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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Editorial Board Member: Gillery, Philippe / Kazmierczak, Steven / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Schlattmann, Peter / Whitfield, John B.

13 Issues per year

IMPACT FACTOR 2013: 2.955
Rank 5 out of 29 in category Medical Laboratory Technology in the 2013 Thomson Reuters Journal Citation Report/Science Edition

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Matrix metalloprotease-2 and -9 concentration and activity in serum and culture medium samples: a methodological reappraisal

Chiara Colotti1 / Valeria Angeli2 / Silvia Del Ry3 / Maristelli Maltinti4 / Simona Vittorini5 / Daniela Giannessi6

1Scuola Superiore S. Anna, Pisa, Italy

2CNR Institute of Clinical Physiology Pisa, Pisa, Italy

3CNR Institute of Clinical Physiology Pisa, Pisa, Italy

4CNR Institute of Clinical Physiology Pisa, Pisa, Italy

5CNR Institute of Clinical Physiology Pisa, Pisa, Italy

6CNR Institute of Clinical Physiology Pisa, Pisa, Italy

Corresponding author: Dr. Daniela Giannessi, CNR Institute of Clinical Physiology, Area della Ricerca, Via Moruzzi, 1, 56100 Pisa, Italy Phone: +39-050-3152664, Fax: +39-050-3152166,

Citation Information: Clinical Chemical Laboratory Medicine. Volume 45, Issue 10, Pages 1292–1298, ISSN (Online) 14374331, ISSN (Print) 14346621, DOI: 10.1515/CCLM.2007.283, October 2007

Publication History

Received:
2007-05-10
Accepted:
2007-06-11
Published Online:
2007-10-10

Abstract

Background: Matrix metalloproteases (MMPs) play an important role in cardiovascular remodeling by degrading the extracellular matrix. The aim of this study was to compare two different methods for MMP-2 and MMP-9 concentration and activity determination.

Methods: MMP-2 and -9 levels were measured by immunometric and enzymatic assays to determine total and active levels. The two procedures differ in assay principle and in the extent of cross-reactions with interfering substances present in biological samples. Both human serum and culture medium from an ex vivo human model of intimal hyperplasia were checked.

Results: All methods were able to detect MMP-2 and -9 with similar levels of sensitivity, reproducibility and accuracy, and furnished positively related results, although significantly different, in both types of sample. Both systems were able to detect changes in MMP production such as the time-course of MMP-2 and -9 release by cultured saphenous vein associated with intima hyperplasia progression.

Conclusions: Our data indicate that different values for MMP concentrations can be obtained using different analytical methods, even if they are intrinsically reliable. This suggests that methodological differences should be taken into account when comparing MMP results from different studies.

Clin Chem Lab Med 2007;45:1292–8.

Keywords: ELISA; enzymatic assay; matrix metalloproteases (MMP); MMP serum levels; restenosis

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