Effects of anticoagulants on the activity of gelatinases

Clinical Biochemistry

Volumn 40, Issue 16-17, 2007, Pages 1272-1276

  Castellazzi, Massimiliano ^a   Tamborino, Carmine ^a   Fainardi, Enrico ^b   Manfrinato, Maria C ^a   Granieri, Enrico ^a   Dallocchio, Franco ^a   Bellini, Tiziana ^a  

^a UNIVERSITY OF FERRARA   (Italy)

^b UNIVERSITY HOSPITAL OF FERRARA   (Italy)

Author keywords

Activity assay; Anticoagulants; Metalloproteinases

Indexed keywords

ANTICOAGULANT AGENT; CALCIUM; CHELATING AGENT; CITRIC ACID; EDETIC ACID; GELATINASE A; GELATINASE B; HEPARIN;

ADULT; ANTICOAGULATION; ARTICLE; BLOOD CLOTTING; BLOOD SAMPLING; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; HUMAN; HUMAN CELL; HUMAN EXPERIMENT; HUMAN TISSUE; MALE; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; THROMBOCYTE; VOLUNTEER;

ADULT; ANTICOAGULANTS; BLOOD SPECIMEN COLLECTION; CITRATES; CITRIC ACID; EDETIC ACID; ENZYME ACTIVATION; FEMALE; GELATINASES; HEPARIN; HUMANS; MALE; MATRIX METALLOPROTEINASE 2; MATRIX METALLOPROTEINASE 9; PLASMA; SERUM;

EID: 35248878176     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2007.08.011     Document Type: Article

References (26)

1. Massova I., Kotra L.P., Fridman R., and Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 12 (1998) 1075-1095
2. Lemaitre V., and Armiento DJ. Matrix metalloproteinases in development and disease. Birth Defects Res. C Embryo Today 78 (2006) 1-10
3. Nagase H. Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378 (1997) 151-160
4. Yong V.W. Metalloproteinases: mediators of pathology and regeneration in the CNS. Nat. Rev., Neurosci. 6 (2005) 931-944
5. Prince H.E. Biomarkers for diagnosing and monitoring autoimmune diseases. Biomarkers 10 Suppl. 1 (2005) S44-S49
6. Turpeenniemi-Hujanen T. Gelatinases (MMP-2 and -9) and their natural inhibitors as prognostic indicators in solid cancers. Biochimie 87 (2005) 287-297
7. Gontero P., Banisadr S., Frea B., and Brausi M. Metastasis markers in bladder cancer: a review of the literature and clinical considerations. Eur. Urol. 46 (2004) 296-311
8. Castillo J., and Rodriguez I. Biochemical changes and inflammatory response as markers for brain ischaemia: molecular markers of diagnostic utility and prognosis in human clinical practice. Cerebrovasc. Dis. 17 Suppl. 1 (2004) 7-18
9. Jung K., Lein M., Laube C., and Lichtinghagen R. Blood specimen collection methods influence the concentration and the diagnostic validity of matrix metalloproteinase 9 in blood. Clin. Chim. Acta 314 (2001) 241-244
10. Alby C., BenAbdesselam O., Foglietti M.J., and Beaudeux J.L. Preanalytical aspects regarding the measurement of metalloproteinase-9 and tissue inhibitor or metalloproteinase-1 in blood. Clin. Chim. Acta 325 (2002) 183-186
11. Mannello F. Effects of blood collection methods on gelatin zymography of matrix metalloproteinases. Clin. Chem. 49 (2003) 339-340
12. Mannello F., Luchetti F., Canonico B., and Papa S. Effect of anticoagulants and cell separation media as preanalytical determinants on zymographic analysis of plasma matrix metalloproteinases. Clin. Chem. 49 (2003) 1956-1957
13. Jung K., Meisser A., and Bischof P. Blood sampling as critical preanalytical determinant to use circulating MMP and TIMP as surrogate markers for pathological processes. Int. J. Cancer 116 (2005) 1000-1001 (author reply 1002-1003)
14. Makowski G.S., and Ramsby M.L. Use of citrate to minimize neutrophil matrix metalloproteinase-9 in human plasma. Anal. Biochem. 322 (2003) 283-286
15. Gerlach R.F., Uzuelli J.A., Souza-Tarla C.D., and Tanus-Santos J.E. Effect of anticoagulants on the determination of plasma matrix metalloproteinase (MMP)-2 and MMP-9 activities. Anal. Biochem. 344 (2005) 147-149
16. Sawicki G., Sanders E.J., Salas E., Wozniak M., Rodrigo J., and Radomski M.W. Localization and translocation of MMP-2 during aggregation of human platelets. Thromb. Haemost. 80 (1998) 836-839
17. Sheu J.R., Fong T.H., Liu C.M., et al. Expression of matrix metalloproteinase-9 in human platelets: regulation of platelet activation in in vitro and in vivo studies. Br. J. Pharmacol. 143 (2004) 193-201
18. Hanemaaijer R., Visser H., Konttinen Y.T., Koolwijk P., and Verheijen J.H. A novel and simple immunocapture assay for determination of gelatinase-B (MMP-9) activities in biological fluids: saliva from patients with Sjogren's syndrome contain increased latent and active gelatinase-B levels. Matrix Biol. 17 (1998) 657-665
19. Fainardi E., Castellazzi M., Bellini T., et al. Cerebrospinal fluid and serum levels and intrathecal production of active matrix metalloproteinase-9 (MMP-9) as markers of disease activity in patients with multiple sclerosis. Mult. Scler. 12 (2006) 294-301
20. Verheijen J.H., Nieuwenbroek N.M., Beekman B., et al. Modified proenzymes as artificial substrates for proteolytic enzymes: colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase. Biochem. J. 323 Pt 3 (1997) 603-609
21. Gerlach R.F., and TanusSantos J.E. Misuse of serum matrix metalloproteinase (MMP)-9 and tissue inhibitor of metalloproteinase (TIMP)-1 as a biomarker in multiple sclerosis. Mult. Scler. 12 (2006) 120
22. Fainardi E., Castellazzi M., Bellini T., and Dallocchio F. Matrix metalloproteinases (MMP): determination of different forms by different techniques may require different preanalytical strategies. Mult. Scler. 13 (2007) 561-562
23. Springman E.B., Angleton E.L., Birkedal-Hansen H., and VanWart H.E. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 364-368
24. Van Wart H.E., and Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 5578-5582
25. Okada Y., Morodomi T., Enghild J.J., et al. Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194 (1990) 721-730
26. Kenagy R.D., Nikkari S.T., Welgus H.G., and Clowes A.W. Heparin inhibits the induction of three matrix metalloproteinases (stromelysin, 92-kD gelatinase, and collagenase) in primate arterial smooth muscle cells. J. Clin. Invest. 93 (1994) 1987-1993