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Study on Design of Macromolecular Matrix for PTCA Application to Suppress Coronary Restenosis

PTCA应用抑制冠状动脉再狭窄的高分子基质设计研究

基本信息

批准号：
09680855
负责人：
OKAMOTO Kouji
金额：
$ 2.11万
依托单位：
Kyushu Institute of Technology
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
1997
资助国家：
日本
起止时间：
1997 至 1999
项目状态：
已结题

项目摘要

<1997> Soluble α-elastin was prepared from insoluble elastin by heated-oxalic acid treatment. Chemical modification of α-elastin was performed by the coupling of Val-OMe(100eq) to α-elastin in the presence of water-soluble carbodiimide (WSC) at various concentrations(5, 10, 20, 30, 50 and 100eq). Coacervation of chemically modified α-elastin matrix[(α-elastin) ; 100(Val-OMe) ; 20(WSC)] was translated to lowest temperature exhibiting onset temperature(ca.17℃). The time -course of the coacervate formation showed that chemically modified a-elastin matrix[(α-elastin) ; 100(Val-OMe) ; 20(WSC)] formed the coacervate layer at an earlier time within 16 min. <1998> CD study exhibited the α-helix structure of chemically modified α-elastin matrix[(α-elastin) ; 100(Val-OMe) ; 20(WSC)]. The incorporation of genistein, a specific inhibitor for tyrosine kinase, into the coacervate layer of chemically modified α-elastin matrix[(α-elastin) ; 100(V al-OMe) ; 20(WSC)] was about 30%. Polypeptide matrix, a high polymer based on the repeating pentapeptide sequence Gly-Val-Gly-Val-Pro(GVGVP), showed a lower onset temperature of coacervation. <1999> The inhibition of platelet aggregation by chemically modified α-elastin matrix[(α-elastin) ; 100(Val-OMe) ; 20(WSC)] was about twice that of α-elastin. Chemically modified α-elastin matrix[(α-elast in) ; 100(Val-OMe) ; 20(WSC)] and polypeptide matrix induced the migration and proliferation of chick vascular smooth muscle cells. However, there was a question whether these matrices induce the migration and proliferation of rabbit or human vascular smooth muscle cells. Further study was continued to solve the above question for one more year. As results, these matrices induced the migration and proliferation of rabbit or human vascular smooth muscle cells, whereas the coacervates of these matrices suppressed the proliferation of these vascular smooth muscle cells.

<1997>以不溶性弹性蛋白为原料，经加热-草酸处理制备可溶性α-弹性蛋白。通过在各种浓度（5、10、20、30、50和100当量）的水溶性碳二亚胺（WSC）存在下将Val-OMe（100当量）偶联至α-弹性蛋白来进行α-弹性蛋白的化学修饰。化学修饰的α-弹性蛋白基质[（α-弹性蛋白）; 100（Val-OMe）; 20（WSC）]的凝聚转化为显示起始温度（约17 ℃）的最低温度。凝聚层形成的时间过程表明，化学修饰的α-弹性蛋白基质[（α-弹性蛋白）; 100（Val-OMe）; 20（WSC）]在16 min内较早形成凝聚层。<1998>CD研究显示化学修饰的α-弹性蛋白基质[（α-弹性蛋白）; 100（Val-OMe）; 20（WSC）]的α-螺旋结构。酪氨酸激酶特异性抑制剂染料木黄酮掺入化学修饰的α-弹性蛋白基质的凝聚层[（α-弹性蛋白）; 100（Val-OMe）; 20（WSC）]约为30%。多肽基质是基于重复的五肽序列Gly-Val-Gly-Val-Pro（GVGVP）的高分子，显示出较低的凝聚起始温度。<1999>化学修饰的α-弹性蛋白基质[（α-弹性蛋白）; 100（Val-OMe）; 20（WSC）]对血小板聚集的抑制作用约为α-弹性蛋白的2倍。化学修饰的α-弹性蛋白基质[（α-elast in）; 100（Val-OMe）; 20（WSC）]和多肽基质诱导鸡血管平滑肌细胞迁移和增殖。然而，这些基质是否诱导兔或人血管平滑肌细胞的迁移和增殖存在疑问。为解决上述问题，又进行了一年的进一步研究。结果，这些基质诱导兔或人血管平滑肌细胞的迁移和增殖，而这些基质的凝聚体抑制这些血管平滑肌细胞的增殖。