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001-es BibID:	BIBFORM083135
035-os BibID:	(cikkazonosító)68 (scopus)85078993240 (wos)000519243400011
Első szerző:	Bencze János (orvos)
Cím:	Lemur tyrosine kinase 2 (LMTK2) level inversely correlates with phospho-tau in neuropathological stages of Alzheimer's disease / János Bencze, Máté Szarka, Viktor Bencs, Renáta Nóra Szabó, László V. Módis, Dag Aarsland, Tibor Hortobágyi
Dátum:	2020
Megjegyzések:	Alzheimer's disease (AD) is the most common neurodegenerative dementia. Mapping the pathomechanism and providing novel therapeutic options have paramount significance. Recent studies have proposed the role of LMTK2 in AD. However, its expression pattern and association with the pathognomonic neurofibrillary tangles (NFTs) in different brain regions and neuropathological stages of AD is not clear. We performed chromogenic (CHR) LMTK2 and fluorescent phospho-tau/LMTK2 double-labelling (FDL) immunohistochemistry (IHC) on 10-10 post-mortem middle frontal gyrus (MFG) and anterior hippocampus (aHPC) samples with early and late neuropathological Braak tau stages of AD. MFG in early stage was our ♭endogenous control' region as it is not affected by NFTs. Semi-quantitative CHR-IHC intensity scoring revealed significantly higher (p<0.001) LMTK2 values in this group compared to NFT-affected regions. FDL-IHC demonstrated LMTK2 predominance in the endogenous control region, while phospho-tau overburden and decreased LMTK2 immunolabelling were detected in NFT-affected groups (aHPC in early and both regions in late stage). Spearman's correlation coefficient showed strong negative correlation between phospho-tau/LMTK2 signals within each group. According to our results LMTK2 expression is inversely proportionate to the extent of NFT pathology, as well as decreased LMTK2 level is not a general feature in AD brain, rather it is characteristic to the NFT-affected regions.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Alzheimer's disease LMTK2 neurodegeneration tau digital image analysis
Megjelenés:	Brain Sciences. - 10 : 2 (2020), p. 1-14. -
További szerzők:	Szarka Máté (1990-) Bencs Viktor (1995-) (orvos) Szabó Renáta Nóra Módis László V. (neurológus) Aarsland, Dag Hortobágyi Tibor (1965-) (patológus)
Pályázati támogatás:	EFOP-3.6.3-VEKOP-16-2017-00009 EFOP ÚNKP-19-3 Egyéb NAP (2017-1.2.1-NKP-2017-00002) Egyéb GINOP-2.3.2-15-2016-00043 GINOP ÚNKP-19-2 Egyéb
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001-es BibID:	BIBFORM072946
Első szerző:	Bencze János (orvos)
Cím:	Biological function of Lemur tyrosine kinase 2 (LMTK2) : implications in neurodegeneration / János Bencze, Gábor Miklós Mórotz, Woosung Seo, Viktor Bencs, János Kálmán, Christopher Charles John Miller, Tibor Hortobágyi
Dátum:	2018
ISSN:	1756-6606
Megjegyzések:	Neurodegenerative disorders are frequent, incurable diseases characterised by abnormal protein accumulationand progressive neuronal loss. Despite their growing prevalence, the underlying pathomechanism remainsunclear. Lemur tyrosine kinase 2 (LMTK2) is a member of a transmembrane serine/threonine-protein kinase family.Although it was described more than a decade ago, our knowledge on LMTK2's biological functions is still insufficient.Recent evidence has suggested that LMTK2 is implicated in neurodegeneration. After reviewing the literature, weidentified three LMTK2-mediated mechanisms which may contribute to neurodegenerative processes: disrupted axonaltransport, tau hyperphosphorylation and enhanced apoptosis. Moreover, LMTK2 gene expression is decreased in anAlzheimer's disease mouse model. According to these features, LMTK2 might be a promising therapeutic target in nearfuture. However, further investigations are required to clarify the exact biological functions of this unique protein.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Alzheimer's disease Axonal transport LMTK2 Neurodegeneration Tau
Megjelenés:	Molecular Brain. - 11 : 20 (2018), p. 1-9. -
További szerzők:	Mórotz Miklós Gábor Woosung Seo Bencs Viktor (1995-) (orvos) Kálmán János Miller, Christopher Charles John Hortobágyi Tibor (1965-) (patológus)
Pályázati támogatás:	ÚNKP-17-3 ÚNKP EFOP-3.6.3-VEKOP-16-2017-00009 EFOP GINOP-2.3.2-15-2016-00043 GINOP 2017- 1.2.1-NKP-2017-00002 Egyéb
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001-es BibID:	BIBFORM071437
Első szerző:	Bereczki Erika
Cím:	Synaptic markers of cognitive decline in neurodegenerative diseases : a proteomic approach / Erika Bereczki, Rui M. Branca, Paul T. Francis, Joana B. Pereira, Jean-Ha Baek, Tibor Hortobágyi, Bengt Winblad, Clive Ballard, Janne Lehtiö, Dag Aarsland
Dátum:	2017
ISSN:	0006-8950
Megjegyzések:	See Attems and Jellinger (doi:10.1093/brain/awx360) for a scientific commentary on this article.Cognitive changes occurring throughout the pathogenesis of neurodegenerative diseases are directly linked to synaptic loss. We used in-depth proteomics to compare 32 post-mortem human brains in the prefrontal cortex of prospectively followed patients with Alzheimer's disease, Parkinson's disease with dementia, dementia with Lewy bodies and older adults without dementia. In total, we identified 10 325 proteins, 851 of which were synaptic proteins. Levels of 25 synaptic proteins were significantly altered in the various dementia groups. Significant loss of SNAP47, GAP43, SYBU (syntabulin), LRFN2, SV2C, SYT2 (synaptotagmin 2), GRIA3 and GRIA4 were further validated on a larger cohort comprised of 92 brain samples using ELISA or western blot. Cognitive impairment before death and rate of cognitive decline significantly correlated with loss of SNAP47, SYBU, LRFN2, SV2C and GRIA3 proteins. Besides differentiating Parkinson's disease dementia, dementia with Lewy bodies, and Alzheimer's disease from controls with high sensitivity and specificity, synaptic proteins also reliably discriminated Parkinson's disease dementia from Alzheimer's disease patients. Our results suggest that these particular synaptic proteins have an important predictive and discriminative molecular fingerprint in neurodegenerative diseases and could be a potential target for early disease intervention.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Brain 141 : 2 (2018), p. 582-595. -
További szerzők:	Branca, Rui M. Francis, Paul T. Pereira, Joana B. Baek, Jean-Ha Hortobágyi Tibor (1965-) (patológus) Winblad, Bengt Ballard, Clive G. Lehtiö, Janne Aarsland, Dag
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001-es BibID:	BIBFORM095314
035-os BibID:	(WoS)000733375400006 (Scopus)85113789602
Első szerző:	Pasha, Terouz
Cím:	Karyopherin abnormalities in neurodegenerative proteinopathies / Terouz Pasha, Anna Zatorska, Daulet Sharipov, Boris Rogelj, Tibor Hortobágyi, Frank Hirth
Dátum:	2021
ISSN:	0006-8950
Megjegyzések:	Neurodegenerative proteinopathies are characterised by progressive cell loss that is preceded by the mislocalisation and aberrant accumulation of proteins prone to aggregation. Despite their different physiological functions, disease-related proteins like tau, alpha-synuclein, Tar DNA binding protein-43, Fused in sarcoma and mutant Huntingtin, all share low complexity regions that can mediate their liquid-liquid phase transitions. The proteins' phase transitions can range from native monomers to soluble oligomers, liquid droplets and further to irreversible, often-mislocalised aggregates that characterise the stages and severity of neurodegenerative diseases. Recent advances into the underlying pathogenic mechanisms have associated mislocalisation and aberrant accumulation of disease-related proteins with defective nucleocytoplasmic transport and its mediators called karyopherins. These studies identify karyopherin abnormalities in amyotrophic lateral sclerosis, frontotemporal dementia, Alzheimer's disease, and synucleinopathies including Parkinson's disease and dementia with Lewy bodies, that range from altered expression levels to the subcellular mislocalisation and aggregation of karyopherin alpha and beta proteins. The reported findings reveal that in addition to their classical function in nuclear import and export, karyopherins can also act as chaperones by shielding aggregation-prone proteins against misfolding, accumulation and irreversible phase-transition into insoluble aggregates. Karyopherin abnormalities can, therefore, be both the cause and consequence of protein mislocalisation and aggregate formation in degenerative proteinopathies. The resulting vicious feedback cycle of karyopherin pathology and proteinopathy identifies karyopherin abnormalities as a common denominator of onset and progression of neurodegenerative disease. Pharmacological targeting of karyopherins, already in clinical trials as therapeutic intervention targeting cancers such as glioblastoma and viral infections like COVID-19, may therefore represent a promising new avenue for disease-modifying treatments in neurodegenerative proteinopathies.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Brain. - 144 : 10 (2021), p. 2915-2932. -
További szerzők:	Zatorska, Anna Sharipov, Daulet Rogelj, Boris Hortobágyi Tibor (1965-) (patológus) Hirth, Frank
Pályázati támogatás:	Nemzeti Agykutatási Program 2017-1.2.1-NKP-2017-00002 Egyéb NKFIH-SNN-132999 Egyéb
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