Title of Invention: USE OF GSTP1 Abstract: The invention discloses the use of glutathione S-transferase P1 (GSTP1) for the prevention or treatment of cardiomyopathies or ischemic heart diseases and for the diagnosis thereof. Detailed Description: The present invention relates to the use of Glutathione-S-transferase P1. The glutathione S-transferases (GSTs) are a multigene family of isozymes that catalyze the nucleophilic attack of the sulfur atom of glutathione (GSH) on electrophilic groups of substrate molecules. GSTs are known as detoxicating enzymes which conjugate toxic substances with GSH to become more water-soluble products which can be metabolised in the liver and finally excreted out of the body. On the basis of the amino acid sequence, the mammalian GSTs are divided into six classes: alpha, mu, omega, pi, theta and zeta. Among these isozymes, glutathione S-transferase P1 (GSTP1; GST-pi, GSTP1-1) is the most prevalent one in mammalian cells. GSTP1 has also generated interest as a neoplastic marker because it is overexpressed in a variety of different human malignancies, including lung, colon, stomach, esophagus, mouth, kidney, ovary and testicular cancers. Most prostate cancer types contain decreased levels of GSTP1 polypeptide relative to normal prostate tissue due to hypermethylation of the GSTP1 promoter resulting in decreased transcription of GSTP1 (US 2009/0186360 A1). GSTP1 is determinant in cellular response to oxidative stress and protects tumor cells from apoptosis elicited by a variety of cytotoxic agents, such as H2O2, UV, cisplatin, adriamycin, etoposide, thiotepa, chlorambucil, ethacrynic acid and arsenic trioxide. GSTP1 is therefore considered as a promising target in tumour medicine, both as a target for drug action and as a tumor marker. GSTP1 also participates in the regulation of stress signalling and protects cells against apoptosis by the mechanisms related to its non-catalytic and ligand-binding activities. For example, GSTP1 prevents LPS-induced excessive production of proinflammatory factors and plays an anti-inflammatory role in response to LPS. GSTP1 expression, both at transcriptional and translational levels, is up-regulated by LPS stimulation. GSTP1 also functions as an endogenous inhibitor of JNK (c-Jun NH2-terminal kinase), via interaction with the C-terminus. It could also be demonstrated that exogenous (recombinant) GSTP1 protein could be delivered into macrophages and suppressed iNOS and COX-2 expression in cells. Furthermore, intraperitoneally administered GSTP1 protein to mice decreased mortality of endotoxic shock significantly and inhibited acute lung injury and peritonitis (Luo et al., Mol. Immunol. 46 (2009), 848-857). EP 1 500 709 A1 suggests GSTP1 as one of 22 inflammation markers. Various isoforms of GSTP1 have also been found relevant to asthma and childhood allergic diseases due to the interaction of GSTP1 with air pollution from traffic (and tobacco smoke) in the respiratory system, as well as association with hypertension in pregnancy (Ohta et al., Sem. Thr. Hem. 29 (2003), 653-659). Cardiomyopathies (CMP) are a heterogeneous group of diseases, including the dilative (DCM), the most frequent entity among cardiomyopathies, and ischemic (ICM) forms. Although pharmacotherapy and surgical interventions have been improved with survival benefit in CMP, causal treatment remains to be a vague goal. Therefore, identification of unknown mechanisms that mediate CMP could be beneficial. Results of the last decade's work clearly provide evidence that inflammation and enhanced release of pro-inflammatory cytokines, especially tumor necrosis factor (TNF)-α might play a role in the pathogenesis of CMP. However, clinical trials have paradoxically indicated a more complicated role for TNF-α in CMP that casted doubts whether TNF-α is a viable therapeutic target for CMP. The pathology of IHD is immediately related to the development of CMP, patients currently receive medications such as beta-blockers or angiotensin converting enzyme (ACE)-blockers with the goal to ameliorate the patient's symptoms and to prevent or delay the development of (ischemic) CMP due to IHD. It is therefore common to use therapies for CMP also for IHD. Importantly, patients who develop CMP based on IHD, in particular end-stage CMP, have currently only limited therapeutic options (e.g. cardiac transplantation or the use of ventricular assist devices, which can be in turn offered only to a limited number of patients). There is still an unmet need for further drug targets and treatment regimen for efficiently preventing and treating CMP and IHD and one of its major causes, that is ischemic heart diseases (also called coronary heart diseases that can result in myocardial infarction), especially elevated blood pressure-induced CMP and volume-induced CMP. Cardiomyopathies result in recurrent exacerbation leading to hospitalization or death. Therefore, also close surveillance and thorough clinical tests are required to achieve the optimal tailored cardiomyopathy treatment in these patients, associated with tremendous health care costs. A biomarker that could identify the evolution of cardiomyopathy and help to optimize treatment monitoring and outcome is therefore highly desirable. Ideally, such a test should be sensitive, specific, none-invasive, quick and cheap. Although, a number of neurohumoral factors and inflammatory cytokines have been reported as diagnostic biomarkers in cardiomyopathy, brain-type natriuretic peptide (BNP) and its inactive N-terminal fragment (proBNP) have gained the broadest acceptance in clinical diagnosis and monitoring of patients with suspected or established chronic CMP. However, circulating BNP and proBNP levels are dramatically affected by renal function and are age- and gender-dependent. In addition, it remains unknown whether proBNP could be beneficial in diagnosis of preserved as opposed to reduced ejection fraction (EF) CMP. It is therefore also an object of the present invention to provide diagnostic means for cardiomyopathies and ischemic heart diseases. Therefore, the invention provides Glutathione S-transferase P1 (GSTP1) for the prevention or treatment of cardiomyopathies (CMPs) as well as for the prevention or treatment of ischemic heart diseases. With the present invention it could be surprisingly shown that GSTP1 is beneficial in CMP treatment and in the treatment of ischemic heart diseases (IHD). GSTP1 has been described as a relevant protein in cancer medicine (e.g. U.S. Pat. No. 5,427,917 A, U.S. Pat. No. 5,552,277 A and WO 98/21359 A1) and in allergic diseases, such as asthma, especially in connection with traffic-related air pollution (e.g. Melen et al., Env. Health Persp. 116 (2008), 1077-1084). GSTP1 has also been suggested to decrease mortality of endotoxic shock and inhibition of acute lung injury and peritonitis (Luo et al., Mol. Immunol. 46 (2009), 848-875). GSTP1 was reported to interact with TRAF2 (tumor necrosis factor receptor-associated factor 2) as a novel ligand-binding function of GSTP1 in regulating kinase signalling (Wu et al., Oncogene 25 (2006), 5787-5800). Although this provided a new insight for analysing the mechanism utilized by GSTP1 to protect cells against different injury stimuli such as cytokines, UV or H2O2, and this teaching was regarded as conceivable that GSTP1 functions as a general survival factor by forming GSTP1-TRAF2 complex in tumor cells, inhibition of this complex was regarded as being limited to antitumor therapy. According to the present invention it was surprisingly found that GSTP1 is specifically upregulated in CMP and IHD patients as compared to controls. It was further found that recombinant GSTP1 mediated GSTP1-TRAF2 association, decreased pro-inflammatory JNK1 and p38 activation and TRAF2 expression dependent on its dose and the underlying form of CMP. This enabled the provision of a new therapy strategy for CMP and IHD by administration of GSTP1. Since GSTP1 ameliorates TNF-α-mediated activation of pro-inflammatory JNK1/p38 by association to TRAF2, GSTP1 is not only beneficial in CMP and IHD treatment but also for the prevention of CMP and IHD, especially in risk patients, such as hypertensive patients. The present invention provides the use of GSTP1 for the manufacture of a medicament for the prevention or treatment of CMP and ischemic heart diseases. The treatment of CMP and IHD according to the present invention involves the administration of an effective amount of GSTP1 to an individual in need of such treatment, e.g. human CMP and IHD patients. For these reasons and based on the fact that the pathology of IHD is immediately related to the development of CMP, patients currently receive medications such as beta-blockers or angiotensin converting enzyme (ACE)-blockers with the goal to ameliorate the patient's symptoms and to prevent or delay the development of (ischemic) CMP due to IHD. The close relationship of the pathology of IHD with CMP that is based on the remodelling of myocardium in patients with IHD, specially in patients developing myocardial infarction due to IHD that in turn leads to remodelling of the cardiac chambers and subsequently to impaired pump function of the heart, a pathological condition that is common to CMP and IHD, specially in myocardial infarction patients, shows the effectiveness of the present invention for the prevention or treatment of IHD and CMP. Therefore, it is evident that the present invention is also suitable for prevention or treatment of IHD. Importantly, patients who develop CMP based on IHD, in particular end-stage CMP, have currently only limited therapeutic options (e.g. cardiac transplantation or the use of ventricular assist devices, which can be in turn offered only to a limited number of patients) and this fact constitutes a preferred use of the present invention in order to prevent or treat patients suffering from IHD, aimed to prevent the development of CMP at the one hand and to improve or stabilise the clinical condition in IHD patients on the other. With the present invention all forms and stages of CMP and IHD, acute and chronic forms thereof, can be treated, independently of the genesis of the CMP or IHD. Of course, the term “treatment” includes preferentially the amelioration of the disease and the prevention or slowing of progression of the disease. For example, CMPs can be caused by myocardial infarction, can be idiopathic dilative or be caused by hypertension. All these forms can be treated with GSTP1 according to the present invention. Specifically ischemic CMPs e.g. caused by myocardial infarction can be treated with GSTP1, however, also non-ischemic forms can be treated (e.g. idiopathic dilated CMPs or hypertension- or volume-induced CMPs). Since in all these CMPs, inflammatory pathways are involved, this makes them eligible for treatment with GSTP1 according to the present invention (even rare forms of CMP, if such inflammatory pathways are involved). Therefore, preferred CMPs according to the present invention are dilated cardiomyopathy, especially congestive cardiomyopathy; obstructive hypertrophic cardiomyopathy, especially hypertrophic subaortic stenosis; other hypertrophic cardiomyopathies, especially nonobstructive hypertrophic cardiomyopathy; endomyocardial (eosinophilic) disease, especially endomyocardial (tropical) fibrosis or Löffler's endocarditis; endocardial fibroelastosis, especially congenital cardiomyopathy; other restrictive cardiomyopathies, especially constrictive cardiomyopathy NOS (not otherwise specified (according to ICD-10)); alcoholic cardiomyopathy, cardiomyopathies due to drugs and other external agents, unspecified cardiomyopathies, especially cardiomyopathy (primary)(secondary) NOS; cardiomyopathy in infectious and parasitic diseases, especially cardiomyopathy in diphtheria; cardiomyopathy in metabolic diseases, especially cardiac amyloidosis; cardiomyopathy in nutritional diseases, especially nutritional cardiomyopathy NOS; Gouty tophi of heart or thyrotoxic heart disease. Specifically preferred forms of CMP or IHD to be treated (or prevented) according to the present invention are CMPs caused by ischemia, especially by myocardial infarction; by hypertension, or by myocarditis. GSTP1 treatment according to the present invention is therefore preferably applied in patients with acute myocarditis, preferably infective myocarditis, especially septic myocarditis; isolated myocarditis, myocarditis in a bacterial disease, especially diphtheritic, gonococcal, meningococcal, syphilitic or tuberculous myocarditis; myocarditis in a viral disease, especially influenzal myocarditis or mumps myocarditis; acute or chronic myocarditis in Chagas' disease, myocarditis in toxoplasmosis, rheumatoid myocarditis or sarcoid myocarditis. The preferred indications according to the present invention are therefore those listed under Chapter IX of the ICD-10 (I11-I15, especially I21, I22 and I23; I20-I25, especially I21 and I22; I40-I43, especially I42; I50-I57, especially I50 and I57). The main focus of the present invention is the treatment of human patients; however, based on the present findings, it is clear that also animal (mammal) CMP and IHD in which inflammation is involved can be successfully treated by GSTP1 according to the present invention. This may be important for farm or zoo animals (especially breeding farm animals, such as (former) racing horses) or pets, for example dogs, cats and horses. Although the present invention is also useable for the prevention of CMP and IHD it is clear that the primary focus of the present invention lies in the treatment of human CMP and IHD patients who have already been diagnosed of CMP or IHD or which have a high risk of developing CMP or IHD, for example patients with hypertension (e.g. Stage 2 patients with systolic pressure of 160 mm Hg or more and/or with diastolic pressure of 100 mm Hg or more). Another preferred embodiment of the preventive aspect of the present invention is for angina pectoris patients, whereby myocardial infarction might or might not have occurred in this set of patients; and heart insufficiency or heart failure (Mc Murray et al., Lancet 365 (2005), 1877-1889) may or may not be present. Here, even continuous intravenous administration or continuous administration to the heart muscle is indicated. Preferred routes of administration of the GSTP1 containing medicament according to the present invention are parenteral routes, preferably intraperitoneal or intravenous administration, intravenous administration being specifically preferred. Intravenous administration can be performed e.g. via bolus injection or by continuous intravenous delivery over a longer time period (e.g. 30 min to 6 h, especially 1 to 3 h). In the process of heart surgery also administration directly to the heart (intramyocardial injection) is preferred. With this route, GSTP1 activity can be directly and in high concentrations delivered to the area of need, e.g. to an infarct region. Another preferred route of administration is administration to the coronary sinus (e.g. via a catheter inserted into the coronary sinus). Oral or mucosal routes (although described for GSTP1 in principle; see e.g. U.S. Pat. No. 5,976,528 A) are less preferred, since GSTP1 is a protein and for this route specific protection measures (enteric coating, encapsulation, etc.) are necessary as well as a significant optimisation with respect to galenic manufacture. Preferred dosages for administration are dosages of 0.001 to 100 mg GSTP1/kg, preferably 0.01 to 10 mg GSTP1/kg, especially 0.1 to 1 mg GSTP1/kg, to a human individual, preferably via intravenous administration; or dosages of 0.1 to 10000 U GSTP1/kg, preferably 1 to 1000 U GSTP1/kg, especially 10 to 100 U GSTP1/kg, to a human individual, preferably via intravenous administration. These are preferred daily dosages for intravenous application (“kg” means kg body weight of the person to be treated). During surgery, these dosages may also be applied, either as a whole or even more than one dosage; or only part of the dosage (having in mind that the GSTP1 can directly be applied during surgery in the area needed). “Ready-to-use” daily dosage forms (e.g. for a 80 kg and/or a 60 kg human individual) can be pre-manufactured and can be made storage-stable by lyophilisation or freezing (and rbradshaw@example.net. −20° C.). The dosage can then be fully or only partially consumed (e.g. based on the body weight of the person to be treated). GSTP1 according to the present invention is also referred to as “GSTP1-1”, “GST class-pi”, “DFN7”, “GST3”, “GST π”, etc. and conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (EC 7867929920; Catalytic activity: RX+glutathione=HX+R—S-glutathione). The human sequence (Seq. ID. No. 1) is listed as “GSTP1 HUMAN, P09211” in the UniProtKB/SwissProt database (HGNC: 4638, Entrez Gene: 2950). SEQ. ID. NO. 1: 1 mppytvvyfp vrgrcaalrm lladqgqswk eevvtvetwq egslkascly gqlpkfqdgd 61 ltlyqsntil rhlgrtlgly gkdqqeaalv dmvndgvedl rckyisliyt nyeagkddyv 121 kalpgqlkpf etllsqnqgg ktfivgdqis fadynlldll lihevlapgc ldafpllsay 181 vgrlsarpkl kaflaspeyv nlpingngkq Several variants exist for this human protein (homozygous as well as heterozygous), the most important variants are a Ile to Val exchange at position 105 and a Ala to Val exchange at position 114 (Melen et al., 2008). Other variants include a Gly to Glu exchange at position 78, a Thr to Ser exchange at position 110, a Gly to Glu exchange at position 139, a Asp to Tyr exchange at position 147 and a Asp to His exchange at position 158. Several other SNPs are known without affecting the amino acid sequence. If the CMP or IHD patient to be treated with GSTP1 according to the present invention has such an allele which results in a (heterozygous or homozygous) amino acid exchange compared to SEQ.ID.No. 1, it may be recommendable to administer to such a patient the allelic form of this protein. This is specifically preferred for patients who are homozygous for this allele, e.g. patients with homozygous 105Val or 114Val allele (who could then receive the 105Val or 114Val GSTP1 variant, respectively). In such cases, the risk of developing adverse reactions, especially adverse immune reactions (which is always a topic for proteinaceous medicaments), is kept low. Anyway, any ingredients in the pharmaceutical preparation containing GSTP1 according to the present invention eliciting or boosting an immune reaction in the patient should be kept at minimum if possible. Orthologs from mammals are known, e.g. from chimpanzee (Pan troglodytes; NCBI accessions: 745954, XM—001152516.1, XP—001152516.1) and mouse (Mus musculus; NCBI accessions: 148701, NM—013541.11, NP—038569.11, AK0791445, BC0020485), but also from non-mammals, such as zebrafish (Danio rerio) and worm (Caenorhabditis elegans). The present invention also relates to a pharmaceutical composition comprising GSTP1, preferably human recombinant GSTP1 or human placenta GSTP1, and a pharmaceutically acceptable carrier for the prevention or treatment of cardiomyopathies or ischemic heart diseases. According to a preferred embodiment, the composition according to the present invention contains 1 to 100000 U GSTP1, preferably 10 to 10000 U GSTP1, especially 10 to 1000 U GSTP1. A unit of GSTP1 activity conjugates 1.0 micro-mole of 1-chloro-2,4-dinitrobenzene with reduced glutathione per minute at pH 6.5 at 25° C. A preferred composition according to the present invention also contains a buffer. Typical buffer systems are the carbonic acid/HCO3 system (pH 6.2 to 8.6; neutral), carbonic acid/silicate buffer (pH 5.0 to 62; weakly acidic), acetic acid/acetate buffer (pH 3.7 to 5.7), phosphate buffer (NaH2PO4+Na2HPO4; pH 5.4 to 7.8), ammonia buffer (NH3+H2O+NH4Cl; pH 8.2 to 10.2), TRIS/HCl (Tris(hydroxymethyl)-aminomethane; pH 7.2 to 9.0), HEPES (4-(2-Hydroxyethyl)-1-piperazinethanesulfonic acid; pH 6.8 to 8.2), HEPPS (4-(2-Hydroxyethyl)-piperazine-1-propane sulfonic acid; pH 7.3 to 8.7) or MES (2-(N-Morpholino)ethanesulfonic acid; pH 5.2 to 6.7). Preferred buffers according to the present invention is a phosphate buffer, a Tris-HCl buffer or a HEPES buffer, with a pH of 5.5 to 9.0, preferably of 6.0 to 8.5, especially of 6.5 to 8.0. Buffer concentrations can preferably be adjusted to 1 mM to 1 M, especially 10 mM to 0.5 M. Other preferred additional ingredients include stabilisers, chelators, salts, etc., such as glycerol, glucose, saccharose, maltose, EDTA or similar substances, NaCl, KCl, NH4Cl and similar salts usable in pharmaceutical preparations. Of course, all ingredients in a pharmaceutical preparation have to be of pharmaceutical grade quality. Pharmaceutically acceptable carriers preferably used are physiological saline, vegetable oils, mineral oil, aqueous sodium caroboxymethyl cellulose or aqueous polyvinylpyrrolidone; however, also sterile water can be used. GSTP1 to be used according to the present invention can be provided by various ways. As mentioned above, GSTP1 from human placenta is one of the preferred natural sources of GSTP1. Other preferred sources are cultures of GSTP1 (over-)expressing cells. GSTP1 preparations are also commercially available. The preferred industrial production route according to the present invention is, however, recombinant production of GSTP1. Recombinant production of GSTP1 is well established, as well as its purification from such sources (e.g. Luo et al., 2009, Wu et al., 2006; WO 98/21359 A1; U.S. Pat. No. 5,976,528; etc.). Expression vectors (e.g. WO 98/21359 A1, Part D (pages 40 to 51) containing the GSTP1 coding sequences are transferred in suitable host cells (such as COS, HEK 293, HeLa, VERO, W138, BHK or MDCK cells, but also yeast, plant, insect and bacterial cells (S. cerevisiae, E. coli, etc.). GSTP1 is then expressed and purified according to standard methods. Recombinant GSTP1 production may also use variant forms of GSTP1 with additional sequences which facilitate purification, such as metal chelating peptides, protein A domains, affinity purification tags, etc. (e.g. U.S. Pat. No. 5,976,528 A, column 16). Such variants can—after purification or in the course of purification—be removed e.g. via cleavable linker sequences (protease, entereokinase, etc.). Purified batch preparations of GSTP1 may contain e.g. 1 to 200 U GSTP1 activity per mg total protein. Preferred pharmaceutical GSTP1 compositions contain 5 to 200 U/mg protein, especially 10 to 150 U/mg protein. The pharmaceutical preparation according to the present invention is always provided as an appropriately labelled product which is sterile and useable for administration to human patients according to the present invention. According to another aspect, the present invention relates to GSTP1 as a diagnostic target for CMP or IHD. The present invention provides the use of GSTP1 for the diagnosis of CMP or IHD. Although GSTP1 is a known and established marker in tumor diagnosis, it was surprising that GSTP1 is a biomarker for CMP or IHD which is even superior to the current “gold standard”, pro-BNP, with respect to sensitivity and specificity. The cardiomyopathies or ischemic heart diseases referred to above for therapeutical use of GSTP1 can also be diagnosed according to the present invention. The present invention therefore relates to a method for diagnosing CMP or IHD, especially the indications mentioned above, by determining the amount of GSTP1 or GSTP1 mRNA in a biological sample and comparing this amount to the GSTP1 or GSTP1 mRNA amount in a biological sample with a defined and known CMP/IHD status, especially from a healthy human individual or a patient. This comparison can be done practically, i.e. in that a real sample is tested in the same manner as the biological sample (side-by-side), it can also be a virtual comparison so that the determined value is compared with a known value of a healthy or diseased sample. Preferred techniques for determining the amount of GSTP1 include antibody-liked techniques, such as ELISA, optionally combined with electrophoresis techniques or radio immunoassay (RIA). Electrophoresis techniques may also be combined with MALDI techniques. Alternatively, GSTP1 mRNA may be determined, e.g. by quantitative real time RT-PCR. The preferred diagnosis target is a human patient who is suspected to have CMP or IHD, a human patient who is at risk for developing CMP or IHD or a human patient who has CMP or IHD (who has to be monitored for progression of the disease). Preferred biological samples according to the present invention include human blood, plasma or serum samples or human myocardial biopsy samples. These samples can also be tested by routine methods. Typically, a high concentration of GSTP1 in serum is indicative of CMP or IHD. In healthy persons, serum concentrations of GSTP1 are below 50 ng/ml or, preferably, even below 10 ng/ml. A CMP or IHD diseased status can be diagnosed at a serum level at 50 ng/ml or above, preferably at 100 ng/ml or above. Severe forms of CMP or IHD can be diagnosed at 200 ng/ml or above. Of course, these levels always depend on the technique used for as-saying the GSTP1 protein. Alternatively, CMP or IHD diseased status can be diagnosed if the serum level of GSTP1 is elevated by at least the factor 2, preferably by at least the factor 5, compared to a healthy status, especially the healthy status of the same patient. Severe forms could be diagnosed, if the serum GSTP1 level is elevated by at least the factor 10, especially by at least the factor 20, compared to a healthy status, especially the healthy status of the same patient. With the present invention determining the amount of GSTP1 or GSTP1 mRNA in a sample can be performed within a very short time by standard test methods, such as ELISA or PCR. Based on the DNA and amino acid sequence according to SEQ.ID.NO.2 atgccgccct acaccgtggt ctatttccca gttcgaggcc gctgcgcggc cctgcgcatg 60 ctgctggcag atcagggcca gagctggaag gaggaggtgg tgaccgtgga gacgtggcag 120 gagggctcac tcaaagcctc ctgcctatac gggcagctcc ccaagttcca ggacggagac 180 ctcaccctgt accagtccaa taccatcctg cgtcacctgg gccgcaccct tgggctctat 240 gggaaggacc agcaggaggc agccctggtg gacatggtga atgacggcgt ggaggacctc 300 cgctgcaaat acgtctccct catctacacc aactatgagg cgggcaagga tgactatgtg 360 aaggcactgc ccgggcaact gaagcctttt gagaccctgc tgtcccagaa ccagggaggc 420 aagaccttca ttgtgggaga ccagatctcc ttcgctgact acaacctgct ggacttgctg 480 ctgatccatg aggtcctagc ccctggctgc ctggatgcgt tccccctgct ctcagcatat 540 gtggggcgcc tcagcgcccg gcccaagctc aaggccttcc tggcctcccc tgagtacgtg 600 aacctcccca tcaatggcaa cgggaaacag tga 633 and SEQ.ID.NO.1 (and the data base entries mentioned above for the GSTP1 gene and the GSTP1 protein), the present invention also provides e.g. a PCR assay for identification of S. aureus infections or a sandwich ELISA assay. In a suitable ELISA according to the present invention, GSTP1 can be caught out of a biological sample with a GSTP1-specific antibody and detected and quantified with a second antibody directed against a different epitope of GSTP1 or an antibody being specific for the previous binding event. Detection of GSTP1 transcripts (m-RNA) is possible by standard quantitative nucleic acid tests, such as quantitative RT-PCR. The present invention therefore also provides a kit for determining the amount of GSTP1 mRNA in a least two synthetic nucleic acid sequences for amplifying at least one nucleic acid sequence encoding GSTP1 or parts thereof, wherein at least of one of the synthetic nucleic acid sequences in the kit is selected from the group consisting of: (a) a suitable primer pair, the primers being a nucleic acid sequence comprising 10-30 consecutive nucleotides of at least one of the following: (i) the GSTP1 mRNA according to SEQ.ID.NO.2 or the complementary sequence thereof; or (ii) from the 5′ or 3′ noncoding region of the GSTP1 gene (e.g. in regions extending up to 500, preferably up to 200, especially up to 100, nucleotides into the 5′- or 3-direction or complementary sequences thereof; such sequences are present in the sequence library entries mentioned above); said primers being usable for polymerising a nucleotide sequence located between the primers on the GSTP1 gene or its 5′- or 3′-region (said polymerizable GSTP1 nucleotide sequence being PCR detectable and preferably up to 1000 bp, more preferred up to 500 bp, even more preferred up to 300 bp in length; on the other hand, the primers may also be selected to polymerise (with PCR) the whole GSTP1 m-RNA); and (b) suitable reagents for a polymerase chain reaction (PCR). Preferably, the kit further comprises: (c) instructions for use and (d) optionally, a positive and/or negative control for determining and/or quantification of GSTP1 mRNA, especially a control nucleic acid encoding GSTP1 or a fragment thereof. Examples of suitable PCR reagents include PCR reaction buffer, Mg2+ (e.g., MgCl2), dNTPs, DNA polymerases (such as reverse transcriptases and thermostable DNA polymerases (e.g., Taq-related DNA polymerases and Pfu-related DNA polymerases)), RNase, PCR reaction enhancers or inhibitors, PCR reaction monitoring agents (e.g., double-stranded DNA dye (such as SYBR™ Green), TaqMan™ probes, molecular beacons, and Scorpions™), and PCR-grade water. The primers described herein are particularly useful in a polymerase chain reaction (PCR) assay. PCR is a practical system for in vitro amplification of a DNA base sequence. For example, a PCR assay may use a heat-stable polymerase and two about 10 to 30 base primers: one complementary to the (+)-strand at one end of the sequence to be amplified, and the other complementary to the (−)-strand at the other end. Because the newly-synthesized biological sample, comprising: (a) a primer set comprising at DNA strands can subsequently serve as additional templates for the same primer sequences, successive rounds of primer annealing, strand elongation, and dissociation may produce rapid and highly-specific amplification of the desired sequence. PCR also may be used to detect the existence of a defined sequence in a GSTP1 m-RNA containing sample. By way of example, a typical PCR assay according to the present invention might start—optionally after reverse transcription of the mRNA into DNA—with two synthetic oligonucleotide primers which are specifically and complementarily binding to two regions of the target DNA or its complementary strand, respectively, encoding GSTP1 or its 5′- and/or 3′ region (one for each strand) that is to be amplified. These may be added to the target DNA (that needs not be pure) in the presence of excess deoxynucleotides (dNTPs) and a thermostable DNA polymerase (e.g., Taq polymerase). In a series (typically 20-40) of temperature cycles, the target DNA may be repeatedly denatured (about 80-100° C., e.g. 90° C.), annealed to the primers (typically at 40-65° C.), and a daughter strand may be extended from the primers (typically at 65-80° C., e.g. 72° C.). As the daughter strands themselves act as templates for subsequent cycles, DNA fragments matching both primers are amplified exponentially, rather than linearly. The target DNA needs be neither pure nor abundant; thus, PCR is specifically suitable in the clinical diagnostics according to the present invention. These tests may preferably employ labels which are also suitable for quantification, such as biotin, fluorescent molecules, radioactive molecules, chromogenic substrates, chemiluminescence markers, and the like. The methods for biotinylating nucleic acids are well known in the art, as are methods for introducing fluorescent molecules and radioactive molecules into oligonucleotides and nucleotides. Detection methods are well known for fluorescent, radioactive, chemiluminescent, chromogenic labels, as well as other commonly used labels. Briefly, chemiluminescence can be identified and quantitated most directly by their emission wavelengths and intensity. When biotin is employed, it is detected by avidin, streptavidin or the like, which is conjugated to a detectable marker, such as an enzyme (e.g. horseradish peroxidase). Steptavidin binds with high affinity to biotin, unbound streptavidin is washed away, and the presence of horseradish peroxidase enzyme is then detected using a luminescence-emission substrate in the presence of peroxide and appropriate buffers. Determining the amount of GSTP1 in a sample preferably includes ELISA, RIA and FACS. Detection and quantification of GSTP1 by using anti GSTP1 antibodies is well established in the art (especially in tumor medicine) and can be readily applied for the purpose of diagnosing CMP or IHD according to the present invention (e.g. WO 98/21359 A1 (“F. Antibodies”); U.S. Pat. No. 5,976,528 A, U.S. Pat. No. 5,427,917 A). Normal or standard values for GSTP1 expression are established by combining body fluids or cell extracts taken from normal mammalian subjects, preferably human, with antibody to GSTP1 under conditions suitable for complex formation. The amount of standard complex formation may be quantified by various methods, preferably by photometric means. Quantities of GSTP1 expressed in subject, samples, control and disease, from biopsied tissues are compared with the standard values. Deviation between standard and subject values establishes the parameters for diagnosing disease. As already stated above, most preferred samples are of human heart biopsies and samples derived from human blood of individual human patients having CMP or IHD, being suspected of having CMP or IHD or being at risk of developing CMP or IHD. The present invention is further illustrated by the following examples and the drawing figures, yet without being restricted thereto. FIG. 1 shows increased GSTP1 and TRAF2 in DCM and ICM patients. (A) Representative gene array images show increased hybridization to GSTP1 and TRAF2 array sequences (arrows) of labelled cDNA probes. (B) Representative protein array images demonstrating enhanced Cy5 (red) staining for cardiac GSTP1 and TRAF2 proteins in DCM and ICM patients compared to the Cy3 (green) staining of controls. (C) Quantification of myocardial GSTP1 and TRAF2 mRNA expressions by real time RT-PCR. GSTP1 (*P<0.0001) and TRAF2 (P<0.0001) mRNA expression is significantly up-regulated in heart failure patients compared to controls. (D) Representative Western blot images and quantification of myocardial GSTP1 and TRAF2 protein expressions corrected for protein loading control levels. Myocardial protein expression levels were elevated in DCM and ICM for GSTP1 (P<0.0001, P=0.0019) and TRAF2 (P<0.0001, P=0.005) as compared to controls. No significant differences were found in GSTP1 mRNA and protein expression when DCM and ICM were compared; although TRAF2 mRNA (†P=0.001) and protein (†P≦0.0001) expression levels were significantly higher in DCM as compared to ICM. *, significantly different versus controls. FIG. 2 shows GSTP1-TRAF2 interaction and activation of JNK and p38 in DCM and ICM. (A) Representative Western blot images and quantification of myocardial GSTP1-TRAF2 complex formation in DCM, ICM and controls. LV myocardial lysates were immunoprecipitated (IP) and precipitates were analyzed on Western blotts. Significantly lower GSTP1-TRAF2 association was found in DCM compared to ICM and controls (*P≦0.008). (B) Representative Western blot images and quantification of myocardial active JNK1 and p38 protein expression in DCM, ICM and controls. In both DCM and ICM cardiac protein expression of active JNK as well as p38 (P<0.0001) is significantly upregulated as compared to controls. Moreover, DCM patients reveal a significantly higher cardiac JNK and p38 protein expression (†P<0.0001) as compared to ICM. All protein expressions were corrected for protein loading control levels. *, significantly different versus control. FIG. 3 shows that GSTP1 modulates cardiac TRAF2-JNK1/p38 system in cardiac tissue cultures. (A) Representative Western blot images of TRAF2, GSTP1, active JNK and active p38 protein expressions in cardiac tissue cultures treated with 5 μg/mL recombinant GSTP1. (B) Quantification of TRAF2, active JNKs and active p38 protein expressions in DCM, ICM and control cardiac tissue cultures treated with recombinant GSTP1 (2.5, 5, 10 μg/ml) for 24 h. Protein expressions of TRAF2 was significantly reduced compared to untreated ones dependent on the concentration used (DCM: P=0.011 for 2.5 μg/mL, P=0.014 for 5 μg/mL, P=0.003 for 10 μg/mL; ICM: P=0.006 for 2.5 μg/mL, P=0.003 for 5 μg/mL, P=0.0001 for 10 μg/mL; controls: P=0.19 for 2.5 μg/mL, P=0.0003 for 5 μg/mL, P=0.03 for 10 μg/mL). Following GSTP1 treatment, active JNK expression declined in DCM, ICM and control cardiac tissue compared to untreated group dependent on the concentration used (DCM: P=0.0009 for 2.5 μg/mL, P=0.01 for 5 μg/mL, P=0.0003 for 10 μg/mL; ICM: P=0.0005 for 2.5 μg/mL, P=0.007 for 5 μg/mL, P<0.0001 for 10 μg/mL; controls: P=0.001 for 2.5 μg/mL, P=0.69 for 5 μg/mL, P=0.71 for 10 μg/mL). Likewise, active p38 expression decreased in response to GSTP1 treatment in DCM, ICM and control cardiac tissue compared to untreated ones dependent on the concentration used (DCM: P=0.004 for 2.5 μg/mL, P<0.0001 for 5 μg/mL, P=0.0009 for 10 μg/mL; ICM: P=0.03 for 2.5 μg/mL, P=0.0001 for 5 μg/mL, P=0.008 for 10 μg/mL; controls: P=0.008 for 2.5 μg/mL, P=0.0004 for 5 μg/mL and μg/mL). The comparison of the applied GSTP1 concentrations with regard to TRAF2, JNK and p38 reduction indicated that in DCM and ICM but not controls the differences between 2.5 μg/mL and 5 μg/mL as well as 10 μg/mL were significant. TRAF2: (DCM: P=0.01 for 2.5 vs. 5 μg/mL and vs. 10 μg/mL, P=0.62 for 5 vs. 10 μg/mL; ICM: P=0.0007 for 2.5 vs. 5 μg/mL, P=0.0004 for 2.5 vs. 10 μg/mL, P=0.35 for 5 vs. 10 μg/mL; control: P=0.07 for 2.5 vs. 5 μg/mL, P=0.06 for 2.5 vs. 10 μg/mL, P=0.15 for 5 vs. 10 μg/mL). JNK: (DCM: P=0.0006 for 2.5 vs. 5 μg/mL, P=0.003 for 2.5 vs. 10 μg/mL, P=0.48 for 5 vs. 10 μg/mL; ICM: P=0.004 for 2.5 vs. 5 μg/mL, P=0.01 for 2.5 vs. 10 μg/mL, P=0.88 for 5 vs. 10 μg/mL; control: P=0.02 for 2.5 vs. 5 μg/mL, P=0.05 for 2.5 vs. 10 μg/mL, P=0.97 for 5 vs. 10 μg/mL). p38 (DCM: P=0.0002 for 2.5 vs. 5 μg/mL, P=0.04 for 2.5 vs. 10 μg/mL, P=0.76 for 5 vs. 10 μg/mL; ICM: P=0.0006 for 2.5 vs. 5 μg/mL, P=0.02 for 2.5 vs. 10 μg/mL, P=0.41 for 5 vs. 10 μg/mL; control: P=0.06 for 2.5 vs. 5 μg/mL, P=0.08 for 2.5 vs. 10 μg/mL, P=0.29 for 5 vs. 10 μg/mL). (C) Representative Western blot images of myocardial GSTP1-TRAF2 complexes from DCM, ICM and controls cardiac tissue cultures treated with recombinant GSTP1 (5 μg/ml) and subjected to immunoprecipitation (IP). GSTP1-treated cardiac tissue cultures association between GSTP1 and TRAF2 was dose and disease-independent and significantly higher (P=0.02 for 5 μg/mL GSTP1 concentration; results for 2.5 and 10 μg/mL GSTP1 concentration not shown) as compared to untreated samples. *, significantly different versus control. †, significantly different versus GSTP1 2.5 μg/ml treated tissue cultures. ‡, significantly different versus GSTP1 5 μg/ml and 10 μg/ml treated tissue FIG. 4 shows that TNF-α abrogates sensitivity of TRAF2-JNK1/p38 cascade to GSTP1 in DCM cardiac cultures. (A) Representative Western blot images and quantification (B) of DCM, ICM and control cardiac tissue cultures treated with TNF-α (50 ng/ml) and GSTP1 (5 μg/ml). TNF-α-activated JNK (P=0.08) and p38 (P=0.75) cascade as well as TRAF2 (P=0.18) protein expression were not affected by recombinant GSTP1 in DCM cardiac tissue cultures. In ICM and controls active JNK (P<0.001; P<0.002), active p38 (P<0.0002; P<0.0001) and TRAF2 (P<0.001; P=0.003) protein expressions was markedly reduced in response to GSTP1 stimulation. The comparison of the GSTP-treated ICM and DCM cardiac tissue cultures indicate significantly lower TRAF2, actives JNK and p38 (†P<0.001) protein expressions in ICM as compared to those of DCM. (C) Representative Western blot images of immunoprecipitated cardiac tissue lysates treated with TNF-α (50 ng/ml) and GSTP1 (5 μg/ml). The failure of GSTP1 to associate with TRAF2 following TNF-α stimulation in DCM cardiac tissue was present in contrast to ICM and control cardiac tissue. FIG. 5 shows that higher GSTP1 concentrations rescue TRAF2-mediated JNK1/p38 downregulation following TNF-α treatment. (A) Representative Western blot images and quantifications (B) of DCM, ICM and control cardiac tissue cultures treated with TNF-α (50 ng/ml) and GSTP1 (10 μg/ml). (B) The results demonstrate that DCM cardiac tissue cultures treated with GSTP1 at 10 μg/mL and TNF-α express markedly reduced JNK and p38 activation as well as reduced TRAF2 protein expression (*P<0.0001) as compared to TNF-α-treated controls. (C) The immunoprecipitates of DCM cardiac tissue lysates demonstrate significant (P≦0.035) increase of GSTP1-TRAF2 association at 10 μg/ml GSTP1 as compared to 5 mg/ml GSTP1. FIG. 6 shows that serum and cardiac GSTP1 is associated with CMP. (A) Representative serum protein array images demonstrate enhanced Cy3 (green) and Cy5 (red) staining for serum GSTP1 protein in end-stage heart failure (HF) (EF≦35%; n=40) patients compared to controls (EF≧65%; n=40). (B) ELISA measurements indicate significant (*P<0.0001) elevation of serum GSTP1 concentration in end-stage HF patients with (EF≦35%; n=40) versus controls with (EF≧65%; n=40). (C) Representative cardiac tissue protein array images demonstrate enhanced Cy3 (green) and Cy5 (red) staining for cardiac GSTP1 protein in end-stage HF patients (EF≦35%; n=40) compared to controls (EF≧65%; n=20). (D) Representative Western blotting images and quantification of myocardial GSTP1 protein expression corrected for protein loading control levels. GSTP1 protein levels were significantly elevated in end-stage HF patients with EF≦35% versus control cardiac graft tissue (*P≦0.001). FIG. 7 shows serum GSTP1 and proBNP association with ejection fraction (EF) and the correlation between GSTP1 and proBNP. (A) Heart failure patients with EF≦22% have significantly higher serum GSTP1 concentrations as compared to all other EF groups. Patients with EF33-42%, EF23-32% and EF≦22% have significantly higher serum GSTP1 concentration as compared to those with EF>52% and EF 43-52%. (B) Patients with EF≦22% have significantly higher serum proBNP concentration as compared to all other EF groups. No significant differences in serum proBNP were observed between all other EF groups. (C) Correlation plot of serum GSTP1 and serum proBNP measurements for all study subjects. Significant positive relationship was noted between serum GSTP1 and proBNP (r=0.47; P<0.0001). *P<0.001 versus control, †P<0.0001 versus EF>52%, ‡P<0.0001 versus EF 43-52%, §P<0.0001 versus EF 33-42%, ∥P<0.0001 versus EF 23-32%. FIG. 8 shows serum GSTP1 and proBNP correlation to cardiac function. (A) Correlation of serum GSTP1 and proBNP concentrations to cardiac ejection fraction (EF) in study subjects. The analysis indicates a higher significant negative correlation of EF with serum GSTP1 (r=−0.74; P<0.0001) as compared to serum proBNP concentration (r=−0.27; P=0.0006). (B) ROC curve analysis indicates at the optimal cut-off level of ≧226 ng/ml (black line; AUC=0.891, P<0.0001) a sensitivity of 81% and a specificity of 82% for serum GSTP1 and at the optimal cut-off level of ≧527 pg/ml (red line; AUC=0.624, P=0.0039) a sensitivity of 97% and a specificity of 26% for serum proBNP to identify EF≦22%. (C) ROC curve analysis indicates at the optimal cut-off level of ≧76 ng/ml (AUC=0.974, P=0.0008) a sensitivity of 93% and a specificity of 100% for serum GSTP1 to identify EF≦42%. FIG. 9 shows that GSTP1 inhibits the inflammatory cytokines in a rat acute MI model. (A) Immunoprecipitation with Western blotting revealed no differences in GSTP1-TRAF2 complex formation between GSTP1-treated and control animals; (B) GSTP1 decreased activated JNK1 protein expression levels as analyzed by Western blotting; (C) GSTP1 inhibits the myocardial tissue mRNA expression of several inflammatory cytokines. *; p<0.01. FIG. 10 shows that GSTP1 ameliorates inflammation in the rat failing heart. (A) GSTP1-treated animals had significantly higher levels of complex formation between GSTP1-TRAF2, GSTP1-JNK1 and GSTP1-p38, as shown by immunoprecipitation and Western blot analyses; (B) the protein expression of activated JNK1, p38 and NF-κB is significantly lower in GSTP1-treated animals as compared to controls as shown by Western blot analyses; (C) GSTP1 inhibits the mRNA expression of inflammatory cytokines TGF-B, IL-1B, IL-2 and IL-17; and increases the mRNA expression of anti-inflammatory cytokine IL-10 in failing myocardium as compared to controls. *; p<0.001. FIG. 11 shows that GSTP1 attenuates myocardial remodeling in a rat ischemia-induced model of heart failure. (A) Goldner trichrome collagen staining reveals significantly lower tissue remodeling in the heart of GSTP1-treated animals as compared to controls; (B) left ventricular (infarct) wall thickness is significantly larger in GSTP1-treated rats compared to controls; (C) representative Tunnel assay images of rat hearts treated with GSTP1 or a control vehicle. Bar=25 μm; (D) GSTP1-treated rats had a significantly lower apoptotic index as compared to controls. *; p<0.01. FIG. 12 shows that GSTP1 improves the left ventricular function in a rat model of ischemia-induced heart failure. (A) GSTP1-treated rats had significantly higher left ventricular ejection fraction at 21 days post-myocardial infarct; (B) the left ventricular end diastolic volume is significantly greater in controls as compared to GSTP1-treated animals. *; p<0.05. EXAMPLES 1.: GSTP1 Ameliorates Inflammation in Cardiomyopathy (CMP) and Ischemic Heart Disease (IHD) Patients and Tissue Sampling This study was approved by the Ethics Committee of the Medical University of Vienna. Cardiac tissue samples of 70 CMP patients who gave informed consent to be enrolled (idiopathic dilated cardiomyopathy (DCM), n=35; ischemic cardiomyopathy (ICM), n=35) were used for the initial array analyses. Then, a total of 100 CMP patients (DCM, n=50; ICM, n=50) were included between January 2004 and July 2008. Table 1 summarizes the demographic, most important clinical and hemodynamic characteristics and the treatment of patients. All patients had optimized heart failure treatment and were scheduled for cardiac transplantation according to the American Heart Association criteria. All patients underwent echocardiography, coronary artery angiography, right-heart catheterization and magnetic resonance imaging for evaluation of ventricular function, myocardial viability and standard hemodynamic parameters by independent cardiologists. The case history, clinical test results, and treatment were documented and coded and blinded to the investigators of cardiac biopsies. The control group consisted of 20 heart donors with no history of cardiac disease whose hearts could not be trans-planted due to quality reasons. TABLE 1 demographic data, hemodynamic parameters and medication of study patients. ICM DCM P Male, % 50 48 0.4300 Age (years) 58 ± 6 55 ± 7 0.1521 BMI (kg/m2) 26 ± 3 25 ± 4 0.6688 BSA (m2) 1.9 ± 0.2 1.9 ± 0.2 0.5883 PAP (mmHg) 30 ± 10 32 ± 8 0.2817 PCWP (mmHg) 21 ± 9 22 ± 7 0.5264 PVR (wood units) 2.5 ± 1.2 2.6 ± 1.7 0.8185 LVEF (%) 19 ± 6 18 ± 6 0.3755 Cardiac output (L/min) 4.0 ± 0.8 4.4 ± 1.5 0.1647 Cardiac index (L/min/m2) 2.1 ± 0.4 2.3 ± 0.8 0.1952 ACE inhibitors (yes/no) 23/4 24/11 0.1299 Angiotensin II receptor antagonists, % 21 31 0.2494 Beta blocker, % 96 83 0.0973 Prostaglandin E2, % 22 20 0.8312 Amiodarone, % 26 29 0.8169 Levosimendan, % 19 20 0.6959 ACE, angiotensin converting enzyme; BMI, body mass index; BSA, body surface area; DCM, dilated cardiomyopathy; ICM, ischemic cardiomyopathy; LVEF, left ventricular ejection fraction; PAP, pulmonary artery pressure; PCWP, pulmonary capillary wedge pressure; PVR, pulmonary vascular resistance. cDNA array Poly(A+)-RNA was isolated with the Oligotex-dT kit (Quiagen, Valencia Calif.) and first-strand cDNA synthesis was performed with avian myeloblastosis virus reverse transcriptase (Promega, Madison, Wis.) on 2 μg poly(A+) RNA. The RNA strand within the DNA-RNA duplex was degraded and products were purified on a Sephadex G-50 spun-column (Pharmacia, Uppsala, Sweden). For reverse-strand priming, first-strand cDNA was used to generate [α-32P]dCTP-labeled second-strand cDNA for the cDNA arrays (GEArray Q Human Apoptosis Gene Array, SuperArray Bioscience, Frederick, Md.) as described (Schäfer et al., Circulation 108 (2003), 1585-1591). Pooled cDNA hybridization signals were quantified using ImageQuant software (Molecular Dynamics, Sunnyvale, Calif.). Cardiac Tissue Protein Array The protein array was performed on antibody Microarray 500 (Clontech, Mountain View, Calif.; 507 proteins) as described (Aharinejad et al., Circulation 120 (2009a), 11 Suppl:S198-205). The proteins in each sample were labeled with 2 different fluorescent dyes and incubated on microarray antibody-coated slides. The protein fluorescent signals of both slides were detected by the GenePix 4000B scanner (Molecular Dynamics, Sunnyvale, Calif.). The quantification of the signal was performed by calculating an internally normalized ratio (INR), yielding the abundance of an antigen in CMP sample relative to that in control samples by using the automated Microarray Analysis Workbook (http://bioinfo.clontech.com). Proteins with INR values outside the threshold interval were considered differentially expressed. mrNA Isolation and Quantitative Real-Time RT-PCR Total RNA was isolated from myocardial biopsies using TRIzol (Invitrogen, Carlsbad, Calif.). The tissue was homogenized in a MagNA Lyser system (Roche, Mannheim, Germany) using MagNA Lyser Green Beads for 20-30 seconds at 6000 rpm. Homogenized samples were then mixed with 200 μL chloroform, incubated 2-3 minutes at room temperature and centrifuged at 12000 g for 15 minutes at 4° C. RNA was collected and cDNA was synthesized using 2 μg total RNA and the M-MuLV-RT kit (Fermentas, St. Leon-Rot, Germany). Real-time RT-PCR was performed on a LightCycler instrument (Roche) as described (Aharinejad et al., Am J. Transplant. 5 (2005), 2185-2192). The primer sequences were sense/antisense: GSTP1: 5′-GGCAACTGAAGCCTTTTGAG-3′/5′-TCATGGATCAGCAGCAAGTC-3′; TRAF2: 5′-GCAGAAGGTCTTGGAGATGG-3′/5′-GGTGGAGCAGCATTAAGGTC-3′; and P2-microglobulin: 5′-GATGAGTATGCCTGCCGTGTG-3′/5′-CAATCCAAATGCGGCATCT-3′. mRNA expression units were determined after normalization to expression of the housekeeping gene β2-microglobulin as described previously (Aharinejad et al., 2009a and 2005; Pfaffl, Nucleic Acids Res. 29 (2001):e45) and plotted for CMP patients as percentage relative to those in controls. Measurements were performed three times. The average value of the three PCR measurements in each sample was used for data analysis. Co-Immunoprecipitation and Western Blotting Human cardiac tissue was lysed in the lysis buffer containing 20 mM Tris (pH 7.5), 135 mM NaCl, 2 mM ethylenediaminetetraacetic acid (EDTA), 2 mM dithiothreitol (DTT), 25 mM β-glycerophosphate, 2 mM sodium pyrophosphate, 10% glycerol, 1% Triton X-100, 1 mM sodium orthovanadate, 10 mM NaF and 1 mM phenylmethylsulfonyl fluoride (PMSF) supplemented with complete protease inhibitor cocktail (Roche Applied Science, Indianapolis, Ind., USA) at 4 C as described (Aharinejad et al., 2005). Lysates were centrifuged (15 000 g) at 4 C for 15 min. For identify GSTP1-TRAF2 complexes formation proteins (500 μg) were immunoprecipitated with TRAF2 antibody (0.5 μg, BD Pharmingen, San Diego, Calif.). The precleared Protein A/G PLUS-agarose beads (Santa Cruz Biotechnology) were incubated with immunocomplexes for another 2 h and washed four times with the lysis buffer. The immunoprecipitates were further subjected on SDS-PAGE and presided with Western blotting analysis using anti-GSTP1 monoclonal anti-body (Bethyl, Montgomery, Tex.). Protein lysates (50 μg/lane) were separated by SDS-PAGE (10%) prior to electrophoretic transfer onto a Nitrocellulose membrane (Bio-Rad, Hercules, Calif.) as described (Aharinejad et al., 2005). The blots were incubated with primary human monoclonal anti-GSTP1 antibody (Bethyl, Montgomery, Tex.), human monoclonal anti-TRAF2 (BD Pharmingen, San Diego, Calif.), human polyclonal phospho-p38 (Promega, Madison, Wis.), human polyclonal phosphor-JNK (Santa Cruz Biotechnology, Santa Cruz, Calif.), human polyclonal anti-JNK (Santa Cruz Biotechnology, Santa Cruz, Calif.), human polyclonal anti-p38 (Santa Cruz Biotechnology, Santa Cruz, Calif.), prior to incubation with horseradish peroxidase-conjugated secondary antibodies (Amersham Biosciences, Piscataway, N.J.). Protein loading was assessed by Ponceau S staining and immunodetection was performed by chemiluminescence (Supersignal-West-Pico, Pierce, Rockford, Bands were quantified by ImageQuant software and specific protein signals were normalized to loading controls and expressed as arbitrary units. The average value of three measurements in each sample was used for data analysis. Cardiac Tissue Culture Experiments Freshly isolated myocardium of control, DCM or ICM patients (2 to 3 mm3) were incubate (100 pieces per 6-well plate) in DMEM containing 10% fetal calf serum (Gibco, Carlsbad, Calif.), 50 U/ml penicillin and 250 μg/ml streptomycin (pH 7.2) at 37° C. in a fully humidified air atmosphere containing 5% CO2 as described (Schafer et al., 2003). After 6 hours, wells were treated with recombinant GSTP1 (2.5, 5 or 10 μg/ml; Assay Design, Ann Arbor, Mich.) and/or TNF-α (50 ng/ml; eBioscience, San Diego, Calif.) (Wu et al., 2006). Following incubation for 24 hours the medium was changed and cardiac tissue culture lysates were analysed. Experiments were performed in triplicate. Statistical Analysis Clinical parameters, patients characteristics, mRNA expression levels of GSTP1 and TRAF2, and protein expression levels of GSTP1, TRAF2, active p38, and active JNK were compared between groups by x2 test and one-way analysis of variance (one-way ANOVA; Tukey's test) according to the scale of the variable (continuous or categorical). All statistical analyses were performed using SAS system for Windows, version 9.1.3 and the Enterprise Guide, version 4.1 (SAS Institute, Inc., Cary, N.C.). Statistical significance was set at P<0.05. Results are expressed as mean±standard deviation (SD). Results GSTP1 and TRAF2 are Overexpressed in Failing Myocardium The screening tissue profiling arrays identified higher cardiac GSTP1 and TRAF2 gene as well as protein expression levels in randomly selected patients with both DCM and ICM compared to the control individuals (FIGS. 1A, 1B). To verify the results obtained in screening arrays, the myocardial expression of GSTP1 and TRAF2 was then prospectively
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