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


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