Biomedical subjects

Attila Tóth

Publications and source records attributed to Attila Tóth.

23 records · Page 2Linked to original sources

PubMed2003

[Direct application of fiber-reinforced composites in splinting in a case of periodontitis. II].

Attachment loss through advanced periodontitis results in tooth mobility, and then loss of teeth. To prevent progression it is needed to eliminate any exciting agent and correct functional disorders in consequence of disease. Regeneration of periodontium is impossible and mastication is difficult because of tooth mobility. Long-term maintenance of mobile teeth is doubtful. We have to prevent the extraction of these teeth to stabilise them by a splint made of material that is inexpensive, reparable, provides sufficient support for the artificial tooth. Fiber-Reinforced Composite (FRC) fulfills the above requirements. In their case-reports the authors demonstrate the practical application of splinting with FRC materials. In these cases the FRC splints are not only periodontal splints but they act as orthodontic retainers or supports for an artificial tooth.

Adult↗

PubMed2003

Calpain-1-dependent degradation of troponin I mutants found in familial hypertrophic cardiomyopathy.

The mechanism by which mutations of the cardiac troponin I (cTnI) gene evoke familial hypertrophic cardiomyopathy (fHCM) is unknown. In this investigation the potential effects of three fHCM-related cTnI mutations on Calpain-1-induced cTnI degradation were tested, and a study was made of whether additional conformational changes due to troponin complex formation and protein kinase A-induced phosphorylation affect the intensity of cTnI proteolysis. Purified recombinant wild-type cTnI and three of its fHCM-related missense mutants (R145G, G203S and K206Q), alone or in the troponin complex (i.e. together with troponin C and troponin T), in the non-phosphorylated or protein kinase A-bisphosphorylated forms were proteolyzed in vitro in the presence of Calpain-1 (0.05-2.5 U) at 30 degrees C. Following incubation with Calpain-1 for 0.5, 30, 60 or 120 min, the extent of protein degradation was evaluated through the use of Western immunoblotting and densitometry. The results indicated that both the wild-type and the mutant cTnI molecules were susceptible to Calpain-1. However, the degradation of the cTnI molecules in the troponin complex was less intense than that of the non-complexed forms. Moreover, phosphorylation by protein kinase A conferred effective protection against cTnI proteolysis. The data suggested that mutations in the central inhibitory domain (R145G) and in the C-terminal region (G203S and K206Q) of cTnI do not affect its Calpain-1-mediated degradation, or the phosphorylation-induced protection against proteolysis.

Blotting, Western↗

PubMed2002

Thapsigargin binds to and inhibits the cloned vanilloid receptor-1.

We investigated the effect of thapsigargin, a well-known sarcoplasmic reticulum ATPase (SERCA) inhibitor, on the non-specific Ca2+ channel vanilloid receptor-1 (VR1) in CHO-VR1 cells. We found that thapsigargin inhibited the VR-1 mediated (45)Ca2+ uptake of CHO-VR1 cells (IC50=6.4+/-1.9 microM) and the [3H]RTX binding to VR1 (IC50=4.0+/-1.3 microM). Further analysis revealed that thapsigargin is a mixed-type inhibitor, suggesting both direct and indirect interactions between thapsigargin and the capsaicin binding site of VR1. Thapsigargin alone transiently elevated the [Ca2+]i in CHO-VR1 cells (EC50=44 nM). However, 45Ca2+ uptake was not detected after thapsigargin treatment, indicating that the emptying of the thapsigargin sensitive intracellular pools of Ca2+ was responsible for the elevated [Ca2+]i level rather than the activation of VR-1. We conclude that thapsigargin represents a new prototype of a VR1 inhibitor and that caution should be exercised in interpreting the effects of thapsigargin, especially when it is used in the micromolar range to inhibit SERCA activity.

Animals↗

PubMed2002

The application of elastomeric connector for multi-channel electrophysiological recordings.

Interest in recording multi-channel electrophysiological data from behaving animals is rapidly growing, and many laboratories tend to record a large number of EEG and/or multi-unit channels, despite the limitation of the size of the headpiece that a small behaving animal can carry. A common drawback of these experiments, therefore, is the relatively large size of even the smallest, commercially available, high-density micro-connectors for the headset. To overcome this problem, we suggest the application of elastomeric or silicone inter-rubber connectors, that are widely used in electronics. The elastomeric or "zebra" connector consists of alternating thin strips of layered electrically conductive and non-conductive materials. The conductive strips provide electrical connections between uninsulated contact surfaces of printed circuit boards such as the connector plate of the micro-drive, that holds the brain electrode wires, and the preamplifier board of the recording system. In the present paper, we provide technical details of the design of this type of connector-sets and discuss common issues arising from their use. By comparing the applicability of two designs, we aim to demonstrate the simplicity, reliability and durability of the elastomeric inter-rubber connectors in electrophysiological experiments on freely moving laboratory animals.

Animals↗

PubMedDate not supplied

Activation of the poly(ADP-ribose) polymerase pathway in human heart failure.

Poly(ADP-ribose) polymerase (PARP) activation has been implicated in the pathogenesis of acute and chronic myocardial dysfunction and heart failure. The goal of the present study was to investigate PARP activation in human heart failure, and to correlate PARP activation with various indices of apoptosis and oxidative and nitrosative stress in healthy (donor) and failing (NYHA class III-IV) human heart tissue samples. Higher levels of oxidized protein end-products were found in failing hearts compared with donor heart samples. On the other hand, no differences in tyrosine nitration (a marker of peroxynitrite generation) were detected. Activation of PARP was demonstrated in the failing hearts by an increased abundance of poly-ADP ribosylated proteins. Immunohistochemical analysis revealed that PARP activation was localized to the nucleus of the cardiomyocytes from the failing hearts. The expression of full-length PARP-1 was not significantly different in donor and failing hearts. The expression of caspase-9, in contrast, was significantly higher in the failing than in the donor hearts. Immunohistochemical analysis was used to detect the activation of mitochondrial apoptotic pathways. We found no significant translocation of apoptosis-inducing factor (AIF) into the nucleus. Overall, the current data provide evidence of oxidative stress and PARP activation in human heart failure. Interventional studies with antioxidants or PARP inhibitors are required to define the specific roles of these factors in the pathogenesis of human heart failure.

Adenosine Diphosphate Ribose↗