Kinins IV pp 167-172 | Cite as

Kininogen as a Pregnancy-Associated Plasma Protein

  • Tytti Kärkkäinen
  • Ulla Hamberg
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 198A)


Pregnancy induces marked changes in plasma protein concentrations. Some proteins are secreted by the placenta into the maternal circulation and are thus called pregnancy-specific plasma proteins. Pregnancy-specific beta-l-glycoprotein (SP1) was the first protein of this group.1 Other plasma proteins also undergo changes during normal pregnancy and in response to contraceptive doses of estrogens.2,3 In early studies several authors reported determination of kininogen during pregnancy, delivery and puerperium4–6 indicating increased kininogen during pregnancy, decreasing values during labor and increasing kininogen content in puerperium. In all these studies kininogen was determined by the estimation of the bradykinin equivalent by bioassay on the rat uterus or guinea pig ileum. Suzuki7 found in a preliminary report a 100% increase of plasma kininogen compared with non- pregnancy levels showing that bradykinin was not released from kininogen during the pregnancy periods. In particular interest has more recently been focused on the HMr (high molecular weight) kininogen due to its function as a cofactor in the activation of F XII and the onset of coagulation. Maki et al.8 reported increase of HMr kininogen during pregnancy and decrease with the start of labor which suggested that the vasoactive bradykinin was relesed during labor through the activation of plasma kallikrein and brought back to normal level after delivery. Similar findings were recently reported by Suzuki et al.9 applying the bradykinin equivalent to determine kininogen while Maki et al.8 were first to utilize immunological determination with HMr specific antiserum in pregnancy.


Plasma Protein Concentration Plasma Kallikrein Single Radial Immunodiffusion Contraceptive Dose Pregnancy Level 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    H. Bohn, Nachweis und characterisierung von schwanger-schaftsproteinen in der menschlichen placenta, sowie ihre quantitative immunologische bestimmung im serum schwangerer frauen, Arch. Gynäk., 210: 440–457 (1971).CrossRefGoogle Scholar
  2. 2.
    C.-B. Laureil, S. Kullander, and J. Thorell, Rate of plasma protein normalization after partutrition and withdrawal of oral contraceptives, Scand. J. Clin. Lab. Invest., 26: 345–348 (1970).CrossRefGoogle Scholar
  3. 3.
    P. O. Ganrot, Variation of the concentrations of some plasma proteins in normal adults, in pregnant women and in newborns, Scand. J. Clin. Lab. Invest., 29 (Suppl.): 83–88 (1972).Google Scholar
  4. 4.
    C. R. Diniz and I. F. Carvalho, A micromethod for determination of bradykininogen under several conditions, Ann. NY Acad. Sci., 104: 77–89 (1963).PubMedCrossRefGoogle Scholar
  5. 5.
    P. Periti and F. Gasparri, Bradykininogen in the blood of women during pregnancy, labor and puerperium, in: “Hypotensive Peptides,” E. G. Erdös, N. Back, and F. Sicuteri, eds., Springer Verlag, New York (1966).Google Scholar
  6. 6.
    B. Wiegershausen, I. Paegelow, E. Neumayer, and H. Walter, Kininogengehalt in plasma und fruchtwsser, Acta Biol. Med. German., 19: 61–71 (1967).Google Scholar
  7. 7.
    S. Suzuki, The evaluation of the role of the kallikrein-kinin systems with coagulation factors during pregnancy, delivery and puerperium, Abstr. VII Int. Cong. Thromb. Haem., 1052 (1979).Google Scholar
  8. 8.
    M. Maki, K. Soga, and K. Gotoh, The kinin-forming enzyme system in pregnancy and abstetrical DIC, in: “Disseminated Intravascular Coagulation,” T. Abe and M. Yamanaka, eds., Karger, Bibliotheca Haematogica, 49:239–246 (1983).Google Scholar
  9. 9.
    S. Suzuki, T. Murakoshi, and W. Sakamoto, Studies on the various causal 4.0 factors related to hypercoagulability in the field of obstetrics - With special reference to the onset of DIC as viewed from the changing of kinin-kallikrein system and fibrinopeptide A, Adv. Exp. Med. Biol. 156B: 1055–1065 (1983).PubMedGoogle Scholar
  10. 10.
    U. Hamberg and T. Kärkkäinen, Determination of human plasma kininogen by a single radial immunodiffusion method and the bradykinin equivalent, Clin. Chim. Acta, 142: 211–220 (1984).CrossRefGoogle Scholar
  11. 11.
    A.-C. Syvänen, T. Kärkkäinen, and U. Hamberg, Conformation and sequence dependent determinants in human low molecular weight kininogen, Mol. Immunol., 20: 669–678 (1983).Google Scholar
  12. 12.
    A.-C. Syvanen, U. Turepinen, S. Siimesmaa, and U. Hamberg, A radioimmuno assay for the detection of molecular forms of human plasma kininogen, FEBS Lett., 129: 241–245 (1981).PubMedCrossRefGoogle Scholar
  13. 13.
    T. Kärkkäinen, A.-C. Syvänen, U. Turpeinen, and U. Hamberg, Isolation and immunologic properties of a heterogeneous antigen with the characteristics of the heavy chain of human plasma kininogen, Mol. Immunol. 19: 179–189 (1982).Google Scholar
  14. 14.
    T. Karkkainen, Immunopurification of human plasma kininogens, Mol. Immunol., In Press (1985).Google Scholar
  15. 15.
    D. M. Kerbiriou and J. Griffin, Human high molecular weight kininogen. Studies of structure-function relationships and of proteilysis of the molecule occurring during contact activation of plasma, J. Biol. Chem., 254: 12020–12027 (1979).PubMedGoogle Scholar
  16. 16.
    D. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, Protein measurement with the folin phenol reagent, J. Biol. Chem., 193: 265–275 (1951).PubMedGoogle Scholar
  17. 17.
    F. W. Putnam, alpha, beta, gamma, omega - the roster of the plasma proteins, in: “Plasma Proteins,” F. W. Putnam, ed., Vol I, Academic Press, New York (1975).Google Scholar
  18. 18.
    D. Proud, J. V. Pierce, and J. J. Pisano, Radioimmunoassay of human high molecular weight kininogen in normal and deficient plasma, J. Lab. Clin. Med., 95: 563–574 (1980).PubMedGoogle Scholar
  19. 19.
    T. Nakayasu and S. Nagasawa, Studies on human kininogen. I. Isolation, characterization and cleavage by plasma kallikrein of high molecular weight (HMW) kininogen, J, Biochem., 85: 249–258 (1979).Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Tytti Kärkkäinen
    • 1
  • Ulla Hamberg
  1. 1.Department of BiochemistryUniversity of HelsinkiHelsinki 17Finland

Personalised recommendations