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1.

001-es BibID:BIBFORM080582
Első szerző:Bai Péter (biokémikus)
Cím:ADP-ribosylation inhibitors in treatment of diseases / Bai Peter, Palmiro Poltronieri, Mariella Di Girolamo
Dátum:2019
ISSN:0006-2952
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biochemical Pharmacology. - 167 (2019), p. 1-2. -
További szerzők:Poltronieri, Palmiro Di Girolamo, Mariella
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM005176
Első szerző:Corzo, Gerardo
Cím:A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venomof the scorpion Centruroides suffusus suffusus / Corzo G., Papp F., Varga Z., Barraza O., Espino-Solis P. G., Rodríguez de la Vega R. C., Gaspar R., Panyi G., Possani L. D.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Kv1.3 Potassium Channel
Potassium
Potassium Channels
Megjelenés:Biochemical Pharmacology 76 : 9 (2008), p. 1142-1154. -
További szerzők:Papp Ferenc (1979-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Barraza, Omar Espino-Solis, Pavel G. Rodriguez de la Vega, Ricardo C. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:

3.

001-es BibID:BIBFORM102212
035-os BibID:(cikkazonosító)115023 (WoS)000793623600002 (Scopus)85127510848
Első szerző:Csóti Ágota (biológus)
Cím:sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity / Csoti Agota, del Carmen Nájera Meza Rosby, Bogár Ferenc, Tajti Gabor, Szanto Tibor G., Varga Zoltan, Gurrola Georgina B., Tóth Gábor K., Possani Lourival D., Panyi Gyorgy
Dátum:2022
ISSN:0006-2952
Megjegyzések:Kv1.3 K+ channels play a central role in the regulation of T cell activation and Ca2+ signaling under physiological and pathophysiological conditions. Peptide toxins targeting Kv1.3 have a significant therapeutic potential in the treatment of autoimmune diseases; thus, the discovery of new toxins is highly motivated. Based on the transcriptome analysis of the venom gland of V. mexicanus smithi a novel synthetic peptide, sVmKTx was generated, containing 36 amino acid residues. sVmKTx shows high sequence similarity to Vm24, a previously characterized peptide from the same species, but contains a Glu at position 32 as opposed to Lys32 in Vm24. Vm24 inhibits Kv1.3 with high affinity (Kd = 2.9 pM). However, it has limited selectivity (~1,500-fold) for Kv1.3 over hKv1.2, hKCa3.1, and mKv1.1. sVmKTx displays reduced Kv1.3 affinity (Kd = 770 pM) but increased selectivity for Kv1.3 over hKv1.2 (~9,000-fold) as compared to Vm24, other channels tested in the panel (hKCa3.1, hKv1.1, hKv1.4, hKv1.5, rKv2.1, hKv11.1, hKCa1.1, hNav1.5) were practically insensitive to the toxin at 2.5 ?M. Molecular dynamics simulations showed that introduction of a Glu instead of Lys at position 32 led to a decreased structural fluctuation of the N-terminal segment of sVmKTx, which may explain its increased selectivity for Kv1.3. sVmKTx at 100 nM concentration decreased the expression level of the Ca2+ -dependent T cell activation marker, CD40 ligand. The high affinity block of Kv1.3 and increased selectivity over the natural peptide makes sVmKTx a potential candidate for Kv1.3 blockade-mediated treatment of autoimmune diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Kv1.3
Toxin-channel interaction
T-cell activation
Patch-clamp
Ion channel selectivity
Scorpion toxin
Megjelenés:Biochemical Pharmacology. - 199 (2022), p. 1-14. -
További szerzők:del Carmen Nájera Meza, Rosby Bogár Ferenc Tajti Gábor (1988-) (gyógyszerész, biofizikus, sejtbiológus) Szántó Gábor Tibor (1980-) (vegyész) Varga Zoltán (1969-) (biofizikus, szakfordító) Gurrola-Briones, Georgina Tóth Gábor K. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:143071
OTKA
K119417
OTKA
K132906
OTKA
EFOP-3.6.2-16-2017-00006
EFOP
GINOP-2.3.2-15-2016-00044
GINOP
PRONACE303045 from National Conseil of Science and Technology of Mexico
Egyéb
Ministry of Human Capacities, Hungary grant, TKP-2020
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM089428
035-os BibID:(cikkazonosító)114310 (Scopus)85097002422 (WOS)000604265300002 (PubMed)33130130
Első szerző:Kelemen Balázs (biológus)
Cím:The TRPM3 ion channel mediates nociception but not itch evoked by endogenous pruritogenic mediators / Balázs Kelemen, Silvia Pinto, Nawoo Kim, Erika Lisztes, Martin Hanyicska, Anita Vladár, Attila Oláh, Zsófia Pénzes, Brian Shu, Joris Vriens, Tamás Bíró, Tibor Rohács, Thomas Voets, Balázs István Tóth
Dátum:2021
ISSN:0006-2952
Megjegyzések:During the molecular transduction of itch, the stimulation of pruriceptors on sensory fibers leads to the activation or sensitization of ion channels, which results in a consequent depolarization of the neurons. These ion channels mostly belong to the transient receptor potential (TRP) channels, which are involved in nociception and thermosensation. In particular, TRPV1 and TRPA1 were described in the transduction of both thermal nociception as well as histaminergic and non-histaminergic itch. The thermosensitive TRPM3 plays an indispensable role in heat nociception together with TRPV1 and TRPA1. However, the role of TRPM3 in the development of pruritus has not been studied yet. Therefore, in this study we aimed at investigating the potential role of TRPM3 in the transduction of pruritus and pain by investigating itch- and nociception-related behavior of Trpm3+/+ and Trpm3?/? mice, and by studying the activation of somatosensory neurons isolated from trigeminal ganglia upon application of algogenic and pruritogenic substances. Activators of TRPM3 evoked only nocifensive responses, but not itch in Trpm3+/+ animals, and these nocifensive responses were abolished in the Trpm3?/? strain. Histamine and endogenous non-histaminergic pruritogens induced itch in both Trpm3+/+ and Trpm3?/? mice to a similar extent. Genetic deletion or pharmacological blockade diminished TRPM3 mediated Ca2+ responses of sensory neurons, but did not affect responses evoked by pruritogenic substances. Our results demonstrate that, in contrast to other thermosensitive TRP channels, TRPM3 selectively mediates nociception, but not itch sensation, and suggest that TRPM3 is a promising candidate to selectively target pain sensation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Nociception
Itch
TRP channels
TRPM3
Cheek model
Endogenous pruritogens
Megjelenés:Biochemical Pharmacology. - 183 (2021), p. 114310. -
További szerzők:Pinto, Silvia Kim, Nawoo Lisztes Erika (1986-) (élettanász) Hanyicska Martin (1992-) (biotechnológus) Vladár Anita Oláh Attila (1984-) (élettanász) Pénzes Zsófia (1992-) (klinikai laboratóriumi kutató) Shu, Brian Vriens, Joris Bíró Tamás (1968-) (élettanász) Rohács Tibor Voets, Thomas Tóth István Balázs (1978-) (élettanász)
Pályázati támogatás:K_120187
OTKA
PD_121360
OTKA
PD-134791
OTKA
FK_125055
OTKA
GINOP-2.3.2-15-2016-00015
GINOP
EFOP-3.6.3- VEKOP-16-2017-00009
EFOP
EFOP-3.6.1-16-2016-00022
EFOP
ÚNKP-20-5-DE-422
ÚNKP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM083138
035-os BibID:(Scopus)85079239909 (WOS)000527342900032 (cikkazonosító)113826 (PubMed)31987857
Első szerző:Kelemen Balázs (biológus)
Cím:Volatile anaesthetics inhibit the thermosensitive nociceptor ion channel transient receptor potential melastatin 3 (TRPM3) / Balázs Kelemen, Erika Lisztes, Anita Vladár, Martin Hanyicska, János Almássy, Attila Oláh, Attila Gábor Szöllősi, Zsófia Pénzes, János Posta, Thomas Voets, Tamás Bíró, Balázs István Tóth
Dátum:2020
ISSN:0006-2952
Megjegyzések:Background Volatile anaesthetics (VAs) are the most widely used compounds to induce reversible loss of consciousness and maintain general anaesthesia during surgical interventions. Although the mechanism of their action is not yet fully understood, it is generally believed, that VAs depress central nervous system functions mainly through modulation of ion channels in the neuronal membrane, including 2-pore-domain K+ channels, GABA and NMDA receptors. Recent research also reported their action on nociceptive and thermosensitive TRP channels expressed in the peripheral nervous system, including TRPV1, TRPA1, and TRPM8. Here, we investigated the effect of VAs on TRPM3, a less characterized member of the thermosensitive TRP channels playing a central role in noxious heat sensation. Methods We investigated the effect of VAs on the activity of recombinant and native TRPM3, by monitoring changes in the intracellular Ca2+ concentration and measuring TRPM3-mediated transmembrane currents. Results All the investigated VAs (chloroform, halothane, isoflurane, sevoflurane) inhibited both the agonist-induced (pregnenolone sulfate, CIM0216) and heat-activated Ca2+ signals and transmembrane currents in a concentration dependent way in HEK293T cells overexpressing recombinant TRPM3. Among the tested VAs, halothane was the most potent blocker (IC50=0.52?0.05 mM). We also investigated the effect of VAs on native TRPM3 channels expressed in sensory neurons of the dorsal root ganglia. While VAs activated certain sensory neurons independently of TRPM3, they strongly and reversibly inhibited the agonist-induced TRPM3 activity. Conclusions These data provide a better insight into the molecular mechanism beyond the analgesic effect of VAs and propose novel strategies to attenuate TRPM3 dependent nociception.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Volatile anaesthetics
TRP ion channels
TRPM3
Nociception
Thermosensation
Megjelenés:Biochemical Pharmacology. - 174 (2020), p. 113826. -
További szerzők:Lisztes Erika (1986-) (élettanász) Vladár Anita Hanyicska Martin (1992-) (biotechnológus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Oláh Attila (1984-) (élettanász) Szöllősi Attila Gábor (1982-) (élettanász) Pénzes Zsófia (1992-) (klinikai laboratóriumi kutató) Posta János (1964-) (vegyész, toxikológus) Voets, Thomas Bíró Tamás (1968-) (élettanász) Tóth István Balázs (1978-) (élettanász)
Pályázati támogatás:GINOP-2.3.2-15-2016-00050
GINOP
ÚNKP-19-4-DE-287
Egyéb
ÚNKP-19-4-DE-142
Egyéb
ÚNKP-19-3-I-DE-140
Egyéb
ÚNKP-19-4-DE-285
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM036657
Első szerző:Landes, Nico
Cím:Vitamin E activates gene expression via the pregnane X receptor / Landes Nico, Pfluger Paul, Kluth Dirk, Birringer Marc, Rühl Ralph, Böl Gaby-Fleur, Glatt Hansruedi, Brigelius-Flohé Regina
Dátum:2003
ISSN:0006-2952
Megjegyzések:Tocopherols and tocotrienols are metabolized by side chain degradation via initial omega-oxidation and subsequent beta-oxidation. omega-Oxidation is performed by cytochrome P450 (CYP) enzymes which are often regulated by their substrates themselves. Results presented here show that all forms of Vitamin E are able to activate gene expression via the pregnane X receptor (PXR), a nuclear receptor regulating a variety of drug metabolizing enzymes. In HepG2 cells transfected with the human PXR and the chloramphenicol acetyl transferase (CAT) gene linked to two PXR responsive elements, CAT activity was most strongly induced by alpha- and gamma-tocotrienol followed by rifampicin, delta-, alpha- and gamma-tocopherol. The inductive efficacy was concentration-dependent; its specificity was underscored by a lower response when cotransfection with PXR was omitted. Up-regulation of endogenous CYP3A4 and CYP3A5 mRNA was obtained by gamma-tocotrienol, the most potent activator of PXR, with the same efficacy as with rifampicin. This points to a potential interference of individual forms of Vitamin E with the metabolism and efficacy of drugs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Pharmacology. - 65 : 2 (2003), p. 269-273. -
További szerzők:Pfluger, Paul Kluth, Dirk Birringer, Marc Rühl, Ralph (1969-) (vegyész) Böl, Gaby-Fleur Glatt, Hansruedi Brigelius-Flohé, Regina
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM086320
035-os BibID:(cikkazonosító)113782 (WoS)000527342900009 (Scopus)85077711551
Első szerző:Luna-Ramirez, Karen
Cím:Structural basis of the potency and selectivity of Urotoxin, a potent Kv1 blocker from scorpion venom / Karen Luna-Ramirez, Agota Csoti, Jeffrey R. McArthur, Yanni K. Y. Chin, Raveendra Anangi, Rosby del Carmen Najera, Lourival D. Possani, Glenn F. King, Gyorgy Panyi, Haibo Yu, David J. Adams, Rocio K. Finol-Urdaneta
Dátum:2020
ISSN:0006-2952
Megjegyzések:Urotoxin (?-KTx 6), a peptide from venom of the Australian scorpion Urodacus yaschenkoi, is the most potent inhibitor of Kv1.2 described to date (IC = 160 pM). The native peptide also inhibits Kv1.1, Kv1.3 and KCa3.1 with nanomolar affinity but its low abundance in venom precluded further studies of its actions. Here we produced recombinant Urotoxin (rUro) and characterized the molecular determinants of Kv1 channel inhibition. The 3D structure of rUro determined using NMR spectroscopy revealed a canonical cysteine-stabilised ?/? (CS?/?) fold. Functional assessment of rUro using patch-clamp electrophysiology revealed the importance of C-terminal amidation for potency against Kv1.1?1.3 and Kv1.5. Neutralization of the putative pore-blocking K25 residue in rUro by mutation to Ala resulted in a major decrease in rUro potency against all Kv channels tested, without perturbing the toxin's structure. Reciprocal mutations in the pore of Uro-sensitive Kv1.2 and Uro-resistant Kv1.5 channels revealed a direct interaction between Urotoxin and the Kv channel pore. Our experimental work supports postulating a mechanism of action in which occlusion of the permeation pathway by the K25 residue in Urotoxin is the basis of its Kv1 inhibitory activity. Docking analysis was consistent with occlusion of the pore by K25 and the requirement of a small, non-charged amino acid in the Kv1 channel vestibule to facilitate toxin-channel interactions. Finally, computational studies revealed key interactions between the amidated C-terminus of Urotoxin and a conserved Asp residue in the turret of Kv1 channels, offering a potential rationale for potency differences between native and recombinant Urotoxin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biochemical Pharmacology. - 174 (2020), p. 1-15. -
További szerzők:Csóti Ágota (1989-) (biológus) McArthur, Jeffrey R. Chin, Yanni K. Y. Anangi, Raveendra Najera, Rosby del Carmen Possani, Lourival Domingos King, Glenn F. Panyi György (1966-) (biofizikus) Yu, Haibo Adams, David J. Finol-Urdaneta, Rocio K.
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
NKFIH K119417
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM079453
035-os BibID:(PMID)31251940
Első szerző:Nagy Lilla (molekuláris biológus)
Cím:Olaparib induces browning of in vitro cultures of human primary white adipocytes / Lilla Nagy, Boglárka Rauch, Noémi Balla, Gyula Ujlaki, Gréta Kis, Omar Abdul-Rahman, Endre Kristóf, Adrienn Sipos, Miklós Antal, Attila Tóth, Tamás Debreceni, Ambrus Horváth, Tamás Maros, Péter Csizmadia, Tamás Szerafin, Péter Bai
Dátum:2019
ISSN:0006-2952
Megjegyzések:Mitochondrial biogenesis is a key feature of energy expenditure and organismal energy balance. Genetic deletion of PARP1 or PARP2 was shown to induce mitochondrial biogenesis and energy expenditure. In line with that, PARP inhibitors were shown to induce energy expenditure in skeletal muscle. We aimed to investigate whether pharmacological inhibition of PARPs induces brown or beige adipocyte differentiation. SVF fraction of human pericardial adipose tissue was isolated and human adipose-derived mesenchymal stem cells (hADMSCs) were differentiated to white and beige adipocytes. A subset of hADMSCs were differentiated to white adipocytes in the presence of Olaparib, a potent PARP inhibitor currently in clinical use, to induce browning. Olaparib induced morphological changes (smaller lipid droplets) in white adipocytes that is a feature of brown/beige adipocytes. Furthermore, Olaparib induced mitochondrial biogenesis in white adipocytes and enhanced UCP1 expression. We showed that Olaparib treatment inhibited nuclear and cytosolic PAR formation, induced NAD+/NADH ratio and consequently boosted SIRT1 and AMPK activity and the downstream transcriptional program leading to increases in OXPHOS. Olaparib treatment did not induce the expression of beige adipocyte markers in white adipocytes, suggesting the formation of brown or brown-like adipocytes. PARP1, PARP2 and tankyrases are key players in the formation of white adipose tissue. Hereby, we show that PARP inhibition induces the transdifferentiation of white adipocytes to brown-like adipocytes suggesting that PARP activity could be a determinant of the differentiation of these adipocyte lineages.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
ARTD
Adipogenesis
Beige adipocytes
Brown adipose tissue
NAD(+)
Olaparib
PARP
SIRT1
Thermogenesis
White adipocytes
White adipose tissue
Megjelenés:Biochemical Pharmacology. - 167 (2019), p. 76-85. -
További szerzők:Rauch Boglárka (1995-) (molekuláris biológus) Balla Noémi (1998-) (mikrobiológus) Ujlaki Gyula (1991-) (molekuláris biológus) Kis Gréta (1979-) (környezetkutató) Omar, Abdul-Rahman Kristóf Endre (1987-) (általános orvos) Sipos Adrienn (1984-) (biológus, biotechnológus) Antal Miklós (1951-) (orvos, anatómus) Tóth Attila (1971-) (biológus) Debreceni Tamás (1982-) (orvos) Horváth Ambrus (1960-) (szívsebész) Maros Tamás Miklós (1969-) (szívsebész) Csizmadia Péter (1983-) (szívsebész szakorvos) Szerafin Tamás (1960-) (szívsebész, mellkassebész) Bai Péter (1976-) (biokémikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00006
GINOP
GINOP-2.3.2-15-2016-00050
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
NKFIH K123975
NKFIH
NKFIH FK128387
NKFIH
NKFIH PD124110
NKFIH
NKFIH PD116262
NKFIH
ÚNKP-18-4
ÚNKP
Internet cím:Szerző által megadott URL
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Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM031969
Első szerző:Szendrei Levente
Cím:Mitochondrial gene expression and ventricular fibrillation in ischemic/reperfused nondiabetic and diabetic myocardium / Szendrei L., Turoczi T., Kovacs P., Vecsernyes M., Das D. K., Tosaki A.
Dátum:2002
Megjegyzések:We investigated the mitochondrial gene expression related to cardiac function and ventricular fibrillation (VF) in ischemic/reperfused nondiabetic and diabetic myocardium. To identify potentially more specific gene responses we performed subtractive screening, Northern blotting, and reverse transcription-polymerase chain reaction (RT-PCR) of mitochondrial genes expressed after 30 min ischemia followed by 120 min reperfusion in isolated rat hearts that showed VF or did not show VF. Cytochrome oxidase B subunit III (COXBIII) and ATP synthase subunit 6, studied and selected out of 40 mitochondrial genes by subtractive screening, showed an expression after 30 min ischemia (no VF was recorded) in both nondiabetic and diabetic subjects. Upon reperfusion, the down-regulation of these genes was only observed in fibrillated hearts. Such a reduction in signal intensity was not seen in nonfibrillated myocardium. In additional studies, nondiabetic and diabetic hearts, without the ischemia/reperfusion protocol, were subjected to electrical fibrillation, and a significant reduction in COXBIII and ATPS6 mRNA signal intensity was observed indicating that VF contributes to the down-regulation of these genes. Cardiac function (heart rate, coronary flow, aortic flow, left ventricular developed pressure) showed no correlation between the up- and down-regulation of these mitochondrial genes in both nondiabetic and diabetic ischemic/reperfused myocardium. Our data suggest that COXBIII and ATPS6 may play a critical role in arrhythmogenesis, and the stimulation of COXBIII and ATPS6 mRNA expression may prevent the development of VF in both nondiabetic and diabetic ischemic/reperfused myocardium
Tárgyszavak:Orvostudományok Gyógyszerészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Pharmacology. - 63 : 3 (2002), p. 543-552. -
További szerzők:Turóczi Tibor (1976-) (molekuláris biológus) Kovács Péter (1939-) (farmakológus) Vecsernyés Miklós (1959-) (gyógyszertechnológus, endokrinológus) Das, Dipak Kumar Tósaki Árpád (1958-) (kísérletes farmakológus, gyógyszerész)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

10.

001-es BibID:BIBFORM090993
Első szerző:Tajti Gábor (gyógyszerész, biofizikus, sejtbiológus)
Cím:The voltage-gated potassium channel KV1.3 as a therapeutic target for venom-derived peptides / Gábor Tajti, Dorothy C. C. Wai, György Panyi, Raymond S. Norton
Dátum:2020
ISSN:0006-2952
Megjegyzések:The voltage-gated potassium channel KV1.3 is a well-established therapeutic target for a range of autoimmune diseases, in addition to being the site of action of many venom-derived peptides. Numerous studies have documented the efficacy of venom peptides that target KV1.3, in particular from sea anemones and scorpions, in animal models of autoimmune diseases such as rheumatoid arthritis, psoriasis and multiple sclerosis. Moreover, an analogue of the sea anemone peptide ShK (known as dalazatide) has successfully completed Phase 1 clinical trials in mild-to-moderate plaque psoriasis. In this article we consider other potential therapeutic applications of inhibitors of KV1.3, including in inflammatory bowel disease and neuroinflammatory conditions such as Alzheimer's and Parkinson's diseases, as well as fibrotic diseases. We also summarise strategies for facilitating the entry of peptides to the central nervous system, given that this will be a pre-requisite for the treatment of most neuroinflammatory diseases. Venom-derived peptides that have been reported recently to target KV1.3 are also described. The increasing number of autoimmune and other conditions in which KV1.3 is upregulated and is therefore a potential therapeutic target, combined with the fact that many venom-derived peptides are potent inhibitors of KV1.3, suggests that venoms are likely to continue to serve as a rich source of new pharmacological tools and therapeutic leads targeting this channel.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Voltage-gated potassium channel
Peptide
Toxin
Inflammatory bowel disease
Neuroinflammation
Fibrosis
Therapeutic development
Megjelenés:Biochemical Pharmacology. - 181 (2020), p. 114146-. -
További szerzők:Wai, Dorothy C. C. Panyi György (1966-) (biofizikus) Norton, Raymond S.
Pályázati támogatás:EFOP-3.6.2-16-2017-00006
EFOP
GINOP-2.3.2-15-2016-00015
GINOP
NKFIH OTKA K119417
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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