Features of a Newly Cloned Pig C1 Esterase Inhibitor
Authors: Kobayashi, Chizuko; Matsunami, Katsuyoshi; Omori, Takeshi; Nakatsu, Shino; Nakahata, Kengo; Xu, Hengjie; Shirakura, Ryota; Fukuzawa, Masahiro; Miyagawa, Shuji
Source: The Journal of Biochemistry, Volume 140, Number 3, September 2006 , pp. 421-427(7)
Publisher: Oxford University Press
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.
Document Type: Research Article
Publication date: 2006-09-01