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PubMed1996

Measurement of regional cerebral blood flow with copper-62-PTSM and a three-compartment model.

UNLABELLED: We evaluated quantitatively 62Cu-labeled pyruvaldehyde bis(N4-methylthiosemicarbazone) copper II (62Cu-PTSM) as a brain perfusion tracer for positron emission tomography (PET). For quantitative measurement, the octanol extraction method is needed to correct for arterial radioactivity in estimating the lipophilic input function, but the procedure is not practical for clinical studies. To measure regional cerebral blood flow (rCBF) by 62Cu-PTSM with simple arterial blood sampling, a standard curve of the octanol extraction ratio and a three-compartment model were applied. METHODS: We performed both 15O-labeled water PET and 62 Cu-PTSM PET with dynamic data acquisition and arterial sampling in six subjects. Data obtained in 10 subjects studied previously were used for the standard octanol extraction curve. Arterial activity was measured and corrected to obtain the true input function using the standard curve. RESULTS: Graphical analysis (Gjedde-Patlak plot) with the data for each subject fitted by a straight regression line suggested that 62Cu-PTSM can be analyzed by the three-compartment model with negligible K4. Using this model, K1-K3 were estimated from curve fitting of the cerebral time-activity curve and the corrected input function. The fractional uptake of 62Cu-PTSM was corrected to rCBF with the individual extraction at steady state calculated from K1-K3. The influx rates (Ki) obtained from three-compartment model and graphical analyses were compared for the validation of the model. A comparison of rCBF values obtained from 62Cu-PTSM and 150-water studies demonstrated excellent correlation. CONCLUSION: The results suggest the potential feasibility of quantitation of cerebral perfusion with 62Cu-PTSM accompanied by dynamic PET and simple arterial sampling.

Brain↗

PubMed1997

Hyperfixation of copper-62-PTSM in rat brain after transient global ischemia.

UNLABELLED: We evaluated the regional distribution of 62Cu-pyruvaldehyde bis(N4-methylthiosemicarbazone) (62Cu-PTSM), a potential PET perfusion agent, in the rat brain and observed hyperfixation in transient global ischemia in rats. METHODS: The distribution of 62Cu-PTSM was examined in comparison with that of 123I-labeled p-iodophenyl-N-isopropylmethanphetamine (123I-IMP) as a reference blood flow marker. Brain uptake of these two tracers was measured in Wistar rats subjected to 30-min four-vessel occlusion followed by recirculation for 10 min, 1 hr or 1, 3 or 5 days. Tracers were injected intravenously into rats 10 min before decapitation. The activities of Complex I and Complex I-III of mitochondria and the concentration of sulfhydryl (SH) groups were also measured. RESULTS: Copper-62-PTSM showed accelerated accumulation in the brain at 1 hr and 1 day after reperfusion when compared with that of 123I-IMP (p < 0.01), and this enhancement was considered to be due to hyperfixation. At these time points, SH concentration was significantly decreased (p < 0.01). On the other hand, the activity of Complex I was not influenced by ischemia/reperfusion, but that of Complex I-III was decreased to 65-70% of the control level (p < 0.01). CONCLUSIONS: Copper-62-PTSM showed hyperfixation most possibly as a result of increased NADH concentration, caused by disturbed electron transport in mitochondria.

Animals↗

PubMed1998

Human biodistribution and dosimetry of the PET perfusion agent copper-62-PTSM.

UNLABELLED: Copper-62-pyruvaldehyde bis(N4-methyl)thiosemicarbazone (PTSM) has been proposed as a generator-produced radiopharmaceutical for perfusion imaging using PET. Several clinical studies have demonstrated the ability of 62Cu-PTSM to quantitate myocardial and cerebral perfusion in humans. Because 62Cu-PTSM is generator-produced, it can be provided to clinical centers without cyclotron availability and, therefore, represents a cost-effective, practical PET perfusion tracer for clinical applications. To assess the safety, time-dependent biodistribution, and whole-body and organ-specific absorbed radiation dose estimates of this tracer, a Phase I study of 62Cu-PTSM was performed using whole-body imaging with PET in 10 healthy volunteers and with the radiopharmaceutical delivered by a compact modular generator unit. METHODS: Five male and five female subjects underwent a series of clinical tests and head-to-midthigh, whole-body PET scans at three time points over 1 hr after intravenous injection of 62Cu-PTSM. Before injection of the tracer, PET transmission scans were performed and used to correct the emission data for attenuation. Final image data were expressed in units of mCi/cc. Using standard organ weights, the percent injected dose per organ was calculated. Biodistribution data were obtained at three different time points and from these data biological half-lives in different organs were determined for calculation of radiation absorbed dose estimates. RESULTS: The liver was seen as the critical organ receiving a dose of 0.0886 rad/mCi. This organ defined the maximum single injected dose at 56 mCi using the limit of 5 rads to a critical organ per study per year. The whole-body dose is 0.0111 rad/mCi, resulting in a 0.622 rad exposure with a maximum single injection dose. Only trace levels of activity were found in the urine, which suggests low levels of urinary excretion and bladder exposure. No significant clinical, electrocardiographic or laboratory abnormalities were seen after the injection of 62Cu-PTSM. CONCLUSION: Copper-62-PTSM is a clinically safe radiopharmaceutical with favorable dosimetry for human studies at injected doses significantly above those projected for use in clinical studies.

Adult↗

PubMed1999

Evaluation of 64Cu-ATSM in vitro and in vivo in a hypoxic tumor model.

UNLABELLED: We have evaluated Cu-diacetyl-bis(N4-methylthiosemicarbazone) (Cu-ATSM), an effective marker for the delineation of hypoxic but viable tissue, in vitro in the EMT6 carcinoma cell line under varying degrees of hypoxia and compared it with the flow tracer 64Cu-pyruvaldehyde-bis(N4-methylthiosemicarbazone) (Cu-PTSM) and the hypoxic tracer 18F-fluoromisonidazole (MISO). We have also compared the uptake of Cu-ATSM and Cu-PTSM in vivo and ex vivo in a murine animal model bearing the EMT6 tumor. METHODS: Uptake of 64Cu-ATSM, 64Cu-PTSM and 18F-MISO in vitro into EMT6 cells was investigated at the dissolved oxygen concentrations of 0, 1 x 10(3), 5 x 10(3), 5 x 10(4) and 2 x 10(5) ppm. Biodistribution performed at 1, 5, 10, 20 and 40 min compared 64Cu-ATSM with 64Cu-PTSM in BALB/c mice bearing EMT6 tumors. To determine long-term retention of 64Cu-ATSM, biodistribution was also performed at 1, 2 and 4 h. Ex vivo autoradiography of tumor slices after co-injection of 60Cu-PTSM (60Cu, T1/2 = 23.7 min) and 64Cu-ATSM (64Cu, t1/2 = 12.7 h) into the same animal was performed. RESULTS: After 1 h, 64Cu-ATSM was taken up by EMT6 cells: 90% at 0 ppm, 77% at 1 x 10(3) ppm, 38% at 5 x 10(3) ppm, 35% at 5 x 10(4) ppm and 31% at 2 x 10(5) ppm. 18F-MISO also showed oxygen concentration dependent uptake, but with lower percentages than 64Cu-ATSM. 64Cu-PTSM showed 83%-85% uptake into the cells after 1 h, independent of oxygen concentration. Biodistribution data of 64Cu-ATSM and 64Cu-PTSM showed optimal tumor uptake after 5 and 10 min, respectively (0.76% injected dose (ID)/organ for 64Cu-ATSM and 1.11%ID/organ for 64Cu-PTSM). Ex vivo imaging experiments showed 60Cu-PTSM uniform throughout the EMT6 tumor, but heterogeneous uptake of 64Cu-ATSM, indicative of selective trapping of 64Cu-ATSM into the hypoxic tumor cells. CONCLUSION: Cu-ATSM exhibits selectivity for hypoxic tumor tissue both in vivo and in vitro and may provide a successful diagnostic modality for the detection of tumor ischemia.

Animals↗

PubMed1999

Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases.

In this study, we investigate the neurotoxicity of glycation, particularly early-stage glycation, and its mechanisms, which are possibly synergized with oxidative stress. Methylglyoxal (MG) and 3-deoxyglucosone (3DG), intermediate products of glycation, are known to further accelerate glycation and advanced glycation endproducts (AGEs) formation. Both compounds showed neurotoxicity on cultured cortical neurons and these effects were associated with reactive oxygen species production followed by neuronal apoptosis. Pretreatment with N-acetylcysteine induced neuroprotection against MG and 3DG. Cotreatment, but not pretreatment, with aminoguanidine protected neurons against the neurotoxicities of both compounds. The present study provides the first evidence that MG and 3DG are neurotoxic to cortical neurons in culture. Interference with the process by which glycation and AGEs formation occur may provide new therapeutic opportunities to reduce the pathophysiological changes associated with neurodegeneration, if, as indicated here, the participation of glycoxidation in the pathogenesis of neurodegenerative diseases is essential.

Acetylcysteine↗

PubMed2000

Methylglyoxal induces apoptosis in Jurkat leukemia T cells by activating c-Jun N-terminal kinase.

Methylglyoxal (MG) is a physiological metabolite, but it is known to be toxic, inducing stress in cells and causing apoptosis. This study examines molecular mechanisms in the MG-induced signal transduction leading to apoptosis, focusing particularly on the role of JNK activation. We first confirmed that MG caused apoptosis in Jurkat cells and that it was cell type dependent because it failed to induce apoptosis in MOLT-4, HeLa, or COS-7 cells. A caspase inhibitor, Z-DEVD-fmk, completely blocked MG-induced poly(ADP-ribose)polymerase (PARP) cleavage and apoptosis, showing the critical role of caspase activation. Inhibition of JNK activity by a JNK inhibitor, curcumin, remarkably reduced MG-induced caspase-3 activation, PARP cleavage, and apoptosis. Stable expression of the dominant negative mutant of JNK also protected cells against apoptosis notably, although not completely. Correspondingly, loss of the mitochondrial membrane potential induced by MG was decreased by the dominant negative JNK. These results confirmed a crucial role of JNK working upstream of caspases, as well as an involvement of JNK in affecting the mitochondrial membrane potential.

Animals↗

PubMed1980

Acute myeloblastic leukemia in elderly patients: treatment and prognostic factors.

The results of treatment of acute myeloblastic leukemia in patients over 60 years of age are evaluated in a retrospective study of 29 previously untreated patients. These results were very similar to those observed for younger patients, with 18 complete remissions (62, 1%), 6 early deaths, and 5 treatment failures. The median survival time was seven and one half months for all patients and 22 for the 18 patients achieving complete remissions. Nineteen patients received chemotherapy identical to that of younger patients (daunorubicin and cytarabine). The initial presence of poor prognostic factors (hyperleukocytosis, and infection) may explain the relativity high number of early deaths (21%). Elderly patients are apparently not exposed to a higher risk of death than younger patients. Daunorubicin toxicity does not appear to increase with age and this agent may therefore be used in the treatment of older patients.

Aged↗

PubMed2002

Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis.

OBJECTIVE: Age is an important risk factor for osteoarthritis (OA). During aging, nonenzymatic glycation results in the accumulation of advanced glycation end products (AGEs) in cartilage collagen. We studied the effect of AGE crosslinking on the stiffness of the collagen network in human articular cartilage. METHODS: To increase AGE levels, human adult articular cartilage was incubated with threose. The stiffness of the collagen network was measured as the instantaneous deformation (ID) of the cartilage and as the change in tensile stress in the collagen network as a function of hydration (osmotic stress technique). AGE levels in the collagen network were determined as: Nepsilon-(carboxy[m]ethyl)lysine, pentosidine, amino acid modification (loss of arginine and [hydroxy-]lysine), AGE fluorescence (360/460 nm), and digestibility by bacterial collagenase. RESULTS: Incubation of cartilage with threose resulted in a dose-dependent increase in AGEs and a concomitant decrease in ID (r = -0.81, P < 0.001; up to a 40% decrease at 200 mM threose), i.e., increased stiffness, which was confirmed by results from the osmotic stress technique. The decreased ID strongly correlated with AGE levels (e.g., AGE fluorescence r = -0.81, P < 0.0001). Coincubation with arginine or lysine (glycation inhibitors) attenuated the threose-induced decrease in ID (P < 0.05). CONCLUSION: Increasing cartilage AGE crosslinking by in vitro incubation with threose resulted in increased stiffness of the collagen network. Increased stiffness by AGE crosslinking may contribute to the age-related failure of the collagen network in human articular cartilage to resist damage. Thus, the age-related accumulation of AGE crosslinks presents a putative molecular mechanism whereby age is a predisposing factor for the development of OA.

Adult↗

PubMed1978

Quantum chemical investigations of charge-transfer interactions in relation to the electronic theory of cancer.

The results of ab initio 'supermolecule' calculations of the charge transfer between formamide and methylglyoxal, dimethylglyoxal and ethylglyoxal are compared for several different relative conformations of the constituent molecules. The extent and sign of the charge transfer is similar for all three molecules; the ketoaldehyde acts as an electron acceptor only for the stacked conformation. Similar calculations on alpha-hydroxytetronic acid as a model for ascorbic acid show that it can act as either an acceptor from formamide or a donor to glyoxal.

Animals↗

PubMed1978

The search for new cancerostatic agents.

Following the lead given by Albert Szent-Györgyi's bioelectronic theory of cancer, work was continued in two major directions: (i) designing new electrophilic molecules, related to methylglyoxal, and (ii) using L-ascorbic acid as a (non-toxic) carrier for methylglyoxal and its derivatives in the form of its acetals. The vinylogue of methylglyoxal, 4-oxopent-2-enal, was expected to be a most reactive electron acceptor, on the basis of quantum mechanical calculations by J.J. Ladik's group. A new reaction, the formation of the ene-2, 3-diol acetal and hemiacetal-hemiketal, was found to occur with 'conjugated' aldehydes, such as methylglyoxal, glyoxal, phenylglyoxal, malealdehyde and acrylaldehyde; the reaction proceeded very smoothly with 4-oxopent-2-enal. The structural determination of these new types of acetals by 1H and 13C n.m.r. spectroscopy and by chemical methods is discussed.

Aldehydes↗

PubMed1978

Interactions of methylglyoxal with methylamine.

Ab initio quantum mechanical calculations are used to study the interactions of the aldehydic group of methylglyoxal with the NH2 groups of protein side-chains, using methylamine as a representative molecule. The hydrogen-bonding interaction, C = O...H - N, results in an electronic charge transfer from methylglyoxal to methylamine in both the ground and first excited triplet states. In this latter state a slight possibility is found for the H atom in the hydrogen bond to tunnel from methylglyoxal to methylamine, leading to the possible formation of two free radical fragments. The approach of methylamine to methylglyoxal in the stacked conformation C...N to form a hemiacetal, associated with electron charge transfer from methylamine to methylglyoxal, is energetically unfavourable in vacuum. The concomitant tunnelling of a proton from a proton-donating solvent molecule to the aldehydic oxygen of methylglyoxal is shown to make this approach favourable. The relative stability of the keto and enol forms of methylglyoxal is also investigated, the keto form being found the more stable in vacuum.

Aldehydes↗

PubMed1978

Methylglyoxal production in human blood.

The research of Szent-Györgyi and others has suggested that the three-carbon ketoaldehyde methylglyoxal has a potential role in the control of cell growth. Its metabolism to D-lactate (not the L-lactate of glycolysis) is catalysed by the mammalian enzymes glyoxalase I (S-lactoyl-glutathione methylglyoxal-lyase, isomerizing; EC 4.4.1.5) and glyoxalase II (S-2-hydroxyacylglutathione hydrolase; 3.1.2.6), with glutathione as a coenzyme. Direct determination of methylglyoxal in biological tissues is difficult because of the active glyoxalase system. However, the product of the glyoxalase system, D-lactate, should indicate formed or added methylglyoxal. A stereospecific assay was used to measure D-lactate in human plasma; it involved the spectrophotometric analysis of NADH at 340 nm catalysed by D-lactate dehydrogenase (D-lactate:NAD+ oxidoreductase; EC 1.1.1.28) from Lactobacillus leichmannii. Blood collected by venepuncture was used for the determination of the plasma concentration of D-lactate. The mean concentration for seven normal subjects was 0.023 mM +/- 0.002 S.E.M. When the glycolytic pathway in whole blood was inhibited in vitro with fluoride, a significant increase in D-lactate was found (about 0.15 mM/hour at 37 degrees C). Added methylglyoxal also produced an increase in D-lactate formation. Some specific precursors of L-lactate (dihydroxyacetone phosphate, for example) added to whole blood produced an increased concentration of D-lactate, even when glycolysis was not inhibited. This finding indicates that catabolites of glucose lead to methylglyoxal synthesis and suggest a control function for the glyoxalase enzyme system in glycolysis that could be exploited for cancer therapy.

Adult↗

PubMed1978

Biological activity of methylglyoxal and related aldehydes.

The effect of methylglyoxal and other aldehydes on several biochemical variables has been studied. Aldehydes inhibit amino acid incorporation into proteins, both in reconstituted systems and in isolated hepatocytes. They also decrease the secretion of protein and lipoprotein from hepatocytes into the incubation medium. This inhibition is seen even with prelabelled proteins, which indicates damage to the secretory mechanism itself. This conclusion is strenghened by the fact that aldehydes also decrease the binding of colchicine to liver tubulin. Aldehydes decrease the respiratory rate of mitochondria, as well as mitochondrial swelling induced by phosphate, by Ca2+ or by K+ plus valinomycin. They also partially inhibit cytochrome P-450. When injected into normal rats, aldehydes produce a decrease in the mitotic index of bone marrow cells and of the epithelial lining of the small intestine. A decrease in mitotic index and in cellularity is seen after injecting aldehydes into the peritoneal cavity of rats bearing transplanted ascites AH-130 Yoshida hepatoma. Aldehydes also impair the function of liver cell ligandin and potentiate the increase in cell permeability induced by 5-hydroxytryptamine (serotonin). The meaning of these results is discussed with special reference to the pathogenesis of cellular lesions in carbon tetrachloride poisoning.

Aldehydes↗

PubMed1978

Carcinostatic activity of methylglyoxal and related substances in tumour-bearing mice.

Methylglyoxal treatment of tumour cells in vitro primarily depresses protein synthesis, in contrast to trans-4-hydroxypent-2-enal (HPE) which preferentially inhibits DNA synthesis. Methylglyoxal and hpe are potent carcinostatic agents in vitro but relatively ineffective in vivo. Both aldehydes have a short half-life in vivo which may explain their poor carcinostatic properties when administered other than peritumorally. Several possibilities of increasing the effective half-life were investigated including (i) multiple intraperitoneal injections, (ii) concomitant administration of an inhibitor of glyoxalase I, (iii) administration of aldehyde-cysteine adducts, and (iv continuous intravenous infusion. Methylglyoxal (36 mg/kg i.p., twice daily) was slightly less effective in inhibiting the growth of the solid form of Ehrlich carcinoma than a dose of 72 mg/kg (inj. 1); 36 mg/kg (inj. 2) 46.2% compared to 51%. The aldehyde was more effective aginst the ascitic form of the tumour, with 99.76% inhibition of growth after giving 72 mg/kg twice daily for five days followed by 36 mg/kg for five days. The glyoxalase I inhibitor S-(p-bromobenzyl)-glutathione didnot significantly enhance the activity of methylglyoxal against the solid form of the tumour. Nicotinamide (1% w/v in the drink) was similarily inactive. Methylglyoxal in combination with nicotinamide was significantly more effect (P less than 0.05) than methylglyoxal alone (36 mg/kg, twice daily) in inhibiting the growth of the ascitic tumour. Methylglyoxal-N-acetyl-L-cysteine was four times less toxic than methylglyoxalalone but was marginally less effective against the ascitic form of the tumour. Doses of these adducts equivalent to 144 mg/kg per day of methylglyoxal were more effective P less than 0.05) than the optimal regime of methylglyoxal in inhibiting the solid tumour (67.5% inhibition compared to 51%). Treatment of mice bearing the ascitic form of Sarcoma 180 with five daily doses (i.p.) of an HPE-cysteine adduct equivalent to a dose of HPE alone of 32-256 mg/kg per day significantly increased survival time by comparison with controls. The adduct was 2-3 times more effective, dose-for-dose, than HPE alone in inhibiting tumour growth. Purified buffered methylglyoxal has an LD50 on continuous infusion into the right lateral tail vein in mice of more than 3.0 mg/g per day (seven days at 2.8 ml/day). Local oedema followed by tail necrosis occurs at doses in excess of 0.25-0.5 mg/g per day in mice bearing the solid forms of the syngeneic tumours: squamous carcinoma D; lymphosarcoma 1 (WH/Ht mice); and spontaneous mammary D5056 (CBA/CA mice). A maximum tumour volume growth delay of 3.4 days at Day 17 (P less than 0.001) after transplantation was observed after infusion of 0.5 mg/g per day methylglyoxal on Days 11-17 in the CBA/CA D40 syngeneic mammary tumour. Tumour regrowth after termination of therapy eliminated the significant difference between control and methylglyoxal-treated tumours by Day 27. Methylglyoxal infusion (0...

Aldehydes↗

PubMed1978

The living state and cancer.

The surrounding world can be divided into two parts: alive and inanimate. What makes the difference is the subtle reactivity of living systems. The difference is so great that it is reasonable to suppose that what underlies life is a specific physical state, 'the living state'. Living systems are built mainly of nucleic acids and proteins. The former are the guardians of the basic blueprint while the business of life is carried on by proteins. Proteins thus have to share the subtle reactivity of living systems. A closed-shell protein molecule, however, has no electronic mobility, and has but a low chemical reactivity. Its orbitals are occupied by electron pairs which are held firmly. The situation can be changed by taking single electrons out of the system. This unpairs electrons, leaves half-occupied orbitals with positive electron holes, making the molecules into highly reactive paramagnetic free radicals. The reactivity of the system depends on the degree of its electronic desaturation. Electrons can be taken out of protein molecules by 'electron aceptors' in 'cahrge transfer'. When life began, our globe was covered by dense water vapour. There was no light and no free oxygen. Electron acceptors could be made out of trioses by concentrating their carbon atoms as carbonyls at one end of the molecule. The resulting methylglyoxal is a weak acceptor which made a low level of development possible. When light appeared, free oxygen was generated by the energy of photons. Oxygen is a strong electron acceptor. Its appearance opened the way to the present level of development. The transfer of electrons from protein to oxygen is effected by a complex chemical mechanism which involves ascorbic acid.

Animals↗

PubMed1978

Energy bands and charge transfer in proteins.

The effects of salts on protein--the causing of a shift in isoelectric point and the altering of the melting temperature--are proposed to be the result of binding to the protein peptide chain, which is considered as a one-dimensional solid. The interaction of methylglyoxal with protein and polylysine to give charge-transfer complexes and allow electrical conductivity are viewed as further support for the band structure of proteins. Calculations on protein chains resembling real proteins show that conductivity should be much less than expected for homopolypeptides.

Electric Conductivity↗

PubMed1978

The mechanisms of conduction in proteins.

Theoretical calculations have already shown that the electronic properties of biopolymers may be described in terms of conduction and valence energy bands in which electrons are delocalized to a significant degree. Because these bands are separated by a large energy gap, it is concluded that electronic conduction in such systems must be by 'holes' in the valence band. The mechanism of this conduction is discussed with special reference to dry proteins where the charge-transfer role of appropriate acceptor molecules and the modulating influence of amino acid residues will encourage localized and delocalized hole production at the valence band edge. It is suggested that there are close similarities, which have shown up in measurements, in the electrical behaviour of proteins and other non-biological semi-crystalline solids. The significance of such long-range conduction and attendant polarization is considered briefly in the light of evidence for the existence of proteins in cell membranes and in the skeleton of the cytoplasm

Electric Conductivity↗

PubMed1985

Effect of methylglyoxal on tumour microtubular protein.

Methylglyoxal inhibits cell division, exerting an antiproliferative action on tumour cells. Supernatants from ascites hepatoma cell homogenate, previously incubated with the aldehyde, showed a decrease in colchicine binding activity dependent on methylglyoxal concentration. In contrast, in vivo treatment of tumour-bearing rats apparently did not cause a significant impairment of microtubular protein, suggesting that the aldehyde interaction with microtubules cannot be considered responsible for its carcinostatic action.

Aldehydes↗