Cloning of the kininogen gene from Lampetra japonica provides insights into its phylogeny in vertebrates

College of Life Sciences, Liaoning Normal University, Dalian 116029, China

More Information

Corresponding author: E-mail address: liqw@263.net (Qingwei Li)

摘要

- /
- /
- /
- /
Abstract: Kininogens, the precursors of bradykinins, ubiquitously exist in vertebrates, including mammals, birds, amphibians, and fishes. To elucidate the phylogeny of kininogen genes in early vertebrates, we cloned the full-length cDNA of kininogen gene from the liver of Lampetra japonica. The open reading frame of this sequence contained 546 bp and encoded 181 amino acids, including a cystatin domain without the canonical binding site for cysteine proteinases and a bradykinin domain. Our results suggested that in lampreys and most of other vertebrates, there might be only one kininogen gene, which was fused by certain sequences during vertebrate evolution and encoded proteins with more functions; however, another special kininogen gene, only encoding the bradykinin domain with multiple copies in some species, arose only in amphibians for adapting themselves to the unique environment. Using reverse transcription PCR, kininogen mRNA was also detected in lamprey gut, kidney, and leukocyte, but absent in lamprey buccal gland. Our findings may provide insights into the phylogeny of kininogen genes as well as other gene families in vertebrates.
- kininogen /
- phylogeny /
- bradykinin domain /
- cystatin domain /
- tissue distribution

HTML全文

参考文献(34)

[1]	Bradford, H.N., Jameson, B.A., Adam, A.A. et al. Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain J. Biol. Chem., 268 (1993),pp. 26546-26551
[2]	Chen, T.B., Orr, D.F., Bjourson, A.J. et al. Peptides, 23 (2002),pp. 1547-1555
[3]	Chen, T.B., Orr, D.F., Bjourson, A.J. et al. Eur. J. Biochem., 269 (2002),pp. 4693-4700
[4]	Chen, T.B., Bjourson, A.J., Mcclean, S. et al. Peptides, 24 (2003),pp. 853-861
[5]	Chen, T.B., Shaw, C. Peptides, 24 (2003),pp. 1123-1130
[6]	Chen, T.B., Zhou, M., Gagliardo, R. et al. Peptides, 27 (2006),pp. 2129-2136
[7]	Conlon, J.M., Yano, K. Comp. Biochem. Physiol. C, 110 (1995),pp. 305-311
[8]	Contreras-Moreira, B., Bates, P.A. Domain Fishing: A first step in protein comparative modelling Bioinformatics, 18 (2002),pp. 1141-1142
[9]	Forey, P., Janvier, P. Agnathans and the origin of jawed vertebrates Nature, 361 (1993),pp. 129-134
[10]	Furuto-Kato, S., Matsumoto, A., Kitamura, N. et al. Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin: Structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor J. Biol. Chem., 260 (1985),pp. 12054-12059
[11]	Gage, S.H., Gage-Day, M. Science, 23 (1927),pp. 282-284
[12]	Gess, R.W., Coates, M.I., Rubidge, B.S. A lamprey from the Devonian period of South Africa Nature, 443 (2006),pp. 981-984
[13]	Ho, D.H., Badellino, K., Baglia, F.A. et al. The role of high molecular weight kininogen and prothrombin as cofactors in the binding of factor XI A3 domain to the platelet surface J. Biol. Chem., 275 (2000),pp. 25139-25145
[14]	Kato, H., Nagasawa, S., Suzuki, T. Studies on the structure of bovine kininogen: Cleavages of disulfide bonds and of methionyl bonds in kininogen-II J. Biochem., 67 (1970),pp. 313-323
[15]	Kumar, S., Tamura, K., Nei, M. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment Brief Bioinform., 5 (2004),pp. 150-163
[16]	Kuratani, S., Kuraku, S., Murakami, Y. Lamprey as an evo-devo model: Lessons from comparative embryology and molecular phylogenetics Genesis, 34 (2002),pp. 175-183
[17]	Lai, R., Liu, H., Lee, W.H. et al. Biochem. Biophys. Res. Commun., 286 (2001),pp. 59-263
[18]	Lai, R., Liu, H., Lee, W.H. et al. Peptides, 24 (2003),pp. 199-204
[19]	Li, L., Bjourson, A.J., He, J.Y. et al. Peptides, 24 (2003),pp. 863-872
[20]	Liang, J.G., Han, Y., Li, J.X. et al. Peptides, 27 (2006),pp. 2683-2687
[21]	McCrudden, C.M., Zhou, M., Chen, T.B. et al. Peptides, 28 (2007),pp. 1275-1281
[22]	Murayama, N., Hayashi, M.A.F., Ohi, H. et al. Proc. Natl. Acad. Sci. USA, 94 (1997),pp. 1189-1193
[23]	Pierce, J.V. Structural features of plasma kinins and kininogens Fed. Proc., 27 (1968),pp. 52-57
[24]	Puri, P.N., Zhou, F., Hu, C.J. et al. High molecular weight kininogen inhibits thrombin-induced platelet aggregation and cleavage of aggregin by inhibiting binding of thrombin to platelets Blood, 77 (1991),pp. 500-507
[25]	Regoli, D., Barabe, J. Pharmacology of bradykinin and related kinins Pharmacol. Rev., 32 (1980),pp. 1-46
[26]	Salvesen, G., Parkes, C., Abrahamson, M. et al. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases Biochem. J., 234 (1986),pp. 429-434
[27]	Semba, U., Shibuya, Y., Okabe, H. et al. Whale high-molecular-weight and low-molecular-weight kininogens Thromb. Res., 97 (2000),pp. 481-490
[28]	Takano, M., Kondo, J., Yayama, K. et al. Molecular cloning of cDNAs for mouse low-molecular-weight and high-molecular-weight prekininogens Biochim. Biophys. Acta, 1352 (1997),pp. 222-230
[29]	Thompson, A.H., Bjourson, A.J., Shaw, C. et al. Rapid Commun. Mass Spectrom., 20 (2006),pp. 3780-3788
[30]	Thompson, J.D., Gibson, T.J., Plewniak, F. et al. The ClustalX Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res., 24 (1997),pp. 4876-4882
[31]	Ylönen, A., Rinne, A., Herttuainen, J. et al. Eur. J. Biochem., 266 (1999),pp. 1066-1072
[32]	Ylönen, A., Helin, J., Bøgwald, J. et al. Purification and characterization of novel kininogens from spotted wolffish and Atlantic cod Eur. J. Biochem., 269 (2002),pp. 2639-2646
[33]	Zhou, J.W., Bjourson, A.J., Coulter, D.J. et al. Peptides, 28 (2007),pp. 781-789
[34]	Zhou, L.W., Li-Ling, J., Huang, H.F. et al. Phylogenetic analysis of vertebrate kininogen genes Genomics, 91 (2008),pp. 129-141