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Originally published In Press as doi:10.1074/jbc.C000899200 on January 5, 2001

J. Biol. Chem., Vol. 276, Issue 11, 7693-7696, March 16, 2001
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ACCELERATED PUBLICATION
Defect in SHAP-Hyaluronan Complex Causes Severe Female Infertility
A STUDY BY INACTIVATION OF THE BIKUNIN GENE IN MICE*

Lisheng ZhuoDagger , Masahiko YonedaDagger §, Ming ZhaoDagger , Wannarat YingsungDagger , Naoko Yoshida||, Yasuo Kitagawa||, Kumiko Kawamura**, Toshiro Suzuki**, and Koji KimataDagger Dagger Dagger

From the Dagger  Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi, 480-1195, the || Graduate Program for Regulation of Biological Signals, Graduate School of Bioagriculture Sciences, Nagoya University, Chikusa, Nagoya 464-8601, and ** Japan SLC Inc., Aoi-higashi, Hamamatsu 433-8114, Japan

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-alpha -trypsin inhibitor (ITI) family, designated as SHAPs (serum-derived hyaluronan-associated proteins), have 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 were 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.

* This work was supported by a preparatory grant for the research at the Division of Matrix Glycoconjugates, Research Center for Infectious Disease, Aichi Medical University, by grants-in-aid from the Ministry of Education, Science, Sport, and Culture of Japan, and by a special research fund from Seikagaku Corp.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Biochemistry and Molecular Biology Laboratory, Aichi Prefectural College of Nursing and Health, Moriyama, Nagoya 463-8502, Japan.

Present address: Laboratory of Cellular and Developmental Biology, NIH, Bethesda, MD 20892.

Dagger Dagger To whom correspondence should be addressed: Inst. for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi, 480-1195, Japan. Tel.: 81-52-2644811 (ext. 2088); Fax: 81-561-633-532; E-mail: kimata@amugw.aichi-med-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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