Serum or Plasma Samples?
2008; Lippincott Williams & Wilkins; Volume: 28; Issue: 4 Linguagem: Letão
10.1161/atvbaha.107.159608
ISSN1524-4636
Autores Tópico(s)Blood properties and coagulation
ResumoHomeArteriosclerosis, Thrombosis, and Vascular BiologyVol. 28, No. 4Serum or Plasma Samples? Free AccessEditorialPDF/EPUBAboutView PDFView EPUBSections ToolsAdd to favoritesDownload citationsTrack citationsPermissions ShareShare onFacebookTwitterLinked InMendeleyReddit Jump toFree AccessEditorialPDF/EPUBSerum or Plasma Samples?The "Cinderella" Role of Blood Collection Procedures Preanalytical Methodological Issues Influence the Release and Activity of Circulating Matrix Metalloproteinases and Their Tissue Inhibitors, Hampering Diagnostic Trueness and Leading to Misinterpretation Ferdinando Mannello Ferdinando MannelloFerdinando Mannello From the Institute of Histology and Laboratory Analysis, Faculty of Sciences and Technologies, University "Carlo Bo", Urbino, Italy. Originally published1 Apr 2008https://doi.org/10.1161/ATVBAHA.107.159608Arteriosclerosis, Thrombosis, and Vascular Biology. 2008;28:611–614Dysregulations of the synthesis and breakdown of the extracellular matrix (ECM) is a key processes in the physiopathology of vascular remodeling and the development of atherothrombotic syndromes.1–4 Matrix metalloproteinases (MMPs) are endopeptidases, belonging to the matrixin family that can degrade almost all the ECM components.5 Although there is little doubt that MMPs are an important components in cancer invasion and metastasis,6 they are also regarded as key regulatory molecules in degenerative processes and inflammation,5,7 as playing roles also in physiopathological remodeling of the vascular wall2,8 and as the pathogenesis of cardio- and cerebrovascular diseases.9,10 Thus, MMPs have emerged as potential biomarkers of atherothrombotic risk and predictors of coronary and cerebrovascular disease recurrence.8ATVB 2008;28:e15–e16.Normal and diseased blood vessel wall cells may upregulate and activate MMPs in a multistep fashion, driven in part by soluble cytokines and cell–cell interactions with platelets and white blood cells. Enhanced MMP activation (alone or in concert with the fibrinolytic system) contributes to increased matrix turnover, which may have beneficial effects (eg, in vascular repair and atherosclerotic plaque stabilization)11 but also detrimental effects (eg, in vascular intimal thickening, atherosclerosis, and in thrombotic syndromes).12Because the changes on the cellular level are reflected in body fluids, determination of MMPs in blood have been recommended as noninvasive tools in the diagnosis and monitoring of several diseases.13 It has been demonstrated repeatedly that both the MMP/tissue inhibitor of matrix metalloproteinase (TIMP) assay and zymography essentially depend on the blood sampling procedures, with some MMPs and TIMPs having higher concentrations in serum than in plasma.14–41 Although assays for an ever-increasing number of MMPs are now commercially available, the preanalytical impact of blood collection methods needs careful evaluation to limit technical pitfalls that may lead to misinterpretation. This needs to be done before the diagnostic validity of these assays can be explored in clinical trials.Among matrixins, MMPs are Ca/Zn-dependent proteinases that can extensively degrade almost all ECM components. Beginning with the discovery of tadpole collagenase in 1962,42 the focus of MMP research for the subsequent 4 decades has been on the proteolysis of ECM proteins, with recent emphasis on cell signaling activities.5 After increased levels of gelatinases, which mainly digest key components of the basement membrane, were identified in cancer cells, MMPs were also implicated in invasion, metastasis, and angiogenesis.6 MMPs are increased not only in cancer cells; stromal and inflammatory cells also showed enhanced MMP activity.5,6 Moreover, increased MMPs have been identified in a wide variety of physiological (eg, cell development, organogenesis, tissue remodeling, apoptosis)43–45 and nonmalignant pathological conditions (eg, inflammatory diseases, such as arthritis, colitis, and periodontitis; shock; atherosclerosis; neurodegenerative syndromes; stroke; cerebro- and cardiovascular diseases; pregnancy).5,46 The release of proteinase into the circulation makes MMP assays and zymography promising biochemical tools in both diagnosis and monitoring of a variety of diseases.13Approximately 20 years ago, it was first described that peripheral blood contains several forms of MMPs47 (ie, soluble constitutive form in plasma, and intracellular zymogens in platelets and leukocytes).48,49 The discrepancy in MMP concentrations between serum and plasma was reported for the first time ≈15 years ago,14 but only beginning in 199617 has the influence of the blood sampling process on MMP concentrations and zymographic profiles been carefully evaluated.18–41 In particular, although MMP-2 and TIMP-2 (activity and concentration) show no significant difference between plasma and serum,15,19,23,24,26,30–32,34,36,50 the levels and zymographic separation of the MMP-1, -8, and -9 forms and TIMP-1 are strongly affected by anticoagulants.14,16–20,22,24–26,28–30,32,33,36,37,40,42 Moreover, serum was found to contain higher levels of TIMP-1 and MMP-1, -3, and -9 forms than those in anticoagulated plasma,17,18,20–22,24,26–28,33–36,40 which suggests a releasing mechanism during coagulation and fibrinolysis.38,51 Accordingly, MMP-9 forms show different expression in serum collected with or without silica-based clot activators.20,21,24,26–29,34,39,41In this issue of Arteriosclerosis, Thrombosis, and Vascular Biology, Jung52 describes the effect of blood sampling on collagenase-2 (EC 3.4.24.34; MMP-8) and TIMP-1 concentrations, providing further evidence that, like gelatinases, stromelysins, and matrilysins, collagenases and TIMPs also behave differently in plasma and serum.Although the report by Jung,52 in agreement with previous studies,14–41 demonstrates that the "artificially" higher levels of serum MMPs could hamper their diagnostic validity, some investigators continue to neglect the importance of blood sampling thereby, generating serious preanalytical flaws that may undermine confidence in the conclusions of otherwise well-conceived studies.To avoid pitfalls that may lead to false conclusions, who use it is important that investigators or clinicians blood MMPs as surrogate biomarkers, or who study their role in pathophysiology, be cognizant of the crucial impact of blood sampling and handling (Figure). Download figureDownload PowerPointFigure. Schematic representation of MMP secretion in serum (with and without clot accelerators) and plasma (with citrate as anticoagulant). During both the coagulation and the fibrinolysis pathways, in the presence or absence of silica/silicate-based clot activators, an enhanced release and activation of MMP-1, -3, -8, and -9 forms occurs in serum. Blood leukocytes (ie, eosinophils, neutrophils, lymphocytes, and monocytes) and platelets contain high amounts of zymogen proforms of MMPs that may be released on activation into blood through the coagulation-induced degranulation, by urokinase-dependent plasminogen activator, and via plasmin-related mechanisms. Intrinsic and extrinsic pathways of coagulation generate fibrin molecules that dose-dependently bind some proforms of MMPs, finally cleared as the active form by plasmin activity. Moreover, thrombin activity may facilitate platelet aggregation and release of active MMP forms. These biochemical mechanisms account for the increased concentrations of MMP forms found in serum versus plasma, in which anticoagulants (in particular sodium citrate and heparin) strongly limit the MMP secretion/release by platelets and leukocytes. Only the constitutive soluble MMP forms can be found in plasma.Platelets and leukocytes contain several TIMPs and MMPs that may be extracellularly released on activation or during aggregation.53–63 The use of anticoagulants (eg, heparin, citrate) limits the mobilization of gelatinase-rich granules of human neutrophils.23,64,65 The major differences between plasma and serum involve TIMP-1 and MMP-1, -8, and -9 forms, and to a much lesser extent MMP-2, which is considered the constitutive gelatinase circulating in blood.47–49 The presence of MMPs in higher amounts in serum than in plasma is related not only to disease status but also to coagulation/fibrinolytic pathways.38 In fact, the rapid separation of serum (minimizing the time between blood drawing and centrifugation) does not prevent the artificially high MMP-9 content in serum.51Other than individual differences in white blood cell count, both the coagulation and fibrinolysis factors may alter the gelatinase, collagenase, and stromelysin expression and activity. During the coagulation process, thrombin facilitates platelet aggregation/activation and secretion of pro- and active MMP-9.66,67 Moreover, thrombin generates fibrin, which binds the fibronectin-like regions present in MMP-9 forms (ie, 92, 130, and 225 kDa); fibrin–proMMP-9 complex is then processed (by plasmin, MMP-3, and urokinase),68–70 finally accumulating active MMP-3 and -9 forms in serum. Moreover, during the fibrinolysis process, urokinase-type plasminogen activator generates plasmin, which stimulates the secretion of pro- and active MMPs from several white blood cells69; accordingly, no active MMP-9 forms were detected in the absence of plasminogen, cathepsins, and stromelysins.71 Finally, silica and silicates (the main components of clot accelerators, sprayed into commercially available plastic devices) were characterized as inducers of in vivo and in vitro release of pro-, active, and complexed forms of several MMPs.39,41The observations of Jung52 are in agreement with data in the literature that demonstrate: (1) Except for MMP-2, -3, and -7 and TIMP-2,15,19,23,24,26,27,30,32,34,36,37,41,50,51 serum (especially with clot accelerators) contains higher amounts and different zymographic profiles than those found in plasma samples (up to now for MMP-1, -4, -8, and -9 and TIMP-1)17,18,20–22,24,26–28,33–36,39–41; (2) anticoagulants interfere with the MMP activity (eg, citrate versus EDTA)14,16–20,22,24–26,28–30,32,33,36,37,40,41; (3) the coagulation/fibrinolysis pathways influence MMP activity but also protein profiles in proteomic studies72–77; and (4) the misuse of serum (in particular when collected with clot accelerators) may generate preanalytical biases.All these data add to the mounting evidence that citrate plasma represents the optimal choice or compromise among anticoagulants to better evaluate MMPs and TIMPs for clinical and diagnostic purposes,21,23,24,27,30,31,33–35,38 especially in vascular biology and atherothrombotic syndromes where the task of unraveling the role of individual MMPs will be very complex and where it is essential to avoid misinterpretations linked to blood collection methods.DisclosuresNone.FootnotesCorrespondence to Ferdinando Mannello, Institute of Histology and Laboratory Analysis, Faculty of Sciences and Technologies, University "Carlo Bo", Via O. 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