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Thromb Haemost 1988; 60(03): 447-452
DOI: 10.1055/s-0038-1646988
Original Article
Schattauer GmbH Stuttgart

Commercial Immunodepleted Deficient Plasmas Contain Cleaved High Molecular Weight Kininogen (HK)

C Mannhalter
*   The First Department of Medicine, Vienna, Austria
,
H Lang
**   The Medical School, Vienna, Austria, and Immuno AG, Vienna, Austria
› Author Affiliations
Further Information

Publication History

Received 29 February 1988

Accepted after revision 26 July 1988

Publication Date:
30 June 2018 (online)

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Summary

Comparative analysis of high molecular weight kininogen (HK) in various commercial congenital and immunodepleted deficiency plasmas was performed by immunoblotting of HK. It was found, that some artificially depleted deficiency plasmas contained proteolytically cleaved, kinin-free kininogen. In contrast, in all congenitally deficient plasmas, HK was present in the intact, single chain form. Thus, cleavage of kininogen could have been triggered by or during the immunodepletion procedure. It was seen, that the degree of proteolytic cleavage and degradation of HK in depleted plasmas differed among various manufacturers. E.g. depleted products of one company contained only trace amounts of cleaved HK, in contrast to products of another one, in which HK was completely degraded. The immunoblot analysis of HK reflects the occurrence of proteolytic events during the production of artificially deficient plasmas and can therefore serve as a quality control method.

Keywords

High molecular weight kininogen - Commercial, immunodepleted deficiency plasmas - Proteolytic events during immunodepletion of plasmas
 

  • References

  • 1 Saito H, Ratnoff OD, Waldmann R, Abraham JP. Fitzgerald trait. Deficiency of a hitherto unrecognized agent, Fitzgerald factor, participating in surface-mediated reactions of clotting, fibrinolysis, generation of kinin, and the property of diluted plasma enhancing vascular permeability (PF/dil). J Clin Invest 1975 55. 1082-1089
    PubMedSearch in Google Scholar
  • 2 Colman RW, Bagdasarian A, Talamo RC, Scott CF, Seavay M, Guimares JA, Pierce JV, Kaplan AP. Williams trait: human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hage-man factor-dependent pathways. J Clin Invest 1975; 56: 16050-16062
    PubMedSearch in Google Scholar
  • 3 Wuepper KD. Prekallikrein deficiency in man. J Exp Med 1973; 138: 1345-1355
    CrossrefPubMedSearch in Google Scholar
  • 4 Rosenthal RL, Dreskin OH, Rosenthal N. New hemophilialike disease caused by deficiency of a third plasma thromboplastin factor. Proc Soc Exp Biol Med 1953; 82: 171-174
    CrossrefPubMedSearch in Google Scholar
  • 5 Seligsohn U. High gene frequency of factor XI (PTA) deficiency in Ashkenazi Jews. Blood 1978; 51: 1223-1228
    PubMedSearch in Google Scholar
  • 6 Mariani G, Mazzucconi MG. Factor VII congenital deficiency. Clinical picture and classification of the variants. Haemostasis 1983 13. 169-177
    PubMedSearch in Google Scholar
  • 7 Gürtler LG, Wernicke D, Eberle J, Zoulek G, Deinhardt F, Schramm W. Increase in prevalence of anti HTLV-III in haemophiliacs. Lancet 1984; II: 1275-1276
    PubMedSearch in Google Scholar
  • 8 Machin SJ, Mc Verry BA, Cheingsong-Popov R, Tedder RS. Seroconversion for HTLV-III since 1980 in British haemophiliacs. Lancet 1985; I: 336
    PubMedSearch in Google Scholar
  • 9 Mannhalter C, Lang H. Vergleichende Untersuchung eines hereditären, unbehandelten Faktor-VIII-Mangelplasmas mit einem hereditären, dampfbehandelten Produkt. Hämostaseologie 1987; 7: 29-31
    Thieme ConnectPubMedSearch in Google Scholar
  • 10 Sugo T, Kato H, Iwanaga S, Takada K, Sakakibara S. Kinetic studies on surface-mediated activation of bovine Factor XII and prekallikrein. Effects of kaolin and high molecular weight kininogen on the activation reactions. Eur J Biochem 1985 146. 43-50
    PubMedSearch in Google Scholar
  • 11 Tans G, Griffin JH. Properties of sulfatides in Factor-XII-dependent contact activation. Blood 1982; 59: 69-75
    CrossrefPubMedSearch in Google Scholar
  • 12 Griffin JH. The role of surface in surface-dependent activation of Hageman Factor (Factor XII). Proc Natl Acad Sci USA 1978; 75: 1998-2002
    CrossrefPubMedSearch in Google Scholar
  • 13 Mandle R, Kaplan AP. Hageman factor substrates. Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman factor-dependent fibrinolysis. J Biol Chem 1977 252. 6097-6104
    PubMedSearch in Google Scholar
  • 14 Bouma BN, Griffin JH. Human blood coagulation Factor XI: Purification, properties and mechanism of activation by activated Factor XII. J Biol Chem 1977; 252: 6432-6437
    PubMedSearch in Google Scholar
  • 15 Wuepper KD, Cochrane CG. Plasma prekallikrein: Isolation, characterization and mechanism of activation. J Exp Med 1972; 135: 1-20
    CrossrefPubMedSearch in Google Scholar
  • 16 Kerbiriou DM, Griffin JH. Human high molecular weight kininogen. Studies of structure-function relationships and of proteolysis of the molecule occurring during contact activation of plasma. J Biol Chem 1979; 254: 12020-12027
    PubMedSearch in Google Scholar
  • 17 Schiffman S, Mannhalter C, Tyner KD. Human high molecular weight kininogen. Effects of cleavage by kallikrein on protein structure and procoagulant activity. J Biol Chem 1980; 255: 6433-6438
    PubMedSearch in Google Scholar
  • 18 Me Conahey PJ, Dixon FJ. A method for trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol 1966; 29: 185-189
    CrossrefPubMedSearch in Google Scholar
  • 19 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970; 227: 680-685
    CrossrefPubMedSearch in Google Scholar
  • 20 Towbin H, Gordon J. Immunoblotting and dot immunobinding -current status and outlook. J Immunol Methods 1984; 72: 313-340
    CrossrefPubMedSearch in Google Scholar
  • 21 Burnette WN. “Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 1981; 112: 195-203
    CrossrefPubMedSearch in Google Scholar
  • 22 Berrettini M, Lammle B, White T, Heeb MJ, Schwarz HB, Zuraw B, Curd J, Griffin JH. Detection of in vitro and in vivo cleavage of high molecular weight kininogen in human plasma by immunoblotting with monoclonal antibodies. Blood 1986; 68: 455-462
    PubMedSearch in Google Scholar
  • 23 Lämmle B, Berrettini M, Griffin JH. Enhanced specificity of immunoblotting using radiolabeled antigen overlay. Studies of blood coagulation Factor XII and prekallikrein in plasma. Anal Biochem 1986 156. 118-125
    PubMedSearch in Google Scholar
  • 24 Tankersley DL, Finlayson JS. Kinetics of activation and autoactivation of human Factor XII. Biochemistry 1984; 23: 273-279
    CrossrefPubMedSearch in Google Scholar
  • 25 Scott CF, Silver LD, Purdon AD, Colman RW. Cleavage of human high molecular weight kininogen by Factor XIa in vitro. Effect on structure and function. J Biol Chem 1985 260. 10856-10863
    PubMedSearch in Google Scholar
  • 26 Mori K, Nagasawa S. Studies on human high molecular weight (HMW) kininogen. Structural change of HMW kininogen by the action of human plasma kallikrein. J Biochem 1981; 89: 1465-1473
    CrossrefPubMedSearch in Google Scholar
  • 27 Wiggins RC. Kinin release from high molecular weight kininogen in the absence of kallikrein. J Biol Chem 1983; 258: 8963-8970
    PubMedSearch in Google Scholar
  • 28 Kleniewski J, Donaldson VH, Wagner CJ. Some molecular and functional changes in high molecular weight kininogen induced by plasmin and trypsin. Thromb Res 1982; 25: 387-399
    CrossrefPubMedSearch in Google Scholar
  • 29 Maier M, Spragg J, Schwartz LB. Inactivation of human high molecular weight kininogen by human mast cell tryptase. J Immunol 1983; 130: 2352-2356
    PubMedSearch in Google Scholar