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1.

001-es BibID:BIBFORM003867
Első szerző:Hernádi László
Cím:The presence and distribution of pituitary adenylate cyclase activating polypeptide and its receptor in the snail helix pomatia / L. Hernádi, Z. Pirger, T. Kiss, J. Németh, L. Mark, P. Kiss, A. Tamas, A. Lubics, G. Toth, S. Shioda, D. Reglodi
Dátum:2008
Megjegyzések:The aim of this study was to show the presence, distribution and function of the pituitary adenylate cyclase activating polypeptide (PACAP) and its receptors in the CNS and peripheral nervous system of the mollusk, Helix pomatia. PACAP-like and pituitary adenylate cyclase activating polypeptide receptor (PAC1-R)-like immunoreactivity was abundant both in the CNS and the peripheral nervous system of the snail. In addition several non-neuronal cells also revealed PACAP-like immunoreactivity. In inactive animals labeled cell bodies were mainly found and in the neuropile of active animals dense immunostained fiber system was additionally detected suggesting that expression of PACAP-like peptide was affected by the behavioral state of the animal. RIA measurements revealed the existence of both forms of PACAP in the CNS where the 27 amino acid form was found to be dominant. The concentration of PACAP27 was significantly higher in samples from active animals supporting the data obtained by immunohistochemistry. In Western blot experiments PACAP27 and PACAP38 antibodies specifically labeled protein band at 4.5 kDa both in rat and snail brain homogenates, and additionally an 14 kDa band in snail. The 4.5 kDa protein corresponds to PACAP38 and the 14 kDa protein corresponds to the preproPACAP or to a PACAP-like peptide having larger molecular weight than mammalian PACAP38. In matrix-assisted laser desorption ionization time of flight (MALDI TOF) measurements fragments of PACAP38 were identified in brain samples suggesting the presence of a large molecular weight peptide in the snail. Applying antibodies developed against the PACAP receptor PAC1-R, immunopositive stained neurons and a dense network of fibers were identified in each of the ganglia. In electrophysiological experiments, extracellular application of PACAP27 and PACAP38 transiently depolarized or increased postsynaptic activity of neurons expressing PAC1-R. In several neurons PACAP elicited a long lasting hyperpolarization which was eliminated after 1.5 h continuous washing. Taken together, these results indicate that PACAP may have significant role in a wide range of basic physiological functions in snail.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
pituitary adenylate cyclase activating polypeptide,
Megjelenés:Neuroscience. - 155 : 2 (2008), p. 387-402. -
További szerzők:Pirger Zsolt Kiss Tibor Németh József (1954-) (vegyész, analitikus) Márk László (1956-) (belgyógyász, kardiológus) Kiss Péter Tamás Andrea (Idegtudomány) (Pécs) Lubics Andrea (Pécs) Tóth Gábor Shioda, Seiji Reglődi Dóra (Idegtudományok)
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2.

001-es BibID:BIBFORM003874
Első szerző:Pirger Zsolt
Cím:PACAP has anti-apoptotic effect in the salivary gland of an invertebrate species, helix pomatia / Zsolt Pirger, Jozsef Nemeth, Laszlo Hiripi, Gabor Toth, Peter Kiss, Andrea Lubics, Andrea Tamas, Laszlo Hernadi, Tibor Kiss, Dora Reglodi
Dátum:2008
Megjegyzések:Pituitary adenylate cyclase activating polypeptide (PACAP) shows a remarkable sequence similarity among species and several studies provide evidence that the functions of PACAP have also been conserved among vertebrate species. Relatively little is known about its presence and functions in invertebrates. The aim of the present study was to investigate whether the well-known anti-apoptotic effect of PACAP can also be demonstrated in invertebrates. This effect was studied in the salivary gland of a molluscan species, Helix pomatia. In this work, we first showed the presence of PACAP-like immunoreactivity in the Helix salivary gland by means of immunohistochemistry. Radioimmunoassay measurements showed that PACAP38-like immunoreactivity dominated in the salivary gland of both active and inactive snails and its concentration was higher in active than in inactive animals in contrast to PACAP27-like immunoreactivity, which did not show activity-dependent changes. PACAP induced a significant elevation of cAMP level in salivary gland extracts. Application of apoptosis-inducing agents, dopamine and colchicine, led to a marked increase in the number of terminal uridine deoxynucleotidyl transferase dUTP nick end labeling (TUNEL)-positive apoptotic cells in the salivary gland, which was significantly attenuated by PACAP treatment. In a similar manner, the number of caspase-positive cells was reduced after co-application of dopamine and PACAP. Taken together, the data indicate that PACAP activates cAMP in a molluscan species and we show, for the first time, that PACAP is anti-apoptotic in the invertebrate Helix pomatia.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Caspase-3
TUNEL
RIA
cAMP
Apoptosis
Megjelenés:Journal of molecular neuroscience. - 36 : 1-3 (2008), p. 105-114. -
További szerzők:Németh József (1954-) (vegyész, analitikus) Hiripi László Tóth Gábor Kiss Péter Lubics Andrea (Pécs) Tamás Andrea (Idegtudomány) (Pécs) Hernádi László Kiss Tibor Reglődi Dóra (Idegtudományok)
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3.

001-es BibID:BIBFORM003875
Első szerző:Reglődi Dóra (Idegtudományok)
Cím:Agonistic behavior of PACAP6-38 on sensory nerve terminals and cytotrophoblast cells / D. Reglodi, R. Borzsei, T. Bagoly, A. Boronkai, B. Racz, A. Tamas, P. Kiss, G. Horvath, R. Brubel, J. Nemeth, G. Toth, Z. Helyes
Dátum:2008
Megjegyzések:The effects of pituitary adenylate cyclase activating polypeptide (PACAP) are mediated through Gprotein-coupled receptors, the specific PAC1 receptor and VPAC1 and VPAC2 receptors which bind vasoactive intestinal peptide with similar affinity. Based on binding affinity studies, PACAP6-38 was discovered as a potent antagonist of PAC1 and it has been used by hundreds of studies as a PACAP antagonist. Recently, we have found that in certain cells/tissues, PACAP6-38 does not antagonize PACAP-induced effects, but surprisingly, it exerts similar actions to PACAP1-38, behaving as an agonist. In the present study, we report on the agonistic behavior of PACAP6-38 on neuropeptide release from sensory nerves of the isolated rat trachea and on the MAPK signaling pathways in cytotrophoblast cells. In isolated rat tracheae, PACAP6-38, similarly to PACAP1-38, induced significant inhibitory effects on the release of three simultaneously measured sensory neuropeptides, substance P, calcitonin gene-related peptide, and somatostatin evoked by both chemical excitation and electrical field stimulation of capsaicin-sensitive afferents. Effects of PACAP6-38 were the same as those of PACAP1-38 on MAPK signaling in human cytotrophoblast cells. Western blot analysis showed that both peptide forms stimulated ERK1/2 and JNK phosphorylation, while they both inhibited p38 MAPK phosphorylation. The most pronounced effects were observed when both peptides were present. In summary, our results show that PACAP6-38, which is a PACAP receptor antagonist in most cells/tissues, can behave as an agonist in other systems. The increasing interest in the effects of PACAP requires further studies on the pharmacological properties of the peptide and its analogues.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
PACAP fragment
Analogue
Somatostatin
Substance P
JAR cytotrophoblast
CGRP
Megjelenés:Journal of Molecular Neuroscience. - 36 : 1-3 (2008), p. 270-278. -
További szerzők:Börzsei Rita Bagoly Teréz Boronkai A. Rácz Boglárka Tamás Andrea (Idegtudomány) (Pécs) Kiss Péter Horváth G. Brubel Réka Tóth Gábor Helyes Zsuzsanna Németh József (1954-) (vegyész, analitikus)
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