Monoclonal antibodies detect receptor-induced binding sites in Glu-plasminogen

Blood

Volumn 118, Issue 6, 2011, Pages 1653-1662

  Han, Jaena ^a   Baik, Nagyung ^a   Kim, Kee Hwan ^a   Yang, Jian Ming ^a   Han, Gye Won ^a   Gong, Yun ^b   Jardí, Mercè ^c   Castellino, Francis J ^d   Felez, Jordi ^e   Parmer, Robert J ^f,g   Miles, Lindsey A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

^c CENTRE FOR GENOMIC REGULATION CRG   (Spain)

^d UNIVERSITY OF NOTRE DAME   (United States)

^e INSTITUT CATALÀ DE LA SALUT   (Spain)

^f UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^g VA SAN DIEGO HEALTHCARE SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; EPITOPE; FIBRIN; FIBRINOGEN; GLUTAMIC ACID; LYSINE; MATRIGEL; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 109; MONOCLONAL ANTIBODY 116; MONOCLONAL ANTIBODY 20; MONOCLONAL ANTIBODY 49; MONOCLONAL ANTIBODY 51; MONOCLONAL ANTIBODY 53; MONOCLONAL ANTIBODY MOPC21; PEPTIDE; PLASMIN; PLASMINOGEN; PLASMINOGEN RECEPTOR; PROTEIN PLG RKT; PROTEINASE; RECEPTOR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; IMMUNOAFFINITY CHROMATOGRAPHY; KRINGLE DOMAIN; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; TANDEM MASS SPECTROMETRY;

EID: 80051614695     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-11-316943     Document Type: Article

References (39)

1. Miles LA, Hawley SB, Baik N, et al. Plasminogen receptors: the sine qua non of cell surface plasminogen activation. Front Biosci. 2005;10:1754-1762. (Pubitemid 40529035)
2. Saksela O. Plasminogen activation and regulation of pericellular proteolysis. Biochim Biophys Acta. 1985;823(1):35-65. (Pubitemid 16233163)
3. Testa JE, Quigley JP. Protease receptors on cell surfaces: new mechanistic formulas applied to an old problem. J Natl Cancer Inst. 1988;80(10):712-713.
4. Gong Y, Kim S-O, Felez J, et al. Conversion of glu-plasminogen to lys-plasminogen is necessary for optimal stimulation of plasminogen activation on the endothelial cell surface. J Biol Chem. 2001;276(22):19078-19083.
5. Miles LA, Castellino FJ, Gong Y. Critical role for conversion of glu-plasminogen to Lys-plasminogen for optimal stimulation of plasminogen activation on cell surfaces. Trends Cardiovasc Med. 2003;13(1):21-30. (Pubitemid 36120546)
6. Zhang L, Gong Y, Grella DK, Castellino FJ, Miles LA. Endogenous plasmin converts Glu-plasminogen to Lys-plasminogen on the monocytoid cell surface. J Thromb Haemost. 2003;1(6):1264-1270.
7. Hoylaerts M, Rijken DC, Lijnen HR, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. J Biol Chem. 1982;257(6):2912-2919. (Pubitemid 12118804)
8. Zamarron C, Ginsberg MH, Plow EF. Monoclonal antibodies specific for a conformationally altered state of fibrinogen. Thromb Haemost. 1990;64(1):41-46. (Pubitemid 20301848)
9. Zamarron C, Ginsberg M, Plow EF. A receptorinduced binding site in fibrinogen elicited by its interaction with platelet membrane glycoprotein IIb-IIIa. J Biol Chem. 1991;266(24):16193-16199. (Pubitemid 21907783)
10. Deutsch DG, Mertz ET. Plasminogen: Purification from human plasma by affinity chromatography. Science. 1970;170(962):1995-1996.
11. Parmer RJ, Mahata M, Gong Y, et al. Processing of chromogranin A by plasmin provides a novel mechanism for regulating catecholamine secretion. J Clin Invest. 2000;106(7):907-915.
12. Sottrup-Jensen L, Claeys H, Zajdel M, Petersen TE, Magnusson S. The primary structure of human plasminogen: isolation of two lysine-binding fragments and one "mini-plasminogen" (MW 38,000) by elastase-catalyzed-specific limited proteolysis. In: Davidson JF, Rowan RM, Samama MM, Desnoyers PC, eds. Progress in Chemical Fibrinolysis and Thrombolysis, Vol. 3. New York, NY: Raven Press;1978:191-209.
13. Miles LA, Dahlberg CM, Plow EF. The cell-binding domains of plasminogen and their function in plasma. J Biol Chem. 1988;263(24):11928-11934.
14. Mitchell JW, Baik N, Castellino FJ, Miles LA. Plasminogen inhibits TNF{alpha}-induced apoptosis in monocytes. Blood. 2006;107(11):4383-4390. (Pubitemid 43801364)
15. Parmer CM, Baik N, Miles LA. Ligand recognition specificity of the novel plasminogen receptor, Plg-RKT [abstract]. J Thromb Haemost. 2009;6:Abstract P9.
16. Miles LA, Dahlberg CM, Levin EG, Plow EF. Gangliosides interact directly with plasminogen and urokinase and may mediate binding of these components to cells. Biochemistry. 1989;280(24):9337-9343.
17. Keller A, Nesvizhskii AI, Kolker E, Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem. 2002;74(20):5383-5392. (Pubitemid 35215372)
18. Andronicos NM, Chen EI, Baik N, et al. Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation. Blood. 2010;115(7):1319-1330.
19. Miles LA, Sebald MT, Fless GM, et al. Interaction of lipoprotein (a) [Lp (a)] with the extracellular matrix. Fibrinolysis Proteolysis. 1998;12(2):79-87.
20. Orkin RW, Gehron P, McGoodwin EB, et al. A murine tumor producing a matrix of basement membrane. J Exp Med. 1977;145(1):204-220. (Pubitemid 8010101)
21. Albini A, Kleinman HK, Martin GR, et al. A rapid in vitro assay for quantitating the invasive potential of tumor cells. Cancer Res. 1987;47(12):3239-3245. (Pubitemid 17082655)
22. Kleinman HK, McGarvey ML, Hassell JR, et al. Basement membrane complexes with biological activity. Biochemistry. 1986;25(2):312-318. (Pubitemid 16053790)
23. Matrisian LM. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 1990;6(4):121-125.
24. Wiman B. Primary structure of peptides released during activation of human plasminogen by urokinase. Eur J Biochem. 1973;39(1):1-9.
25. Wiman B, Wallen P. Activation of human plasminogen by an insoluble derivative or urokinase. Structural changes of plasminogen in the course of activation to plasmin and demonstration of a possible intermediate complex. Eur J Biochem. 1973;36(1):25-31.
26. Violand BN, Castellino FJ. Mechanism of the urokinase-catalyzed activation of human plasminogen. J Biol Chem. 1976;251(13):3906-3912.
27. Horrevoets AJG, Smilde AE, Fredenburgh JC, Pannekoek H, Nesheim ME. The activation-resistant conformation of recombinant human plasminogen is stabilized by basic residues in the amino-terminal hinge region. J Biol Chem. 1995;270(26):15770-15776.
28. Claeys H, Vermylen J. Physico-chemical and proenzyme properties of NH2-terminal glutamic acid and NH2-terminal lysine human plasminogen. Influence of 6-aminohexanoic acid. Biochim Biophys Acta. 1974;342(2):351-359.
29. Thorsen S, Mullertz S. Rate of activation and electrophoretic mobility of unmodified and partially degraded plasminogen. Effects of 6-aminohexanoic acid and related compounds. Scand J Clin Lab Invest. 1974;34(2):167-176.
30. Markus G, Evers JL, Hobika GH. Comparison of some properties of natiave (glu) and modified (lys) human plasminogen. J Biol Chem. 1978;253(3):733-739. (Pubitemid 8271448)
31. Markus G, Priore RL, Wissler FC. The binding of tranexamic acid to native (Glu) and modified (Lys) human plasminogen and its effect on conformation. J Biol Chem. 1979;254(4):1211-1216.
32. Pappin DJ, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol. 1993;3(6):327-332.
33. Castellino FJ, Ploplis VA. Structure and function of the plasminogen/plasmin system. Thromb Haemost. 2005;93(4):647-654. (Pubitemid 40485399)
34. Castellino FJ, McCance SG. The kringle domains of human plasminogen. Ciba Found Symp. 1997;212:46-60.
35. Ho-Tin-Noe B, Rojas G, Vranckx R, Lijnen HR, Angles-Cano E. Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmininduced cell detachment and apoptosis. FEBS J. 2005;272(13):3387-3400. (Pubitemid 40979309)
36. Cockell CS, Marshall JM, Dawson KM, Cederholm-Williams SA, Ponting CP. Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptide. Biochem J. 1998;333(Pt 1):99-105. (Pubitemid 28342498)
37. Dejouvencel T, Doeuvre L, Lacroix R, et al. Fibrinolytic cross-talk: a new mechanism for plasmin formation. Blood. 2010;115(10):2048-2056.
38. Miles LA, Dahlberg CM, Plescia J, et al. Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry. 1991;30(6):1682-1691.
39. Longstaff C, Clough AM, Gaffney PJ. Kinetics of plasmin actiavation of single chain urinary-type plasminogen activator(scu-PA) and demonstration of a high affinity interaction between scu-PA and plasminogen. J Biol Chem. 1992;267(1):173-179.