Ren Lai, Hajime Takeuchi, Jan Jonczy, Huw H Rees, Philip C Turner
Cell Regulation and Signalling Division, School of Biological Sciences, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK.
Gene 2004 Nov 24A novel thrombin inhibitor named Amblin was identified from the haemolymph of the ixodid (hard) tick, Amblyomma hebraeum, and the coding cDNA was isolated from a tick cDNA library. This cDNA codes for a preprotein of 166 amino acids, including a predicted signal peptide composed of 15 amino acids N-terminal to the mature Amblin. The 151-amino-acid mature Amblin contains 14 cysteines and two Kunitz-like domains. It displays high sequence similarity with a tissue factor pathway inhibitor (TFPI), Ixolaris, from the ixodid tick, Ixodes scapularis, which has 10 cysteines, and a thrombin inhibitor, Boophilin, from the ixodid tick, Boophilus microplus, which has 12 cysteines. Recombinant Amblin specifically inhibited thrombin as efficiently as native Amblin did. This is the first report of a thrombin inhibitor from tick haemolymph.
Ren Lai, Hajime Takeuchi, Jan Jonczy, Huw H Rees, Philip C Turner. A thrombin inhibitor from the ixodid tick, Amblyomma hebraeum. Gene. 2004 Nov 24;342(2):243-9
PMID: 15527983
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