Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Higgins PJ, Ko JL, Lobell R, Sardonini C, Alessi MK, Yeh CG
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------>journal_name=Journal of Immunology
------>paper_name=A soluble chimeric complement inhibitory protein that possesses both decay-accelerating and factor I cofactor activities
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------>fullAbstract=A chimeric gene was constructed from the genes coding for the human complement regulatory proteins, membrane cofactor protein (CD46) and decay-accelerating factor (CD55). The recombinant chimeric gene was transfected into Chinese hamster ovary cells. The gene product is a soluble, glycosylated, 110-kDa protein named complement activation blocker-2 (CAB-2). This protein possesses both factor I cofactor activity and decay-accelerating activity, and inactivates classical and alternative C3/C5 convertases in vitro. The specific activity of CAB-2 against cell-associated convertases is greater than that of soluble forms of either membrane cofactor protein or decay-accelerating factor or of both factors combined. CAB-2 also blocks the activation of complement in vivo, inhibiting both the Arthus reaction and Forssman shock in guinea pigs. Studies in rats demonstrate CAB-2 to exhibit favorable biphasic pharmacokinetics with a t1/2 alpha of 10 min and a t1/2 beta of 8 h; the beta phase accounts for 93% of the administered dose. CAB-2 may be an effective therapeutic treatment of acute human diseases in which excessive complement activation causes damage to normal tissues.
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------>authors=Higgins PJ, Ko JL, Lobell R, Sardonini C, Alessi MK, Yeh CG
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------>updateTitle=A soluble chimeric complement inhibitory protein that possesses both decay-accelerating and factor I cofactor activities.
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------>no=6
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------>publish_year=1997
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z