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The Kallikrein-Kinin System: A Functional Role of Plasma Kallikrein and Kininogen in Blood Coagulation

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Biological Functions of Proteinases

Abstract

Bradykinin is a nonapeptide with potent pharmacological activities such as smooth muscle contraction and hypotension. In mammalian plasma, this physiologically active peptide is in precursor form, called kininogen, and liberated by the action of specific enzyme, plasma kallikrein, or tissue kallikreins. Bovine plasma contains at least two kininogens, named high molecular weight (HMW) kininogen and low molecular weight (LMW) kininogen (Yano et al., 1967). In Figure 1, the linear polypeptide sequences of kininogens are shown for comparison. The areas of which amino acid sequence has been established are indicated by shaded areas. HMW kininogen consists of a single chain with a molecular weight of 76,000, containing four segments, heavy chain, the kinin moiety, fragment 1·2 and light chain (Han et al., 1976). It contains 580 amino acid residues and 12.5% carbohydrates. This kininogen is the physiological substrate of plasma kallikrein (Yano et al., 1971). LMW kininogen, on the other hand, has a molecular weight of 48,000. It consists of 380 residues and 16.4% carbohydrate (Kato et al., 1976).

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References

  • Endo Y, Yamashita K, Han YN, Iwanaga S, Kobata A (1977) The carbohydrate structure of a glycopeptide released by the action of plasma kallikrein on bovine high-molecular-weight kininogen. J Biochem 82: 545–550

    PubMed  CAS  Google Scholar 

  • Griffin JH, Cochrane CG (1976) Mechanism for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor. Proc Natl Acad Sci USA 73: 2554–2558

    Article  PubMed  CAS  Google Scholar 

  • Han YN, Komiya M, Iwanaga S, Suzuki T (1975) Studies on the primary structure of bovine high-molecular-weight kininogen. Amino acid sequence of a fragment ( Histidinerich peptide’) released by plasma kallikrein. J Biochem 77: 55–68

    Google Scholar 

  • Han YN, Kato H, Iwanaga S, Suzuki T (1976) Primary structure of bovine plasma high-molecular -weight kininogen: The amino acid sequence of a glycopeptide portion (Fragment 1) following the C-terminus of the bradykinin moiety. J Biochem 79: 1201–1222

    CAS  Google Scholar 

  • Han YN, Kato H, Iwanaga S, Oh-ishi S, Katori M (1978a) Primary structure of bovine plasma high-molecular-weight kininogen. Characterization of carbohydrate-free fragment 1–2 ( Fragment X) released by the action of plasma kallikrein and its biological activity. J Biochem 83: 213–221

    Google Scholar 

  • Han YN, Kato H, Iwanaga S, Komiya M (1978b) Action of urinary kallikrein, plasmin and other kininogenase on bovine plasma high-molecular-weight kininogen. J Biochem 83: 223–235

    PubMed  CAS  Google Scholar 

  • Hashimoto N, Han YN, Kato H, Iwanaga S (1977) Primary structure of bovine HMW kininogen. Limited hydrolysis with various kininogenases. Seikagaku 49: 896

    Google Scholar 

  • Kaplan AP, Meier HL, Mandle R Jr (1976) The Hageman dependent pathways of coagulation, fibrinolysis and kinin generation. Semin Thromb Hemostas 3: 1–26

    CAS  Google Scholar 

  • Kato H, Han YN, Iwanaga S, Suzuki T, Komiya M (1976) Bovine plasma HMW and LMW kininogens: Structural differences between heavy and light chains derived from their kinin-free proteins. J Biochem 80: 1299–1311

    Google Scholar 

  • Kato H, Han YN, Iwanaga S, Hashimoto M, Sugo T, Fujii S, Suzuki T (1977) In: Haberland GL, Rohen JW, Suzuki T (eds) Kininogenases-Kallikrein 4. Schattauer, Stuttgart New York, p 63–72

    Google Scholar 

  • Kato H, Sugo T, Ikari N, Hashimoto H, Maruyama I, Han YN, Iwanaga S, Fujii S (1978) Role of bovine high-molecular-weight (HMW) kininogen in contact-mediated activation of bovine Factor XII. Suzuki T (eds) Proc Int Symp Kinins, Nov 6–9. Plenum Press, Tokyo, in press

    Google Scholar 

  • Komiya M, Kato H, Suzuki T (1974a) Bovine plasma kininogens. I. Further purification of high molecular weight kininogen and its physicochemical properties. J Biochem 76: 811–822

    Google Scholar 

  • Komiya M, Kato H, Suzuki T (1974b) Bovine plasma kininogens. II. Microheterogeneities of high molecular weight kininogens and their structural relationships. J Biochem 76: 823–832

    Google Scholar 

  • Lie CY, Scott CF, Bagdasarian A, Pierce JV, Kaplan AP, Colman RW (1977) Potentiation of the function of Hageman factor fragments by high molecular weight kininogen. J Clin Invest 60: 7–17

    Article  Google Scholar 

  • Matheson RT, Miller ER, Lacombe MJ, Han YN, Iwanaga S, Kato H, Wuepper KD (1976) Flaujeac factor deficiency: Reconstitution with highly purified bovine HMW kininogen and delineation of a new permeability enhancing peptide released by plasma kallikrein from bovine HMW kininogen. J Clin Invest 58: 1395–1406

    Google Scholar 

  • Meier HL, Pierce JV, Colman RW, Kaplan AP (1977) Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein. J Clin Invest 60: 18–31

    Google Scholar 

  • Morita T, Kato H, Iwanaga S, Takada K, Kimura T, Sakakibara S (1977) New fluorogenic substrates for α-thrombin, factor Xa, kallikreins and urokinase. J Biochem 82: 1495–1498

    PubMed  CAS  Google Scholar 

  • Oh-ishi S, Katori M, Han YN, Iwanaga S, Kato H, Suzuki T (1977) Possible physiological role of new peptide fragments released from bovine high-molecular-weight kininogen by plasma kallikrein. Biochem Pharmacol 26: 115–120

    Article  CAS  Google Scholar 

  • Scicli AG, Waldmann R, Guimaraes JA, Scicli G, Carretero OA, Kato H, Han YN, Iwanaga S (1979) Relationship between structure and correcting activity of bovine high molecular weight kininogen upon the clotting time of Fitzgerald-trait plasma. J Exp Med 149: 847–855

    Article  PubMed  CAS  Google Scholar 

  • Sugo T, Kato H, Iwanaga S, Fujii S, Takamatsu J, Kamiya T (1978) Molecular mechanism of the surface-mediated activation of Factor XII(I). Seikagaku 50: 763

    Google Scholar 

  • Sugo T, Kato H, Iwanaga S, Fujii S (1979) Occurrence of Leu-Lys-bradykinin and histidinerich peptide in high-molecular-weight kininogen isolated from horse plasma. Biochim Biophys Acta, 579: 474–478

    PubMed  CAS  Google Scholar 

  • Waldmann R, Scicli AG, McGregor RK, Carretero OA, Abraham JP, Kato H, Han YN, Iwanaga S (1976) Effect of bovine high molecular weight kininogen and its fragments on Fitzgerald trait plasma. Thromb Res 8: 785–795

    Article  PubMed  CAS  Google Scholar 

  • Waldmann R, Scicli AG, Scicli GM, Guimaraes J, Carretero OA, Kato H, Han YN, Iwanaga S (1977) Significant role of fragment 1·2 plus light chain of bovine high molecular weight kininogen in contact mediated coagulation. Thromb Haemostas 38: 14

    Google Scholar 

  • Weber K, Osborn M (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 244: 4406–4412

    PubMed  CAS  Google Scholar 

  • Wuepper KD, Miller DR, Han YN, Kato H, Iwanaga S (1978) HMW-kininogen deficiency: Delineation of a fragment of bovine HMW-kininogen which repairs the defect. Fed Proc 37: 1587

    Google Scholar 

  • Yano M, Nagasawa S, Horiuchi K, Suzuki T (1967) Separation of a new substrate, kininogen-I, for plasma kallikrein in bovine plasma. J Biochem 62: 504–506

    PubMed  CAS  Google Scholar 

  • Yano M, Nagasawa S, Suzuki T (1971) Partial purification and some properties of high molecular weight kininogen, bovine kininogen-I. J Biochem 69: 471–481

    PubMed  CAS  Google Scholar 

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© 1979 Springer-Verlag Berlin Heidelberg

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Iwanaga, S., Kato, H., Sugo, T., Ikari, N., Hashimoto, N., Fujii, S. (1979). The Kallikrein-Kinin System: A Functional Role of Plasma Kallikrein and Kininogen in Blood Coagulation. In: Holzer, H., Tschesche, H. (eds) Biological Functions of Proteinases. Colloquium der Gesellschaft für Biologische Chemie 26.–28. April 1979 in Mosbach/Baden, vol 30. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81395-5_23

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  • DOI: https://doi.org/10.1007/978-3-642-81395-5_23

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-81397-9

  • Online ISBN: 978-3-642-81395-5

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