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Journal of Biochemistry Advance Access published online on August 17, 2006
Journal of Biochemistry, doi:10.1093/jb/mvj175
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© 2006 The Japanese Biochemical Society.
Received July 19, 2006
Accepted July 20, 2006

Regular Paper

Features of a Newly Cloned Pig C1 Esterase Inhibitor1

Chizuko Kobayashi 1, Katsuyoshi Matsunami 1, Takeshi Omori 2, Shino Nakatsu 1, Kengo Nakahata 1, Hengjie Xu 1, Masahiro Fukuzawa 2, Ryota Shirakura 1, and Shuji Miyagawa 1 *

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

* To whom correspondence should be addressed.
Shuji Miyagawa, E-mail: miyagawa{at}orgtrp.med.osaka-u.ac.jp


  Abstract

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.

Keywords: New Effects of Biomaterials; Complement; Gene expresion; Blood Coagulation; Structure of Glycoproteins.
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