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Papers In Press, published online ahead of print January 5, 2001
J. Biol. Chem, 10.1074/jbc.C000899200
Submitted on December 20, 2000
Revised on January 5, 2001
Accepted on January 5, 2001
Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480-1195
Corresponding Author: kimata{at}amugw.aichi-med-u.ac.jp
Hyaluronan (HA) associates with proteins and proteoglycans to form the extracellular HA-rich matrices that significantly affect cellular behaviors. So far, only the heavy chains of the plasma inter-a-trypsin inhibitor (ITI) family, designated as SHAPs (serum derived hyaluronan-associated proteins), has been shown to bind covalently to HA. The physiological significance of such a unique covalent complex has been unknown but is of great interest because HA and the ITI family are abundant in tissues and in plasma, respectively, and the SHAP-HA complex is formed wherever HA meets plasma. We abolished the formation of the SHAP-HA complex in mice by targeting the gene of bikunin, the light chain of the ITI family members, which is essential for their biosynthesis. As a consequence, the cumulus oophorus, an investing structure unique to the oocyte of higher mammals, had a defect in forming the extracellular HA-rich matrix during expansion. The ovulated oocytes were completely devoid of matrix and unfertilized, leading to severe female infertility. Intraperitoneal administration of ITI, accompanied by the formation of the SHAP-HA complex, fully rescued the defects. We conclude that the SHAP-HA complex is a major component of the HA-rich matrix of the cumulus oophorus and is essential for fertilization in vivo.
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