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Journal of Biochemistry Advance Access originally published online on August 17, 2006
Journal of Biochemistry 2006 140(3):421-427; doi:10.1093/jb/mvj175
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© 2006 The Japanese Biochemical Society.

ARTICLE

Features of a Newly Cloned Pig C1 Esterase Inhibitor

Chizuko Kobayashi1, Katsuyoshi Matsunami1, Takeshi Omori2, Shino Nakatsu1, Kengo Nakahata1, Hengjie Xu1, Ryota Shirakura1, Masahiro Fukuzawa2 and Shuji Miyagawa1,*

1 Division of Organ Transplantation, Department of Molecular Therapeutics, and 2 Department of Surgery, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871

* To whom correspondence should be addressed. Tel:+81-6-6879-3062, Fax: +81-6-6879-3069, E-mail: miyagawa{at}orgtrp.med.osaka-u.ac.jp

The pig cDNA encoding C1 esterase inhibitor (C1-INH) was isolated and the homology of the sequence was compared with that from other animals. The structure of pig C1-INH contains a two disulfide bridge pattern identical to the human C1-INH. In the amino acid sequence of the first Cys-91 to the C-terminal end, the pigC1-INH has a 76.2% homology with the human protein, and the sequence of the reactive site is close to the human. A surface-bound form of pig and human C1-INH, pC1-INH-PI and hC1-INH, respectively, were next constructed. Stable Chinese hamster ovarian tumor (CHO) cell lines and pig endothelial cell (PEC) lines expressing these C1-INH-PI were prepared by transfection. The basic function and the species specificity of pCI-INH were then investigated using these transfectants. pC1-INH and hC1-INH have almost the same suppressive effect on pig, human, dog and rabbit sera in complement-dependent cell lysis, indicating little species specificity.


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