthetic tetrapeptida (Arg-Gly-Asp-Ser) which was recently identified as the common attachment site of adhesive proteins such as fibrinogen, fibronectin and vitronectin. These studies compiled from the surface reactivity-biological activation of each biological systems input a general "Surface Property-Biological Relationshuip", which will serve as a logical basis of the molecular design of biocompatible surfaces.l serve as a logical basis of the molecular design