间α胰蛋白酶抑制剂与胞外间质  

Inter α Trypsin Inhibitor and Extracellular Matrix .

作　　者：赵明[1] 米田雅彦 木全弘治[2] 

机构地区：[1]中国科学院上海生物化学研究所,上海200031 [2]日本爱知医科大学分子医科学研究所,爱知县48011

出　　处：《生物化学与生物物理进展》1997年第3期220-223,共4页Progress In Biochemistry and Biophysics

摘　　要：间α胰蛋白酶抑制剂 (ITI)家族是在人和动物的血液中广泛存在的一类蛋白质 .ITI由一条硫酸软骨素糖链将三条蛋白质肽链共价地结合在一起 ,其中两条肽链与硫酸软骨素链以氨基酸的羧基与糖链上的羟基形成酯键的形式相连 .在细胞外间质中 ,这种酯键可以转移到透明质酸糖链上 ,进而调控细胞外间质的大小和细胞的性质 .另一条肽链具有Kunitz型蛋白酶抑制剂的结构 。Inter α trypsin inhibitor (ITI) is a kind of protein widely existed in human and animal blood. ITI was composed of three peptides convalently linked together by a chondroitin sulfate chain. Two of the three peptides were linked to the chondroitin sulfate chain each by an ester bond between the carboxyl group of the final amino acid of the peptide and an internal C 6 hydroxyl group of the sugar chain. In extracellular matrix, this kind of ester bond can be transferred from chondroitin sulfate chain to hyaluronan. Thus the extracellular matrix and cell functions were regulated. The other peptide chain of ITI has kunitz type protease inhibitor domains. As a medicine, it can be separated from urine.

关 键 词：间α胰蛋白酶 蛋白酶抑制剂 胞外间质 间质调节 

分 类 号：Q556.3[生物学—生物化学]