Zhu Long, Zhuo Lisheng, Watanabe Hideto, Kimata Koji
Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi, Japan.
Connect Tissue Res. 2008;49(1):48-55. doi: 10.1080/03008200701820955.
Inter-alpha-trypsin inhibitor (IalphaI) family molecules are composed of a common light chain of chondroitin sulfate proteoglycan, bikunin, and one or two of three genetically distinct heavy chain isoforms (designated HC1, 2, 3) that are bound covalently to the chondroitin sulfate chain. Hyaluronan can substitute for chondroitin sulfate to form a covalent complex with HCs. Important physiological and pathological roles of the formation of HC-hyaluronan complex have been well established. However, the involvement of the three HC isoforms in the assembly of IalphaI family molecules and the subsequent formation of SHAP-hyaluronan complex has not been studied yet in mice. In this study, we showed that mouse IalphaI and pre-alpha inhibitor contain HC1 approximately HC3 and HC3, respectively. All three HC isoforms are found in the SHAP-hyaluronan complexes of physiological or pathological origins as well as that formed in vitro, indicating that the three HC isoforms are all potential in forming complex with hyaluronan.
α-胰蛋白酶抑制剂（IαI）家族分子由硫酸软骨素蛋白聚糖的共同轻链、比基尼和三种基因不同的重链异构体（分别命名为HC1、2、3）中的一种或两种组成，这些重链异构体与硫酸软骨素链共价结合。透明质酸可以替代硫酸软骨素与重链形成共价复合物。重链-透明质酸复合物形成的重要生理和病理作用已经得到充分证实。然而，在小鼠中，三种重链异构体在IαI家族分子组装以及随后形成SHAP-透明质酸复合物中的作用尚未得到研究。在本研究中，我们发现小鼠IαI和前α抑制剂分别含有HC1约HC3和HC3。在生理或病理来源的SHAP-透明质酸复合物以及体外形成的复合物中均发现了所有三种重链异构体，这表明三种重链异构体都有与透明质酸形成复合物的潜力。
