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1.

001-es BibID:BIBFORM091525
035-os BibID:(scopus)85100002242 (wos)000612002300001
Első szerző:Alvarado, Diana
Cím:A Novel Insecticidal Spider Peptide that Affects the Mammalian Voltage-Gated Ion Channel hKv1.5 / Diana Alvarado, Samuel Cardoso-Arenas, Ligia-Luz Corrales-García, Herlinda Clement, Iván Arenas, Pavel Andrei Montero-Dominguez, Timoteo Olamendi-Portugal, Fernando Zamudio, Agota Csoti, Jesús Borrego, Gyorgy Panyi, Ferenc Papp, Gerardo Corzo
Dátum:2021
ISSN:1663-9812
Megjegyzések:Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, even for mammal species. In this work, thirty animal venoms were screened against hKv1.5, a potential target for atrial fibrillation therapy. The whole venom of the spider Oculicosa supermirabilis, which is also insecticidal to house crickets, caused voltage-gated potassium ion channel modulation in hKv1.5. Therefore, a peptide from the spider O. supermirabilis venom, named Osu1, was identified through HPLC reverse-phase fractionation. Osu1 displayed similar biological properties as the whole venom; so, the primary sequence of Osu1 was elucidated by both of N-terminal degradation and endoproteolytic cleavage. Based on its primary structure, a gene that codifies for Osu1 was constructed de novo from protein to DNA by reverse translation. A recombinant Osu1 was expressed using a pQE30 vector inside the E. coli SHuffle expression system. recombinant Osu1 had voltage-gated potassium ion channel modulation of human hKv1.5, and it was also as insecticidal as the native toxin. Due to its novel primary structure, and hypothesized disulfide pairing motif, Osu1 may represent a new family of spider toxins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
atrial fibrillation
Kv1.5
Oculicosa supermirabilis
recombinant expression
spider venom
Megjelenés:Frontiers in Pharmacology. - 11 (2021), p. 1-13. -
További szerzők:Cardoso-Arenas, Samuel Corrales-García, Ligia-Luz Clement, Herlinda Arénas Iván Montero-Dominguez, Pavel Andrei Olamendi-Portugal, Timoteo Zamudio, Fernando Z. Csóti Ágota (1989-) (biológus) Borrego, Jesús Panyi György (1966-) (biofizikus) Papp Ferenc (1979-) (biofizikus) Corzo, Gerardo
Pályázati támogatás:K119417
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
GINOP-2.3.2-15-2016-00015
GINOP
University of Debrecen, Faculty of Medicine, Bridging Fund
Egyéb
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2.

001-es BibID:BIBFORM095264
035-os BibID:(scopus)85107216771 (wos)000655485500001
Első szerző:Bene Zsolt (orvos)
Cím:Enhanced Expression of Human Epididymis Protein 4 (HE4) Reflecting Pro-Inflammatory Status Is Regulated by CFTR in Cystic Fibrosis Bronchial Epithelial Cells / Zsolt Bene, Zsolt Fejes, Tibor Gabor Szanto, Ferenc Fenyvesi, Judit Váradi, Luka A. Clarke, Gyorgy Panyi, Milan Macek Jr., Margarida D. Amaral, István Balogh, Béla Nagy Jr.
Dátum:2021
ISSN:1663-9812
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Frontiers in Pharmacology. - 12 (2021), p. 1-16. -
További szerzők:Fejes Zsolt (1988-) (molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) Fenyvesi Ferenc (1977-) (gyógyszerész, gyógyszertechnológus) Váradi Judit (1973-) (gyógyszerész, gyógyszertechnológus) Clarke, Luka A. Panyi György (1966-) (biofizikus) Macek Jr., Milan Amaral, Margarida D. Balogh István (1972-) (molekuláris biológus, genetikus) Nagy Béla Jr. (1980-) (labordiagnosztikai szakorvos)
Pályázati támogatás:OTKA FK 135327
OTKA
GINOP-2.3.2-15-2016-00043
GINOP
Internet cím:Szerző által megadott URL
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3.

001-es BibID:BIBFORM120201
Első szerző:Cozzolino, Marco (biológus)
Cím:Intracellular acidity impedes KCa3.1 activation by Riluzole and SKA-31 / Cozzolino Marco, Panyi Gyorgy
Dátum:2024
ISSN:1663-9812
Megjegyzések:Based on our data we conclude that KCa3.1 currents are not sensitive the either the intracellular or the extracellular pH in the physiological and pathophysiological range. However, intracellular acidosis in T cells residing in the tumor microenvironment could hinder the potentiating effect of KCa3.1 positive modulators administered to boost their activity. Further research is warranted both to clarify the molecular interactions between the modulators and KCa3.1 at different intracellular pH conditions and to define whether this loss of potency can be observed in cancer models as well.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
ion channels
KCa3.1
Riluzole
SKA-31
acidity
cancer
Megjelenés:Frontiers in Pharmacology. - 15 (2024), p. 1-23. -
További szerzők:Panyi György (1966-) (biofizikus)
Pályázati támogatás:K119417
OTKA
813834-pHioniC-H2020-MSCA-ITN-2018
Egyéb
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4.

001-es BibID:BIBFORM091510
035-os BibID:(cikkazonosító)586599 (scopus)85102899354 (wos)000615362700001
Első szerző:Hofschröer, Verena
Cím:Ion Channels Orchestrate Pancreatic Ductal Adenocarcinoma Progression and Therapy / Hofschröer Verena, Najder Karolina, Rugi Micol, Bouazzi Rayhana, Cozzolino Marco, Arcangeli Annarosa, Panyi Gyorgy, Schwab Albrecht
Dátum:2021
ISSN:1663-9812
Megjegyzések:Pancreatic ductal adenocarcinoma is a devastating disease with a dismal prognosis. Therapeutic interventions are largely ineffective. A better understanding of the pathophysiology is required. Ion channels contribute substantially to the "hallmarks of cancer." Their expression is dysregulated in cancer, and they are "misused" to drive cancer progression, but the underlying mechanisms are unclear. Ion channels are located in the cell membrane at the interface between the intracellular and extracellular space. They sense and modify the tumor microenvironment which in itself is a driver of PDAC aggressiveness. Ion channels detect, for example, locally altered proton and electrolyte concentrations or mechanical stimuli and transduce signals triggered by these microenvironmental cues through association with intracellular signaling cascades. While these concepts have been firmly established for other cancers, evidence has emerged only recently that ion channels are drivers of PDAC aggressiveness. Particularly, they appear to contribute to two of the characteristic PDAC features: the massive fibrosis of the tumor stroma (desmoplasia) and the efficient immune evasion. Our critical review of the literature clearly shows that there is still a remarkable lack of knowledge with respect to the contribution of ion channels to these two typical PDAC properties. Yet, we can draw parallels from ion channel research in other fibrotic and inflammatory diseases. Evidence is accumulating that pancreatic stellate cells express the same "profibrotic" ion channels. Similarly, it is at least in part known which major ion channels are expressed in those innate and adaptive immune cells that populate the PDAC microenvironment. We explore potential therapeutic avenues derived thereof. Since drugs targeting PDAC-relevant ion channels are already in clinical use, we propose to repurpose those in PDAC. The quest for ion channel targets is both motivated and complicated by the fact that some of the relevant channels, for example, KCa3.1, are functionally expressed in the cancer, stroma, and immune cells. Only in vivo studies will reveal which arm of the balance we should put our weights on when developing channeltargeting PDAC therapies. The time is up to explore the efficacy of ion channel targeting in (transgenic) murine PDAC models before launching clinical trials with repurposed drugs
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
pancreatic ductal adenocarcinoma
ion channels
therapy
immune cells
fibrosis
Megjelenés:Frontiers in Pharmacology. - 11 (2021), p. 1-28. -
További szerzők:Najder, Karolina Rugi, Micol Bouazzi, Rayhana Cozzolino, Marco (1991-) (biológus) Arcangeli, Annarosa Panyi György (1966-) (biofizikus) Schwab, Albrecht
Pályázati támogatás:Marie Skodowska-Curie Innovative Training Network (ITN) - 813834 - pHioniC - H2020-MSCA-ITN-2018
Egyéb
K119417
OTKA
EFOP-3.6.2-16-2017-00006
EFOP
GINOP-2.3.2-15-2016-00015
GINOP
AIRC, Grant N? IG 15627 and IG 21510 to AA, PRIN Italian Ministry of University and Research (MIUR)
Egyéb
LIONESS 20174TB8KW
Egyéb
DFG; SCHW 407/17-1 & SCHW 407/22-1; GRK 2515/1, Chembion
Egyéb
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5.

001-es BibID:BIBFORM098765
035-os BibID:(cikkazonosító)733610 (scopus)85117131062 (wos)000707249000001
Első szerző:Naseem, Muhammad Umair (biofizikus, molekuláris biológus)
Cím:Optimization of Pichia pastoris Expression System for High-Level Production of Margatoxin / Naseem Muhammad Umair, Tajti Gabor, Gaspar Attila, Szanto Tibor G., Borrego Jesús, Panyi Gyorgy
Dátum:2021
ISSN:1663-9812
Megjegyzések:Margatoxin (MgTx) is a high-affinity blocker of voltage-gated potassium (Kv) channels. It inhibits Kv1.1?Kv1.3 ion channels in picomolar concentrations. This toxin is widely used to study physiological function of Kv ion channels in various cell types, including immune cells. Isolation of native MgTx in large quantities from scorpion venom is not affordable. Chemical synthesis and recombinant production in Escherichia coli need in vitro oxidative refolding for proper disulfide bond formation, resulting in a very low yield of peptide production. The Pichia pastoris expression system offers an economical approach to overcome all these limitations and gives a higher yield of correctly refolded recombinant peptides. In this study, improved heterologous expression of recombinant MgTx (rMgTx) in P. pastoris was obtained by using preferential codons, selecting the hyper-resistant clone against Zeocin, and optimizing the culturing conditions. About 36 ? 4 mg/L of >98% pure His-tagged rMgTx (TrMgTx) was produced, which is a threefold higher yield than has been previously reported. Proteolytic digestion of TrMgTx with factor Xa generated untagged rMgTx (UrMgTx). Both TrMgTx and UrMgTx blocked the Kv1.2 and Kv1.3 currents (patch-clamp) (Kd for Kv1.2 were 64 and 14 pM, and for Kv1.3, 86 and 50 pM, respectively) with comparable potency to the native MgTx. The analysis of the binding kinetics showed that TrMgTx had a lower association rate than UrMgTx for both Kv1.2 and Kv1.3. The dissociation rate of both the analogues was the same for Kv1.3. However, in the case of Kv1.2, TrMgTx showed a much higher dissociation rate with full recovery of the block than UrMgTx. Moreover, in a biological functional assay, both peptides significantly downregulated the expression of early activation markers IL2R and CD40L in activated CD4+ TEM lymphocytes whose activation was Kv1.3 dependent. In conclusion, the authors report that the Pichia expression system is a powerful method to produce disulfide-rich peptides, the overexpression of which could be enhanced noticeably through optimization strategies, making it more cost-effective. Since the presence of the His-tag on rMgTx only mildly altered the block equilibrium and binding kinetics, recombinant toxins could be used in ion channel research without removing the tag and could thus reduce the cost and time demand for toxin production.
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Pichia pastoris
patch-clamp
margatoxin
recombinant expression
Kv1.3 blocker
CD4+ TEM cells
Megjelenés:Frontiers in Pharmacology. - 12 (2021), p. 1-18. -
További szerzők:Tajti Gábor (1988-) (gyógyszerész, biofizikus, sejtbiológus) Gáspár Attila (1970-) (vegyész, kémikus) Szántó Gábor Tibor (1980-) (vegyész) Borrego, Jesús Panyi György (1966-) (biofizikus)
Pályázati támogatás:K119417
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
GINOP2.3.2-15-2016-00044
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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