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Matrix metalloprotease-2 and -9 concentration and activity in serum and culture medium samples: a methodological reappraisal
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Chiara Colotti
Veröffentlicht/Copyright:
10. Oktober 2007
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.
Received: 2007-5-10
Accepted: 2007-6-11
Published Online: 2007-10-10
Published in Print: 2007-10-01
©2007 by Walter de Gruyter Berlin New York
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Schlagwörter für diesen Artikel
ELISA;
enzymatic assay;
matrix metalloproteases (MMP);
MMP serum levels;
restenosis
Artikel in diesem Heft
- Atrial natriuretic peptide and related peptides
- The −374A allele of the receptor for advanced glycation end products (RAGE) gene promoter is a protective factor against cardiovascular lesions in type 2 diabetes mellitus patients
- Biochemical properties of endogenous presenilin 1 and presenilin 2 in cultured human B-lymphocytes
- CD36 polymorphism and its relationship with body mass index and coronary artery disease in a Korean population
- Preservation of RNA for functional analysis of separated alleles in yeast: comparison of snap-frozen and RNALater® solid tissue storage methods
- Mother-child double incompatibility at vWA and D5S818 loci in paternity testing
- Matrix metalloprotease-2 and -9 concentration and activity in serum and culture medium samples: a methodological reappraisal
- Are changes in blood-ethanol concentration during storage analytically significant? Importance of method imprecision
- Measurement of arginine derivatives in pediatric patients with chronic kidney disease using high-performance liquid chromatography-tandem mass spectrometry
- The soluble transferrin receptor reflects tumor load in chronic lymphocytic leukemia
- Calculated low-density lipoprotein cholesterol remains a viable and important test for screening and targeting therapy
- Angiotensin-converting enzyme (ACE) I/D corrected serum ACE activity and severity assessment of community-acquired pneumonia
- Differentiating transudative from exudative pleural effusion: should we measure effusion cholesterol dehydrogenase?
- Association of classical and related inflammatory markers with high-sensitivity C-reactive protein in healthy individuals: results from the Stanislas cohort
- Cytokines and growth factors in mostly atherosclerotic patients on hemodialysis determined by biochip array technology
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- High plasma levels of tissue inhibitor of metalloproteinase-1 (TIMP-1) and interleukin-8 (IL-8) characterize patients prone to ventricular fibrillation complicating myocardial infarction
- Methylprednisolone, cortisol and the cell-mediated immune response in children after ventricular septal defect repair
- Standardization of γ-glutamyltransferase assays by intermethod calibration. Effect on determining common reference limits
- The effect of endurance exercise-induced lactacidosis on biochemical markers of bone turnover
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- National survey on critical values reporting in a cohort of Italian laboratories
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