Abstract
Kininogens are precursor proteins of bradykinin that are widely distributed in mammalian blood plasma1-3. Kininogens are comprised of two distinct proteins, designated low molecular weight (LMW) and high molecular weight (HMW) kininogens. Both kininogens are single-chain glycoproteins and carry a bradykinin moiety in the interior of the polypeptide chains bridged by a disulfide linkage. The kininogens thus consist of three domains: an amino-terminal heavy chain (H chain), bradykinin, and a carboxyl-terminal light chain (L chain). The key functions of kininogens, effected via kinin, are smooth muscle contraction, induction of hypotension, pain generation and increase of vascular permeability. Another well-established kininogen function is related to the initial step of blood coagulation and fibrinolysis, and this function is attributed to the L chain of HMW kininogen. Although the pharmacology, physiology and biochemistry of the kinin-kininogen system have been remarkably developed through studies conducted in a number of laboratories, the molecular and genetic aspects of this system remained to be clarified. Our laboratory is concerned with investigations on the structure, expression and regulation of the kininogen gene with the aid of molecular cloning and its related technology.
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References
S. Nakanishi, N. Kitamura and H. Ohkubo, Structure, regulation and evolution of the genes for the renin-angiotensin and the kallikrein-kinin systems, Bio Technology 3: 1089–1098 (1985).
W. Müller-Esterl, S. Iwanaga and S. Nakanishi, Kininogens revisited. Trends iochem. Sci. 11: 336–339 (1986).
S. Nakanishi, Substance P precursor and kininogen: their structures, gene organizations, and regulation, Physiol. Rev. 67: 1117–1142 (1987).
H. Nawa, N. Kitamura, T. Hirose, M. Asai, S. Inayama and S. Nakanishi, Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs, Proc. Natl. Acad. Sci. USA 80: 90–94 (1983).
N. Kitamura, Y. Takagaki, S. Furuto, T. Tanaka, H. Nawa and S. Nakanishi, A single gene for bovine high molecular weight and low molecular weight kininogens, Nature 305: 545–549 (1983).
Y. Takagaki, N. Kitamura and S. Nakanishi, Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens—primary structures of two human prekininogens, J. Biol. Chem. 260: 8601–8609 (1985).
N. Kitamura, H. Kitagawa, D. Fukushima, Y. Takagaki, T. Miyata and S. Nakanishi, Structural organization of the human kininogen gene and a model for its evolution, J. Biol. Chem. 260: 8610–8617 (1985).
S. Furuto-Kato, A. Matsumoto, N. Kitamura and S. Nakanishi, Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin—structural relationship of kininogens with major acute phase protein and a1-cysteine proteinase inhibitor, J. Biol. Chem. 260: 12054–12059 (1985).
H. Kitagawa, N. Kiatamura, H. Hayashida, T. Miyata and S. Nakanishi, Differing expression patterns and evolution of the rat kininogen gene family, J. Biol. Chem. 262: 2190–2198 (1987).
R. Kageyama, N. Kitamura, H. Ohkubo and S. Nakanishi, Differential expression of the multiple forms of rat prekininogen mRNAs after acute inflammation, J. Biol. Chem. 260: 12060–12064 (1985).
K. P. Anderson, A. D. Martin, and E. C. Heath, Rat major acute-phase protein: biosynthesis and characterization of a cDNA clone, Arch. Biochem. Biophys. 233; 624–635 (1984).
F. Esnard and F. Gauthier, Rat ai-cysteine proteinase inhibitor: an acute phase reactant identical with a1 acute phase globulin, J. Biol. Chem. 258: 12443–12447 (1983).
I. Ohkubo, T. Kurachi, T. Takasawa, H. Shiokawa and M. Sasaki, Isolation of a human cDNA for a1-thiol proteinase inhibitor and its identity with low molecular weight kininogen, Biochemistry 23: 5691–5697 (1984).
T. Sueyoshi, T. Miyata, N. Hashimoto, H. Kato, H. Hayashida, T. Miyata and S. Iwanaga, Bovine high molecular weight kininogen: the amino acid sequence, positions of carbohydrate chains and disulfide bridges in the heavy chain portion, J. Biol. Chem. 262: 2768–2779 (1987).
R. Kageyama, N. Kitamura, H. Ohkubo and S. Nakanishi, Differing utilization of homologous transcription initiation sites of rat K and T kininogen genes under inflammation condition, J. Biol. Chem. 262: 2345–2351 (1987).
A. Kakizuka, N. Kitamura and S. Nakanishi, Localization of DNA sequences governing alternative mRNA production of rat kininogen genes, J. Biol. Chem. in press.
H. Nawa, T. Hirose, H. Takashima, S. Inayama and S. Nakanishi, Nucleotide sequences of cloned cDNAs for two types of bovine brain substance P precursor, Nature 306: 32–36 (1983).
H. Nawa, M. Doteuchi, K. Igano, K. Inouye and S. Nakanishi, Substance K: A novel mammalian tachykinin that differs from substance P in its pharmacological profile, Lifeci. 34: 1153–1160 (1984).
H. Nawa, H. Kotani and S. Nakanishi, Tissue-specific generation of two preprotachykinin mRNAs from one gene by alternative RNA splicing, Nature 312: 729–734 (1984).
H. Kotani, M. Hoshimaru, H. Nawa and S. Nakanishi, Structure and gene organization of bovine neuromedin K precursor, Proc. Natl. Acad. Sci. USA 83: 7074–7078 (1986).
S. Nakanishi, Structure and ragulation of the preprotachykinin gene, Trends eurosci. 9: 41–44 (1986).
Y. Harada, T. Takahashi, M. Kuno, K. Nakayama, Y. Masu and S. Nakanishi, Expression of two different tachykinin receptors in Xenopus oocytes by exogenous mRNAs, J. Neurosci. 7: 3265–3273 (1987).
Y. Masu, K. Nakayama, H. Tamaki, Y. Harada, M. Kuno and S. Nakanishi, cDNA cloning of bovine substance-K receptor through oocyte expression system, Nature 329: 836–838 (1987).
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© 1989 Plenum Press, New York
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Nakanishi, S. et al. (1989). Control of Kininogen Gene Expression. In: Abe, K., Moriya, H., Fujii, S. (eds) Kinins V. Advances in Experimental Medicine and Biology, vol 247 A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9543-4_2
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DOI: https://doi.org/10.1007/978-1-4615-9543-4_2
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