Thromb Haemost 1992; 67(01): 060-062
DOI: 10.1055/s-0038-1648380
Original Articles
Schattauer GmbH Stuttgart

Presence and Possible Origin of ɛ(γ-Glutamyl)Lysine Isodipeptide in Human Plasma

J Harsfalvi
Department of Biochemistry, University School of Medicine, Debrecen
,
E Tarcsa
*   The 2nd Department of Medicine, University School of Medicine, Debrecen
,
M Udvardy
Department of Biochemistry, University School of Medicine, Debrecen
,
G Zajka
#   Institute of lsotopes, Hungarian Academy of science, Budapest, Hungary
,
T Szarvas
#   Institute of lsotopes, Hungarian Academy of science, Budapest, Hungary
,
L Fesus
*   The 2nd Department of Medicine, University School of Medicine, Debrecen
› Author Affiliations
Further Information

Publication History

Received 15 May 1991

Accepted after revision 15 August 1991

Publication Date:
02 July 2018 (online)

Summary

ɛ(γ-glutamyl)lysine isodipeptide has been detected in normal human plasma by a sensitive HPLC technique in a concentration of 1.9-3.6 μmol/1. Incubation of in vitro clotted plasma at 37° C for 12 h resulted in an increased amount of isodipeptide, and there was no further significant change when streptokinase was also present. Increased in vivo isodipeptide concentrations were also observed in hypercoagulable states and during fibrinolytic therapy.

 
  • References

  • 1 Matacic SS, Loewy AG. The identification of isodipeptide crosslinks in insoluble fibrin. Biochem Biophys Res Commun 1968; 30: 356-362
  • 2 Pisano JJ, Finlayson JS, Peyton MP. Crosslink in fibrin polymerized by factor XIII: ɛ(γ-glutamyl)lysine. Science 1968; 160: 892-893
  • 3 Folk JE, Chung SI. Molecular and catalytic properties of transglutaminases. Adv Enzymol 1973; 38: 109-191
  • 4 Loewy AG. The Ne-(γ-glutamic) lysine cross-link: method of analysis, occurrence in extracellular and cellular proteins. In: Methods in Enzymology. Wold F, Moldave K. (eds). Academic Press; New York: 1984. pp 241-257
  • 5 Folk JE. Transglutaminase. Annu Rev Biochem 1980; 49: 517-531
  • 6 Fesus L, Thomazy V. Searching for the function of tissue transglutaminase: its possible involvement in the biochemical pathway of programmed cell death. In: Advances in Experimental Medicine and Biology. Vol 231. Advances in Posttranslational Modification of Proteins and Aging. Zappia V, Galletti P, Porta R, Wold F. (eds). Plenum Press; New York and London: 1988. pp 119-134
  • 7 Fesus L, Thomazy V, Autuory F, Ceru MM, Tarcsa E, Piacentini M. Apoptotic hepatocytes become insoluble in detergents and chaotropic agents. FEBS Lett 1989; 245: 150-154
  • 8 Fesus L, Tarcsa E. Formation of Ne-(γ-glutamyl)lysine isodipeptide in Chinese-hamster ovary cells. Biochem J 1989; 263: 843-848
  • 9 Tarcsa E, Fesus L. Determination of s(γ-glutamyl)-lysine crosslink in proteins using phenylisothiocyanate derivatization and high pressure liquid chromatographic separation. Anal Biochem 1990; 186: 135-140
  • 10 Fink ML, Chung SI, Folk JE. γ-glutamylamine cyclotransferase: specificity toward ε(γ-glutamyl)lysine and related compounds. Proc Natl Acad Sci USA 1980; 77: 4564-4568
  • 11 Folk JE. Synthesis of N1-(γ-glutamyl)spermidine, N8-(γ-glutamyl) spermidine, N1, N8-bis(γ-glutamyl)spermidine, N1(γ-glutamytysper-mine, N1, N12-bis(γ-glutamyl)spermine and N1, N4-bis(γ-glutamyl) putrescine. Methods Enzymol 1983; 94: 451-457
  • 12 Gron B, Bennick A, Nieuwenhuizen W, Brosstad F. Normal and fibrinaemic patient plasma contain high-molecular weight crosslinked fibrin(ogen) derivatives with intact fibrinopeptide A. Thromb Res 1990; 57: 259-270
  • 13 Pizzo SV, Taylor RM, Schwartz ML, Hill RL, McKee PA. Subunit structure of fragment D from fibrinogen and cross-linked fibrin. J Biol Chem 1973; 248: 4584-4590
  • 14 Gaffney PJ, Brasher M. Subunit structure of the plasmin-induced degradation products of cross-linked fibrin. Biochim Biophys Acta 1973; 295: 308-313
  • 15 Gaffney PJ, Lane DA, Kakkar W, Brasher M. Characterisation of a soluble D dimer-E complex in crosslinked fibrin digest. Thromb Res 1975; 7: 89-99
  • 16 Purves LR, Lindsey GG, Franks JJ. Sides of D-domain interaction in human fibrin-derived D-dimer. Biochemistry 1980; 19: 4051-4058
  • 17 Brenner B, Francis CW, Totterman S, Kessler CM, Rao AK, Rubin R, Kwaan HC, Gabriel KR, Marder VJ. Quantitation of venous clot lysis with the D-dimer immunoassay during fibrinolytic therapy requires correction for soluble fibrin degradation. Circulation 1990; 81: 1818-1825
  • 18 Boisclair MD, Ireland H, Lane DA. Assessment of hypercoagulable states by measurement of activation fragments and peptides. Blood Rev 1990; 4: 25-40
  • 19 Mosesson MW. Fibrin polymerization and its regulatory role in hemostasis. J Lab Clin Med 1990; 116: 8-17
  • 20 Langleben D, Moroz LA, Schlesinger RD, McCans JL, Dragatakis L, Latour PV, Gosselin C, Rosenberg A. Cellular phase fibrinolysis and coronary reperfusion during acute myocardial infarction: A study in patients receiving intravenous streptokinase-methylprednisolone therapy. Thromb Res 1990; 59: 247-258
  • 21 Thomazy V, Fesus L. Differential expression of tissue transglutaminase in human cells. Cell Tissue Res 1989; 255: 215-224
  • 22 Fesus L, Tarcsa E, Kedei N, Autuori F, Piacentini M. Degradation of cells dying by apoptosis leads to accumulation of ε(γ-glutamyl)lysine isodipeptide in culture fluid and blood. FEBS Lett 284 1991; 109-112
  • 23 Fink ML. Breakdown of the ɛ(γ-glutamyl)Lysine crosslink by γ-glutamylamine cyclotransferase and γ-glutamyltranspeptidase (abs). Noble Conference in Cellular and Molecular Biology. “Transglutaminase and Protein Crosslinking Reactions”. Miami: 1987