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Article ; Online: Connexin-36 distribution and layer-specific topography in the cat retina.

Telkes, Ildikó / Kóbor, Péter / Orbán, József / Kovács-Öller, Tamás / Völgyi, Béla / Buzás, Péter

2019 Volume 224, Issue 6, Page(s) 2183–2197

Abstract: Connexin-36 (Cx36) is the major constituent of mammalian retinal gap junctions positioned in key signal pathways. Here, we examined the laminar and large-scale topographical distribution of Cx36 punctate immunolabels in the retina of the cat, a classical ...

Abstract	Connexin-36 (Cx36) is the major constituent of mammalian retinal gap junctions positioned in key signal pathways. Here, we examined the laminar and large-scale topographical distribution of Cx36 punctate immunolabels in the retina of the cat, a classical model of the mammalian visual system. Calretinin-immunoreactive (CaR-IR) cell populations served to outline the nuclear and plexiform layers and to stain specific neuronal populations. CaR-IR cells included horizontal cells in the outer retina, numerous amacrine cells, and scattered cells in the ganglion cell layer. Cx36-IR plaques were found among horizontal cell dendrites albeit without systematic colocalization of the two labels. Diffuse Cx36 immunoreactivity was found in the cytoplasm of AII amacrine cells, but no colocalization of Cx36 plaques was observed with either the perikarya or the long varicose dendrites of the CaR-IR non-AII amacrine cells. Cx36 puncta were seen throughout the entire inner plexiform layer showing their highest density in the ON sublamina. The densities of AII amacrine cell bodies and Cx36 plaques in the ON sublamina were strongly correlated across a wide range of eccentricities suggesting their anatomical association. However, the high number of plaques per AII cell suggests that a considerable fraction of Cx36 gap junctions in the ON sublamina is formed by other cell types than AII amacrine cells drawing attention to extensive but less studied electrically coupled networks.
MeSH term(s)	Amacrine Cells/metabolism ; Animals ; Calbindin 2/metabolism ; Cats ; Connexins/metabolism ; Dendrites/metabolism ; Gap Junctions/metabolism ; Immunohistochemistry/methods ; Retina/metabolism ; Retinal Rod Photoreceptor Cells/metabolism ; Visual Pathways/physiology ; Gap Junction delta-2 Protein
Chemical Substances	Calbindin 2 ; Connexins
Language	English
Publishing date	2019-06-06
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2273162-3
ISSN	1863-2661 ; 1863-2653
ISSN (online)	1863-2661
ISSN	1863-2653
DOI	10.1007/s00429-019-01876-y
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Article: FASCIN and alpha-actinin can regulate the conformation of actin filaments.

Türmer, Katalin / Orbán, József / Gróf, Pál / Nyitrai, Miklós

Biochimica et biophysica acta

2015 Volume 1850, Issue 9, Page(s) 1855–1861

Abstract: Background: Actin filament bundling proteins mediate numerous processes in cells such as the formation of cell membrane protrusions or cell adhesions and stress fiber based locomotion. Among them alpha-actinin and fascin are the most abundant ones. This ...

Abstract	Background: Actin filament bundling proteins mediate numerous processes in cells such as the formation of cell membrane protrusions or cell adhesions and stress fiber based locomotion. Among them alpha-actinin and fascin are the most abundant ones. This work characterizes differences in molecular motions in actin filaments due to the binding of these two actin bundling proteins. Methods: We investigated how alpha-actinin and fascin binding modify the conformation of actin filaments by using conventional and saturation transfer EPR methods. Results: The result characteristic for motions on the microsecond time scale showed that both actin bundling proteins made the bending and torsional twisting of the actin filaments slower. When nanosecond time scale molecular motions were described the two proteins were found to induce opposite changes in the actin filaments. The binding of one molecule of alpha-actinin or fascin modified the conformation of numerous actin protomers. Conclusion: As fascin and alpha-actinin participates in different cellular processes their binding can serve the proper tuning of the structure of actin by establishing the right conformation for the interactions with other actin binding proteins. Our observations are in correlation with the model where actin filaments fulfill their biological functions under the regulation by actin-binding proteins. General significance: Supporting the general model for the cellular regulation of the actin cytoskeleton we showed that two abundant actin bundling proteins, fascin and alpha-actinin, alter the conformation of actin filaments through long range allosteric interactions in two different ways providing the structural framework for the adaptation to specific biological functions.
MeSH term(s)	Actin Cytoskeleton/chemistry ; Actinin/metabolism ; Carrier Proteins/metabolism ; Electron Spin Resonance Spectroscopy ; Microfilament Proteins/metabolism ; Molecular Conformation
Chemical Substances	Carrier Proteins ; Microfilament Proteins ; Actinin (11003-00-2) ; fascin (146808-54-0)
Language	English
Publishing date	2015-09
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2015.05.018
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Article ; Online: O

Fisi, Viktória / Kátai, Emese / Orbán, József / Dossena, Silvia / Miseta, Attila / Nagy, Tamás

Molecules (Basel, Switzerland)

2018 Volume 23, Issue 6

Abstract: ... ...

Abstract	O
MeSH term(s)	Acetylglucosamine/metabolism ; Cell Cycle ; Glycosylation ; HeLa Cells ; Humans ; Mitosis ; Nuclear Pore Complex Proteins/metabolism ; Protein Processing, Post-Translational ; Thymidine/metabolism
Chemical Substances	Nuclear Pore Complex Proteins ; Acetylglucosamine (V956696549) ; Thymidine (VC2W18DGKR)
Language	English
Publishing date	2018-05-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules23061275
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Article: Developmental changes in the expression level of connexin36 in the rat retina

Kovács-Öller, Tamás / Raics, Katalin / Orbán, József / Nyitrai, Miklós / Völgyi, Béla

Cell and tissue research. 2014 Nov., v. 358, no. 2

2014

Abstract: Connexin36 (Cx36) is the major gap junction forming protein in the brain and the retina; thus, alterations in its expression indicate changes in the corresponding circuitry. Many structural changes occur in the early postnatal retina before functional ... ...

Abstract	Connexin36 (Cx36) is the major gap junction forming protein in the brain and the retina; thus, alterations in its expression indicate changes in the corresponding circuitry. Many structural changes occur in the early postnatal retina before functional neuronal circuits are finalized, including those that incorporate gap junctions. To reveal the time-lapse formation of inner retinal gap junctions, we examine the developing postnatal rat retina from birth (P₀) to young adult age (P₂₀) and follow the expression of Cx36 in the mRNA and protein levels. We found a continuous elevation in the expression of both the Cx36 transcript and protein between P₀ and P₂₀ and a somewhat delayed Cx36 plaque formation throughout the inner plexiform layer (IPL) starting at P₁₀. By using tristratificated calretinin positive (CaR⁺) fibers in the IPL as a guide, we detected a clear preference of Cx36 plaques for the ON sublamina from the earliest time of detection. This distributional preference became more pronounced at P₁₅ and P₂₀ due to the emergence and widespread expression of large (>0.1 μm²) Cx36 plaques in the ON sublamina. Finally, we showed that parvalbumin-positive (PV⁺) AII amacrine cell dendrites colocalize with Cx36 plaques as early as P₁₀ in strata 3 and 4, whereas colocalizations in stratum 5 became characteristic only around P₂₀. We conclude that Cx36 expression in the rat IPL displays a characteristic succession of changes during retinogenesis reflecting the formation of the underlying electrical synaptic circuitry. In particular, AII cell gap junctions, first formed with ON cone bipolar cells and later with other AII amacrine cells, accounted for the observed Cx36 expressional changes.
Keywords	adults ; brain ; dendrites ; gap junctions ; messenger RNA ; rats ; retina
Language	English
Dates of publication	2014-11
Size	p. 289-302.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	125067-x
ISSN	1432-0878 ; 0302-766X
ISSN (online)	1432-0878
ISSN	0302-766X
DOI	10.1007/s00441-014-1967-9
Database	NAL-Catalogue (AGRICOLA)

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Article: Connexin36 Expression in the Mammalian Retina: A Multiple-Species Comparison.

Kovács-Öller, Tamás / Debertin, Gábor / Balogh, Márton / Ganczer, Alma / Orbán, József / Nyitrai, Miklós / Balogh, Lajos / Kántor, Orsolya / Völgyi, Béla

Frontiers in cellular neuroscience

2017 Volume 11, Page(s) 65

Abstract: Much knowledge about interconnection of human retinal neurons is inferred from results on animal models. Likewise, there is a lack of information on human retinal electrical synapses/gap junctions (GJ). Connexin36 (Cx36) forms GJs in both the inner and ... ...

Abstract	Much knowledge about interconnection of human retinal neurons is inferred from results on animal models. Likewise, there is a lack of information on human retinal electrical synapses/gap junctions (GJ). Connexin36 (Cx36) forms GJs in both the inner and outer plexiform layers (IPL and OPL) in most species including humans. However, a comparison of Cx36 GJ distribution in retinas of humans and popular animal models has not been presented. To this end a multiple-species comparison was performed in retinas of 12 mammals including humans to survey the Cx36 distribution. Areas of retinal specializations were avoided (e.g., fovea, visual streak, area centralis), thus observed Cx36 distribution differences were not attributed to these species-specific architecture of central retinal areas. Cx36 was expressed in both synaptic layers in all examined retinas. Cx36 plaques displayed an inhomogenous IPL distribution favoring the ON sublamina, however, this feature was more pronounced in the human, swine and guinea pig while it was less obvious in the rabbit, squirrel monkey, and ferret retinas. In contrast to the relative conservative Cx36 distribution in the IPL, the labels in the OPL varied considerably among mammals. In general, OPL plaques were rare and rather small in rod dominant carnivores and rodents, whereas the human and the cone rich guinea pig retinas displayed robust Cx36 labels. This survey presented that the human retina displayed two characteristic features, a pronounced ON dominance of Cx36 plaques in the IPL and prevalent Cx36 plaque conglomerates in the OPL. While many species showed either of these features, only the guinea pig retina shared both. The observed similarities and subtle differences in Cx36 plaque distribution across mammals do not correspond to evolutionary distances but may reflect accomodation to lifestyles of examined species.
Language	English
Publishing date	2017-03-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2017.00065
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Book: Katolikus papok békemozgalma Magyarországon 1950 - 1956

Orbán, József Gyula

(METEM könyvek ; 33)

2001

Author's details	Orbán József Gyula
Series title	METEM könyvek ; 33
Language	Hungarian
Size	307 S
Publisher	Magyar Egyháztörténeti Enciklopédia Munkaközösség
Publishing place	Budapest
Document type	Book
Note	Die Friedensbewegung katholischer Geistlicher in Ungarn 1950 - 1956
ISBN	9638472510 ; 9789638472519
Database	Former special subject collection: coastal and deep sea fishing

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Article ; Online: Developmental changes in the expression level of connexin36 in the rat retina.

Kovács-Öller, Tamás / Raics, Katalin / Orbán, József / Nyitrai, Miklós / Völgyi, Béla

Cell and tissue research

2014 Volume 358, Issue 2, Page(s) 289–302

Abstract	Connexin36 (Cx36) is the major gap junction forming protein in the brain and the retina; thus, alterations in its expression indicate changes in the corresponding circuitry. Many structural changes occur in the early postnatal retina before functional neuronal circuits are finalized, including those that incorporate gap junctions. To reveal the time-lapse formation of inner retinal gap junctions, we examine the developing postnatal rat retina from birth (P0) to young adult age (P20) and follow the expression of Cx36 in the mRNA and protein levels. We found a continuous elevation in the expression of both the Cx36 transcript and protein between P0 and P20 and a somewhat delayed Cx36 plaque formation throughout the inner plexiform layer (IPL) starting at P10. By using tristratificated calretinin positive (CaR(+)) fibers in the IPL as a guide, we detected a clear preference of Cx36 plaques for the ON sublamina from the earliest time of detection. This distributional preference became more pronounced at P15 and P20 due to the emergence and widespread expression of large (>0.1 μm(2)) Cx36 plaques in the ON sublamina. Finally, we showed that parvalbumin-positive (PV(+)) AII amacrine cell dendrites colocalize with Cx36 plaques as early as P10 in strata 3 and 4, whereas colocalizations in stratum 5 became characteristic only around P20. We conclude that Cx36 expression in the rat IPL displays a characteristic succession of changes during retinogenesis reflecting the formation of the underlying electrical synaptic circuitry. In particular, AII cell gap junctions, first formed with ON cone bipolar cells and later with other AII amacrine cells, accounted for the observed Cx36 expressional changes.
MeSH term(s)	Amacrine Cells/cytology ; Amacrine Cells/metabolism ; Animals ; Animals, Newborn ; Connexins/genetics ; Connexins/metabolism ; Gap Junctions/metabolism ; Gene Expression Regulation, Developmental ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rats, Wistar ; Retina/growth & development ; Retina/metabolism ; Gap Junction delta-2 Protein
Chemical Substances	Connexins ; RNA, Messenger
Language	English
Publishing date	2014-08-12
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	125067-x
ISSN	1432-0878 ; 0302-766X
ISSN (online)	1432-0878
ISSN	0302-766X
DOI	10.1007/s00441-014-1967-9
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Article ; Online: Functional dynamics of a single tryptophan residue in a BLUF protein revealed by fluorescence spectroscopy.

Karadi, Kristof / Kapetanaki, Sofia M / Raics, Katalin / Pecsi, Ildiko / Kapronczai, Robert / Fekete, Zsuzsanna / Iuliano, James N / Collado, Jinnette Tolentino / Gil, Agnieszka A / Orban, Jozsef / Nyitrai, Miklos / Greetham, Greg M / Vos, Marten H / Tonge, Peter J / Meech, Stephen R / Lukacs, Andras

Scientific reports

2020 Volume 10, Issue 1, Page(s) 2061

Abstract: Blue Light Using Flavin (BLUF) domains are increasingly being adopted for use in optogenetic constructs. Despite this, much remains to be resolved on the mechanism of their activation. The advent of unnatural amino acid mutagenesis opens up a new toolbox ...

Abstract	Blue Light Using Flavin (BLUF) domains are increasingly being adopted for use in optogenetic constructs. Despite this, much remains to be resolved on the mechanism of their activation. The advent of unnatural amino acid mutagenesis opens up a new toolbox for the study of protein structural dynamics. The tryptophan analogue, 7-aza-Trp (7AW) was incorporated in the BLUF domain of the Activation of Photopigment and pucA (AppA) photoreceptor in order to investigate the functional dynamics of the crucial W104 residue during photoactivation of the protein. The 7-aza modification to Trp makes selective excitation possible using 310 nm excitation and 380 nm emission, separating the signals of interest from other Trp and Tyr residues. We used Förster energy transfer (FRET) between 7AW and the flavin to estimate the distance between Trp and flavin in both the light- and dark-adapted states in solution. Nanosecond fluorescence anisotropy decay and picosecond fluorescence lifetime measurements for the flavin revealed a rather dynamic picture for the tryptophan residue. In the dark-adapted state, the major population of W104 is pointing away from the flavin and can move freely, in contrast to previous results reported in the literature. Upon blue-light excitation, the dominant tryptophan population is reorganized, moves closer to the flavin occupying a rigidly bound state participating in the hydrogen-bond network around the flavin molecule.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Bacterial Proteins/radiation effects ; Flavins/chemistry ; Flavins/metabolism ; Flavins/radiation effects ; Flavoproteins/chemistry ; Flavoproteins/metabolism ; Flavoproteins/radiation effects ; Fluorescence Resonance Energy Transfer ; Hydrogen Bonding/radiation effects ; Light ; Molecular Conformation ; Molecular Dynamics Simulation ; Photoreceptors, Microbial/chemistry ; Photoreceptors, Microbial/metabolism ; Photoreceptors, Microbial/radiation effects ; Tryptophan/analogs & derivatives ; Tryptophan/chemistry ; Tryptophan/metabolism ; Tryptophan/radiation effects
Chemical Substances	AppA protein, Rhodobacter sphaeroides ; Bacterial Proteins ; Flavins ; Flavoproteins ; Photoreceptors, Microbial ; 7-azatryptophan (1137-00-4) ; Tryptophan (8DUH1N11BX)
Language	English
Publishing date	2020-02-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-59073-5
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Article: Noncooperative stabilization effect of phalloidin on ADP.BeFx- and ADP.AlF4-actin filaments.

Orbán, József / Lorinczy, Dénes / Hild, Gábor / Nyitrai, Miklós

Biochemistry

2008 Volume 47, Issue 15, Page(s) 4530–4534

Abstract: Actin plays important roles in eukaryotic cell motility. During actin polymerization, the actin-bound ATP is hydrolyzed to ADP and P i. We carried out differential scanning calorimetry experiments to characterize the cooperativity of the stabilizing ... ...

Abstract	Actin plays important roles in eukaryotic cell motility. During actin polymerization, the actin-bound ATP is hydrolyzed to ADP and P i. We carried out differential scanning calorimetry experiments to characterize the cooperativity of the stabilizing effect of phalloidin on actin filaments in their ADP.P i state. The ADP.P i state was mimicked by using ADP.BeF x or ADP.AlF 4. The results showed that the binding of the nucleotide analogues or phalloidin stabilized the actin filaments to a similar extent when added separately. Phalloidin binding to ADP.BeF x- or ADP.AlF 4-actin filaments further stabilized them, indicating that the mechanism by which phalloidin and the nucleotide analogues affect the filament structure was different. The results also showed that the stabilization effect of phalloidin binding to ADP.BeF x or ADP.AlF 4-bound actin filaments was not cooperative. Since the effect of phalloidin binding was cooperative in the absence of these nucleotide analogues, these results suggest that the binding of ADP.BeF x or ADP.AlF 4 to the actin modified the protomer-protomer interactions along the actin filaments.
MeSH term(s)	Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/drug effects ; Adenosine Diphosphate/analogs & derivatives ; Adenosine Diphosphate/chemistry ; Beryllium/chemistry ; Calorimetry, Differential Scanning ; Fluorides/chemistry ; Organometallic Compounds/chemistry ; Phalloidine/pharmacology
Chemical Substances	Organometallic Compounds ; adenosine diphosphate tetrafluoroaluminate ; Phalloidine (17466-45-4) ; beryllium fluoride (499FU9DQ5C) ; Adenosine Diphosphate (61D2G4IYVH) ; Beryllium (OW5102UV6N) ; Fluorides (Q80VPU408O)
Language	English
Publishing date	2008-03-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi800068e
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Article ; Online: Nucleotide dependent differences between the alpha-skeletal and alpha-cardiac actin isoforms.

Orbán, József / Lorinczy, Dénes / Nyitrai, Miklós / Hild, Gábor

Biochemical and biophysical research communications

2008 Volume 368, Issue 3, Page(s) 696–702

Abstract: The thermodynamic properties of the actin filaments prepared from cardiomyocytes were investigated with differential scanning calorimetry. This method could distinguish between the alpha-cardiac and alpha-skeletal components of the actin filaments ... ...

Abstract	The thermodynamic properties of the actin filaments prepared from cardiomyocytes were investigated with differential scanning calorimetry. This method could distinguish between the alpha-cardiac and alpha-skeletal components of the actin filaments polymerised from ADP-actin monomers by their different melting temperatures (T(m)). Similar separation was not possible with filaments polymerised from ATP-actin monomers. Further analyses revealed that the activation energy (E(act)) was greater for filaments of alpha-skeletal actin than for alpha-cardiac actin monomers when the filaments were polymerised from ADP-actin monomers. These results showed that the alpha-cardiac actin filaments were thermodynamically less stable than the filaments of alpha-skeletal actin and their difference was nucleotide dependent. Based on these results and considering previous observations it was concluded that the existence of two actin isoforms and their nucleotide dependent conformational differences are part of the tuning regulatory mechanism by which the cardiac muscle cells can maintain their biological function under pathological conditions.
MeSH term(s)	Actin Cytoskeleton/chemistry ; Actin Cytoskeleton/ultrastructure ; Actins/chemistry ; Actins/ultrastructure ; Animals ; Cattle ; Cells, Cultured ; Computer Simulation ; Models, Chemical ; Models, Molecular ; Muscle Fibers, Skeletal/metabolism ; Myocytes, Cardiac/metabolism ; Nucleotides/chemistry ; Protein Conformation ; Protein Isoforms/chemistry ; Protein Isoforms/ultrastructure ; Structure-Activity Relationship
Chemical Substances	Actins ; Nucleotides ; Protein Isoforms
Language	English
Publishing date	2008-02-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2008.01.158
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