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1.

001-es BibID:BIBFORM039245
Első szerző:Ács Géza (traumatológus)
Cím:Differential activation and desensitization of sensory neurons by resiniferatoxin / Acs, G., Biro, T., Acs, P., Modarres, S., Blumberg, P. M.
Dátum:1997
ISSN:0270-6474
Megjegyzések:Recently, with use of rat dorsal root ganglion (DRG) neurons we have been able to dissociate the binding affinities of vanilloids from their potencies to induce Ca-45 uptake, which suggests the existence of distinct classes of the vanilloid receptor (Acs et al., 1996). In the present study, we have demonstrated that the ultrapotent capsaicin analog resiniferatoxin (RTX) desensitized rat DRG neurons to the subsequent induction of Ca-45 uptake by capsaicin and RTX with affinity and cooperativity similar to that found for [H-3]RTX binding, contrasting with a similar to 10-fold weaker potency and lack of cooperativity to induce Ca-45 uptake. Likewise, the competitive antagonist capsazepine inhibited RTX-induced desensitization with potency similar to that for inhibition of specific [H-3]RTX binding, whereas the potency of capsazepine was similar to 10-fold higher for inhibiting RTX-induced Ca-45 uptake. Finally, the noncompetitive antagonist ruthenium red inhibited both the RTX-induced desensitization and Ca-45 uptake but showed similar to 60-fold selectivity for inhibiting RTX-induced desensitization. The RTX-induced desensitization was not associated with loss of specific [H-3]RTX binding, suggesting lack of gross cell toxicity. In contrast to RTX, capsaicin caused desensitization with a potency corresponding to that for Ca-45 uptake and did so in a noncooperative manner. Unlike the RTX-induced desensitization, the desensitization by capsaicin was blocked by ruthenium red only at doses that blocked Ca-45 uptake and depended on external calcium, Our findings provide further support for the existence of vanilloid receptor subtypes on DRG neurons with distinct pharmacology and distinct patterns of desensitization.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Neuroscience. - 17 : 14 (1997), p. 5622-5628. -
További szerzők:Bíró Tamás (1968-) (élettanász) Ács Péter Modarres, Shayan Blumberg, Peter M.
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM039234
035-os BibID:PMID:9268359
Első szerző:Ács Péter
Cím:The catalytic domain of protein kinase C chimeras modulates the affinity and targeting of phorbol ester-induced translocation / Péter Ács, Krisztina Bögi, Patricia S. Lorenzo, Adriana M. Marquez, Tamás Bíró, Zoltán Szállási, Peter M. Blumberg
Dátum:1997
ISSN:0021-9258
Megjegyzések:Abstract Emerging evidence suggests important differences among protein kinase C (PKC) isozymes in terms of their regulation and biological functions. PKC is regulated by multiple interdependent mechanisms, including enzymatic activation, translocation of the enzyme in response to activation, phosphorylation, and proteolysis. As part of our ongoing studies to define the factors contributing to the specificity of PKC isozymes, we prepared chimeras between the catalytic and regulatory domains of PKCalpha, -delta, and -epsilon. These chimeras, which preserve the overall structure of the native PKC enzymes, were stably expressed in NIH 3T3 fibroblasts. Their intracellular distribution was similar to that of the endogenous enzymes, and they responded with translocation upon treatment with phorbol 12-myristate 13-acetate (PMA). We found that the potency of PMA for translocation of the PKCalpha/x chimeras from the soluble fraction was influenced by the catalytic domain. The ED50 for translocation of PKCalpha/alpha was 26 nM, in marked contrast to the ED50 of 0.9 nM in the case of the PKCalpha/epsilon chimera. In addition to this increase in potency, the site of translocation was also changed; the PKCalpha/epsilon chimera translocated mainly into the cytoskeletal fraction. PKCx/epsilon chimeras displayed twin isoforms with different mobilities on Western blots. PMA treatment increased the proportion of the higher mobility isoform. The two PKCx/epsilon isoforms differed in their localization; moreover, their localization pattern depended on the regulatory domain. Our results emphasize the complex contributions of the regulatory and catalytic domains to the overall behavior of PKC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Journal of Biological Chemistry. - 272 : 35 (1997), p. 22148-22153. -
További szerzők:Bögi Krisztina Lorenzo, Patricia S. Marquez, Adriana M. Szállási Zoltán Blumberg, Peter M. Bíró Tamás (1968-) (élettanász)
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3.

001-es BibID:BIBFORM039265
035-os BibID:PMID:9353351
Első szerző:Ács Péter
Cím:Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells / Péter Ács, Qiming J. Wang, Krisztina Bögi, Adriana M. Marquez, Patricia S. Lorenzo, Tamás Bíró, Zoltán Szállási, J. Frederic Mushinski, Peter M. Blumberg
Dátum:1997
ISSN:0021-9258
Megjegyzések:Protein kinase C (PKC) isozymes exhibit important differences in terms of their regulation and biological functions. Not only may some PKC isoforms be active and others not for a given response, but the actions of different isoforms may even be antagonistic. In NIH 3T3 cells, for example, PKCdelta arrests cell growth whereas PKCepsilon stimulates it. To probe the contribution of the regulatory and the catalytic domains of PKC isozymes to isozyme-specific responses, we prepared chimeras between the regulatory and the catalytic domains of PKCalpha, -delta, and -epsilon. These chimeras, which preserve the overall structure of the native PKC enzymes, were stably expressed in mouse fibroblasts. A major objective was to characterize the growth properties of the cells that overexpress the various PKC constructs. Our data demonstrate that both the regulatory and the catalytic domains play roles in cell proliferation. The regulatory domain of PKCepsilon enhanced cell growth in the absence or presence of phorbol 12-myristate 13-acetate (PMA), and, in the presence of PMA, all chimeras with the PKCepsilon regulatory domain also gave rise to colonies in soft agar; the role of the catalytic domain of PKCepsilon was evident in the PMA-treated cells that overexpressed the PKC chimera containing the delta regulatory and the epsilon catalytic domains (PKCdelta/epsilon). The important contribution of the PKCepsilon catalytic domain to the growth of PKCdelta/epsilon-expressing cells was also evident in terms of a significantly increased saturation density in the presence of PMA, their formation of foci upon PMA treatment, and the induction of anchorage-independent growth. Aside from the growth-promoting effect of PKCepsilon, we have shown that most chimeras with PKCalpha and -delta regulatory domains inhibit cell growth. These results underscore the complex contributions of the regulatory and catalytic domains to the overall behavior of PKC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Journal of Biological Chemistry. - 272 : 45 (1997), p. 28793-28799. -
További szerzők:Wang, Qiming J. Bögi Krisztina Marquez, Adriana M. Lorenzo, Patricia S. Szállási Zoltán Mushinski, J. Frederic Blumberg, Peter M. Bíró Tamás (1968-) (élettanász)
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4.

001-es BibID:BIBFORM039246
Első szerző:Bíró Tamás (élettanász)
Cím:Recent advances in understanding of vanilloid receptors : a therapeutic target for treatment of pain and inflammation in skin / Biro, T., Acs, G., Acs, P., Modarres, S., Blumberg, P. M.
Dátum:1997
Megjegyzések:C-fiber sensory afferent neurons, which contain neuropeptides such as calcitonin-gene related peptide and substance P, mediate a wide variety of physiologic responses, including chemogenic pain, thermoregulation, and neurogenic inflammation. Capsaicin, the pungent constituent in red pepper, functions to activate and then, at higher doses and longer times, desensitize this class of neurons, This latter response provides the basis for the therapeutic application of capsaicin, A major advance in the field has been the identification of resiniferatoxin, a phorbol-related diterpene, as an analog of capsaicin that is ultrapotent but with differential selectivity, In particular, resiniferatoxin is only similar in potency for induction of pain but is much more effective for desensitization, Structure-activity analysis in whole animal experiments provides further evidence for dissociation of biologic endpoints, strongly arguing for the existence of vanilloid receptor subclasses, Using resiniferatoxin, we have been able to define specific, high-affinity receptors for capsaicin both in animal models such as rats and in man, Of great importance, the pharmacologic characterization in cultured dorsal root ganglion cells of the high-affinity resiniferatoxin-binding site and of tile physiologic response believed to be directly coupled to the receptor, viz, calcium uptake, differed in structure-activity and in cooperativity. We conclude that multiple high-affinity vanilloid receptor subclasses mediate vanilloid response; moreover, the resiniferatoxin-selective subclass of vanilloid receptors is not the voltage-independent, cation-nonselective ion channel as previously believed, Optimization of ligands for the individual vanilloid receptor subclasses should revolutionize this therapeutic area.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Investigative Dermatology Symposium Proceedings. - 2 : 1 (1997), p. 56-60. -
További szerzők:Ács Géza (1939-) (traumatológus) Ács Péter Modarres, Shayan Blumberg, Peter M.
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM039266
Első szerző:Bíró Tamás (élettanász)
Cím:Characterization of functional vanilloid receptors expressed by mast cells / Biro, T., Maurer, M., Modarres, S., Lewin, N. E., Brodie, C., Acs, G., Acs, P., Paus, R., Blumberg, P. M.
Dátum:1998
ISSN:0006-4971
Megjegyzések:Capsaicin and its ultrapotent analog resiniferatoxin (RTX) act through specific vanilloid receptors on sensory neurons. The C-type receptor is coupled to Ca-45 uptake, whereas the R-type is detectable by [H-3]RTX binding. We describe here specific vanilloid responses in murine mast cells (MCs). In the MC lines and in bone marrow-derived mast cells. capsaicin and RTX induced Ca-45 uptake similarly to that observed for cultured rat dorsal root ganglion neurons (DRGs). This response was antagonized by the antagonists capsazepine and ruthenium red. As in DRGs, pretreatment of MCs with capsaicin or RTX induced desensitization to subsequent stimulation of Ca-45 uptake. The potency for desensitization by RTX in the MCs corresponded to that for Ca-45 uptake, whereas in DRGs it occurred at significantly lower concentrations corresponding to that for the high-affinity [H-3]RTX binding site. Consistent with this difference, in MCs we were unable to detect [H-3]RTX binding. Vanilloids were noncytotoxic to the MCs, in contrast to the DRGs. Although vanilloids did not cause degranulation in MCs, in the P815 clone capsaicin evoked selective interleukin-4 release. We conclude that certain MCs possess vanilloid receptors, but only the C-type that functions as a channel. Our finding that MCs can respond directly to capsaicin necessitates a reevaluation of the in vivo pathway of inflammation in response to vanilloids. This is a US government work. There are no restrictions on its use.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Blood. - 91 : 4 (1998), p. 1332-1340. -
További szerzők:Maurer, Marcus Modarres, Shayan Lewin, Nancy E. Brodie, Chaya Ács Géza (1939-) (traumatológus) Ács Péter Paus, Ralf Blumberg, Peter M.
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6.

001-es BibID:BIBFORM039235
035-os BibID:PMID:9602075
Első szerző:Bíró Tamás (élettanász)
Cím:Specific vanilloid responses in C6 rat glioma cells / Tamás Bíró, Chaya Brodie, Shayan Modarres, Nancy E. Lewin, Péter Ács, Peter M. Blumberg
Dátum:1998
ISSN:0169-328X
Megjegyzések:Capsaicin and its ultrapotent analog resiniferatoxin (RTX) act through specific vanilloid receptors on sensory neurons. Here, we describe specific vanilloid responses in rat C6 glioma cells. Capsaicin and RTX stimulated 45Ca uptake in a similar fashion to that found for cultured rat dorsal root ganglion neurons (DRGs); this response was antagonized by the antagonists capsazepine and ruthenium red. As in DRGs, pretreatment of C6 cells with capsaicin or RTX produced desensitization to subsequent stimulation of 45Ca uptake. The potency for desensitization by RTX in the C6 cells corresponded to that for 45Ca uptake, whereas in DRGs it occurred at significantly lower concentrations corresponding to that for the high affinity [3H]RTX binding site. Consistent with this difference, in C6 cells we were unable to detect [3H]RTX binding. These characteristics suggest the presence of C-type but not R-type vanilloid receptors on C6 cells. After 2 day treatment, capsaicin but not RTX inhibited the proliferation and altered the differentiation of the cells and produced apoptosis. In the long term experiments, capsazepine, instead of antagonizing the effect of capsaicin, acted as an agonist. Moreover, capsazepine displayed these effects with higher potency than that of capsaicin. The different potencies and structure activity relations suggest a distinct mechanism for these long-term vanilloid effects. Our finding that C6 cells can respond directly to capsaicin necessitates a reevaluation of the in vivo pathway of response to vanilloids, and highlights the importance of the neuron-glial network.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Molecular Brain Research. - 56 : 1-2 (1998), p. 89-98. -
További szerzők:Brodie, Chaya Modarres, Shayan Lewin, Nancy E. Ács Péter Blumberg, Peter M.
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7.

001-es BibID:BIBFORM014361
Első szerző:Czifra Gabriella (élettanász)
Cím:Insulin-like growth factor-I-coupled mitogenic signaling in primary cultured human skeletal muscle cells and in C2C12 myoblasts : a central role of protein kinase C[delta] / Gabriella Czifra, István Balázs Tóth, Rita Marincsák, István Juhász, Ilona Kovács, Péter Ács, László Kovács, Peter M. Blumberg, Tamás Bíró
Dátum:2006
ISSN:0898-6568
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cellular Signalling. - 18 : 9 (2006), p. 1461-1472. -
További szerzők:Tóth István Balázs (1978-) (élettanász) Marincsák Rita (1979-) (fogszakorvos) Juhász István (1956-) (bőrgyógyász, bőrsebész, kozmetológus, klinikai onkológus) Kovács Ilona (1965-) (patológus) Ács Péter Kovács László Blumberg, Peter M. Bíró Tamás (1968-) (élettanász)
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8.

001-es BibID:BIBFORM014365
Első szerző:Papp Helga
Cím:Opposite roles of protein kinase C isoforms in proliferation, differentiation, apoptosis, and tumorigenicity of human HaCaT keratinocytes / H. Papp, G. Czifra, E. Bodó, J. Lázár, I. Kovács, M. Aleksza, I. Juhász, P. Ács, S. Sipka, L. Kovács, P. M. Blumberg, T. Bíró
Dátum:2004
ISSN:1420-682X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cellular And Molecular Life Sciences. - 61 : 9 (2004), p. 1095-1105. -
További szerzők:Czifra Gabriella (1975-) (élettanász) Bodó E. Lázár J. Kovács Ilona (1965-) (patológus) Aleksza Magdolna Juhász István (1956-) (bőrgyógyász, bőrsebész, kozmetológus, klinikai onkológus) Ács Péter Sipka Sándor (1945-) (laboratóriumi szakorvos) Kovács László (1939-) (élettanász) Blumberg, Peter M. Bíró Tamás (1968-) (élettanász)
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9.

001-es BibID:BIBFORM042105
Első szerző:Szállási Zoltán
Cím:Non-equivalent roles for the first and second zinc fingers of protein kinase Cdelta : effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells / Szállási Z., Bogi, K., Gohari, S., Biro, T., Acs, P., Blumberg, P. M.
Dátum:1996
ISSN:0021-9258
Megjegyzések:Classical and novel protein kinase C (PKC) isozymes contain two, so-called cysteine-rich zinc finger domains that represent the binding sites for phorbol esters and the diacylglycerols. X-ray crystallographic, mutational, and modeling studies are providing detailed understanding of the interactions between the phorbol esters and individual PKC zinc fingers. In the present study, we explore the roles of the individual zinc fingers in the context of the intact enzyme. Our approach was to mutate either the first, the second, or both zinc fingers of PKC?, to express the mutated enzyme in NIH 3T3 cells, and to monitor the effect of the mutations on the dose-response curve for translocation induced by phorbol 12-myristate 13-acetate. The introduced mutations change into glycine the consensus proline in the phorbol ester binding loop of the zinc finger; in the isolated zinc finger, this mutation causes a 125-fold decrease in phorbol ester binding affinity. We observed that mutation in the first zinc finger caused almost no shift in the dose-response curve for translocation; mutation in the second zinc finger caused a 21-fold shift, whereas mutation in both zinc fingers caused a 138-fold shift. We conclude that the zinc fingers in the intact PKC are not equivalent and that the second zinc finger plays the predominant role in translocation of protein kinase C? in response to phorbol 12-myristate 13-acetate. Our findings have important implications for the understanding and design of PKC inhibitors targeted to the zinc finger domains.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein kinase C
PKC zinc fingers
Megjelenés:Journal Of Biological Chemistry. - 271 : 31 (1996), p. 18299-18301. -
További szerzők:Bogi, K. Gohari, S. Bíró Tamás (1968-) (élettanász) Ács Péter Blumberg, Peter M.
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Intézményi repozitóriumban (DEA) tárolt változat
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