Features of a newly cloned pig C1 esterase inhibitor.
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.
Kobayashi
Chizuko
C
Division of Organ Transplantation, Department of Molecular Therapeutics, and Department of Surgery, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871.
Matsunami
Katsuyoshi
K
Omori
Takeshi
T
Nakatsu
Shino
S
Nakahata
Kengo
K
Xu
Hengjie
H
Shirakura
Ryota
R
Fukuzawa
Masahiro
M
Miyagawa
Shuji
S
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D003001:Cloning, Molecular; D003174:Complement C1 Inactivator Proteins / Q000235:genetics*; D006224:Cricetinae; D003412:Cricetulus; D017931:DNA Primers; D018076:DNA, Complementary / Q000235:genetics; D005434:Flow Cytometry; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013045:Species Specificity; D034421:Sus scrofa / Q000235:genetics*
D003174:Complement C1 Inactivator Proteins; D017931:DNA Primers; D018076:DNA, Complementary