Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1993 Apr 15;291(Pt 2):623–625. doi: 10.1042/bj2910623

Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma.

K Bangert 1, A H Johnsen 1, U Christensen 1, S Thorsen 1
PMCID: PMC1132569  PMID: 8484741

Abstract

Mature alpha 2-plasmin inhibitor in human plasma has 12 more N-terminal residues than hitherto anticipated. The first residue is the methionine at position 28, downstream from the N-terminus of the pre-protein. The cDNA sequence predicts that the site cleaved upon formation of the mature inhibitor is a typical signal-peptidase recognition site. The mature inhibitor (464 residues) and the previously reported, and presumably degraded, form with N-terminal asparagine (452 residues), are present in plasma in about equal amounts. They both form a stable complex with plasmin. Recent studies on a recombinant alpha 2-plasmin inhibitor suggest that the 12 additional residues have functional implications [Sumi, Ichikawa, Nakamura, Miura and Aoki (1989) J. Biochem. 106, 703-707].

Full text

PDF
623

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aoki N., Harpel P. C. Inhibitors of the fibrinolytic enzyme system. Semin Thromb Hemost. 1984 Jan;10(1):24–41. doi: 10.1055/s-2007-1004405. [DOI] [PubMed] [Google Scholar]
  2. Brower M. S., Harpel P. C. Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase. J Biol Chem. 1982 Aug 25;257(16):9849–9854. [PubMed] [Google Scholar]
  3. Christensen U., Clemmensen I. Kinetic properties of the primary inhibitor of plasmin from human plasma. Biochem J. 1977 May 1;163(2):389–391. doi: 10.1042/bj1630389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Christensen U., Ipsen H. H. Steady-state kinetics of plasmin- and trypsin-catalysed hydrolysis of a number of tripeptide-p-nitroanilides. Biochim Biophys Acta. 1979 Aug 15;569(2):177–183. doi: 10.1016/0005-2744(79)90052-4. [DOI] [PubMed] [Google Scholar]
  5. Clemmensen I., Thorsen S., Müllertz S., Petersen L. C. Properties of three different molecular forms of the alpha 2 plasmin inhibitor. Eur J Biochem. 1981 Nov;120(1):105–112. doi: 10.1111/j.1432-1033.1981.tb05675.x. [DOI] [PubMed] [Google Scholar]
  6. Holmes W. E., Lijnen H. R., Collen D. Characterization of recombinant human alpha 2-antiplasmin and of mutants obtained by site-directed mutagenesis of the reactive site. Biochemistry. 1987 Aug 11;26(16):5133–5140. doi: 10.1021/bi00390a036. [DOI] [PubMed] [Google Scholar]
  7. Holmes W. E., Nelles L., Lijnen H. R., Collen D. Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin). J Biol Chem. 1987 Feb 5;262(4):1659–1664. [PubMed] [Google Scholar]
  8. Huber R., Carrell R. W. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry. 1989 Nov 14;28(23):8951–8966. doi: 10.1021/bi00449a001. [DOI] [PubMed] [Google Scholar]
  9. Kluft C., Los N. Demonstration of two forms of alpha 2-antiplasmin in plasma by modified crossed immunoelectrophoresis. Thromb Res. 1981 Jan 1;21(1-2):65–71. doi: 10.1016/0049-3848(84)90033-1. [DOI] [PubMed] [Google Scholar]
  10. Knäuper V., Reinke H., Tschesche H. Inactivation of human plasma alpha 1-proteinase inhibitor by human PMN leucocyte collagenase. FEBS Lett. 1990 Apr 24;263(2):355–357. doi: 10.1016/0014-5793(90)81412-h. [DOI] [PubMed] [Google Scholar]
  11. Lijnen H. R., Holmes W. E., van Hoef B., Wiman B., Rodriguez H., Collen D. Amino-acid sequence of human alpha 2-antiplasmin. Eur J Biochem. 1987 Aug 3;166(3):565–574. doi: 10.1111/j.1432-1033.1987.tb13551.x. [DOI] [PubMed] [Google Scholar]
  12. Lindmark B., Lilja H., Alm R., Eriksson S. The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide. Biochim Biophys Acta. 1989 Jul 27;997(1-2):90–95. doi: 10.1016/0167-4838(89)90139-8. [DOI] [PubMed] [Google Scholar]
  13. Mast A. E., Enghild J. J., Nagase H., Suzuki K., Pizzo S. V., Salvesen G. Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J Biol Chem. 1991 Aug 25;266(24):15810–15816. [PubMed] [Google Scholar]
  14. Rawlings N. D., Polgar L., Barrett A. J. A new family of serine-type peptidases related to prolyl oligopeptidase. Biochem J. 1991 Nov 1;279(Pt 3):907–908. doi: 10.1042/bj2790907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sakata Y., Aoki N. Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest. 1982 Mar;69(3):536–542. doi: 10.1172/JCI110479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Shieh B. H., Travis J. The reactive site of human alpha 2-antiplasmin. J Biol Chem. 1987 May 5;262(13):6055–6059. [PubMed] [Google Scholar]
  17. Suenson E., Thorsen S. The course and prerequisites of Lys-plasminogen formation during fibrinolysis. Biochemistry. 1988 Apr 5;27(7):2435–2443. doi: 10.1021/bi00407a029. [DOI] [PubMed] [Google Scholar]
  18. Sumi Y., Ichikawa Y., Nakamura Y., Miura O., Aoki N. Expression and characterization of pro alpha 2-plasmin inhibitor. J Biochem. 1989 Oct;106(4):703–707. doi: 10.1093/oxfordjournals.jbchem.a122920. [DOI] [PubMed] [Google Scholar]
  19. Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T. Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. J Biochem. 1987 Nov;102(5):1033–1041. doi: 10.1093/oxfordjournals.jbchem.a122141. [DOI] [PubMed] [Google Scholar]
  20. Wiman B. Affinity-chromatographic purification of human alpha 2-antiplasmin. Biochem J. 1980 Oct 1;191(1):229–232. doi: 10.1042/bj1910229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Winyard P. G., Zhang Z., Chidwick K., Blake D. R., Carrell R. W., Murphy G. Proteolytic inactivation of human alpha 1 antitrypsin by human stromelysin. FEBS Lett. 1991 Feb 11;279(1):91–94. doi: 10.1016/0014-5793(91)80258-5. [DOI] [PubMed] [Google Scholar]
  22. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES