Full Text Journal Articles by
Author Stefan Kins

Advertisement

Find full text journal articles






Converging roles of PSENEN/PEN2 and CLN3 in the autophagy-lysosome system.

Marcel Klein, Abuzar Kaleem, Sandra Oetjen, Daniela Wünkhaus, Lars Binkle, Sandra Schilling, Milena Gjorgjieva, Ralf Scholz, Doris Gruber-Schoffnegger, Stephan Storch, Stefan Kins, Gerard Drewes, Sabine Hoffmeister-Ullerich, Dietmar Kuhl, Guido Hermey,

PSENEN/PEN2 is the smallest subunit of the γ-secretase complex, an intramembrane protease that cleaves proteins within their transmembrane domains. Mutations in components of the γ-secretase underlie familial Alzheimer disease. In addition to its proteolytic activity, supplementary, γ-secretase independent, functions in the macroautophagy/autophagy-lysosome system have been proposed. Here, we screened for ... Read more >>

Autophagy (Autophagy)
[2021, :1-18]

Cited: 0 times

View full text PDF listing >>



Drug development for neurodegenerative diseases.

Stefan Kins, Karl-Herbert Schäfer, Kristina Endres,

Biol Chem (Biological chemistry)
[2021, 403(1):1]

Cited: 0 times

View full text PDF listing >>



Advertisement

Brothers in arms: proBDNF/BDNF and sAPPα/Aβ-signaling and their common interplay with ADAM10, TrkB, p75NTR, sortilin, and sorLA in the progression of Alzheimer's disease.

Simone Eggert, Stefan Kins, Kristina Endres, Tanja Brigadski,

Brain-derived neurotrophic factor (BDNF) is an important modulator for a variety of functions in the central nervous system (CNS). A wealth of evidence, such as reduced mRNA and protein level in the brain, cerebrospinal fluid (CSF), and blood samples of Alzheimer's disease (AD) patients implicates a crucial role of BDNF ... Read more >>

Biol Chem (Biological chemistry)
[2022, 403(1):43-71]

Cited: 0 times

View full text PDF listing >>



The role of mycotoxins in neurodegenerative diseases: current state of the art and future perspectives of research.

Vu Thu Thuy Nguyen, Svenja König, Simone Eggert, Kristina Endres, Stefan Kins,

Mycotoxins are fungal metabolites that can cause various diseases in humans and animals. The adverse health effects of mycotoxins such as liver failure, immune deficiency, and cancer are well-described. However, growing evidence suggests an additional link between these fungal metabolites and neurodegenerative diseases. Despite the wealth of these initial reports, ... Read more >>

Biol Chem (Biological chemistry)
[2022, 403(1):3-26]

Cited: 0 times

View full text PDF listing >>



Fe65: A Scaffolding Protein of Actin Regulators.

Vanessa Augustin, Stefan Kins,

The scaffolding protein family Fe65, composed of Fe65, Fe65L1, and Fe65L2, was identified as an interaction partner of the amyloid precursor protein (APP), which plays a key function in Alzheimer's disease. All three Fe65 family members possess three highly conserved interaction domains, forming complexes with diverse binding partners that can ... Read more >>

Cells (Cells)
[2021, 10(7):]

Cited: 1 time

View full text PDF listing >>



Artemisinin-treatment in pre-symptomatic APP-PS1 mice increases gephyrin phosphorylation at Ser270: a modification regulating postsynaptic GABAAR density.

Eva Kiss, Stefan Kins, Karin Gorgas, Maret Orlik, Carolin Fischer, Kristina Endres, Andrea Schlicksupp, Joachim Kirsch, Jochen Kuhse,

Artemisinins, a group of plant-derived sesquiterpene lactones, are efficient antimalarial agents. They also share anti-inflammatory and anti-viral activities and were considered for treatment of neurodegenerative disorders like Alzheimer's disease (AD). Additionally, artemisinins bind to gephyrin, the multifunctional scaffold of GABAergic synapses, and modulate inhibitory neurotransmission <i>in vitro</i>. We previously reported ... Read more >>

Biol Chem (Biological chemistry)
[2022, 403(1):73-87]

Cited: 1 time

View full text PDF listing >>



Artesunate restores the levels of inhibitory synapse proteins and reduces amyloid-β and C-terminal fragments (CTFs) of the amyloid precursor protein in an AD-mouse model.

Eva Kiss, Stefan Kins, Yasmin Zöller, Sandra Schilling, Karin Gorgas, Dagmar Groß, Andrea Schlicksupp, Rita Rosner, Joachim Kirsch, Jochen Kuhse,

Alzheimer's disease (AD) is the most frequent form of dementia, characterized histopathologically by the formation of amyloid plaques and neurofibrillary tangles in the brain. Amyloid β-peptide (Aβ) is a major component of amyloid plaques and is released together with carboxy-terminal fragments (CTFs) from the amyloid precursor protein (APP) through proteolytic ... Read more >>

Mol Cell Neurosci (Molecular and cellular neurosciences)
[2021, 113:103624]

Cited: 1 time

View full text PDF listing >>



The amyloid precursor protein affects glyceraldehyde 3-phosphate dehydrogenase levels, organelle localisation and thermal stability.

Alexandré Delport, Stefan Kins, Raymond Hewer,

Glyceraldehyde 3-phosphate dehydrogenase's (GAPDH) proapoptotic response to cellular oxidative stress has suspected implication for Alzheimer's disease (AD). Interestingly, the overexpression of the amyloid precursor protein (APP) can initiate oxidative stress responses within mammalian cell lines. Here, APP695 and APP770 overexpression significantly increased the level of GAPDH, while no effect was ... Read more >>

Mol Biol Rep (Molecular biology reports)
[2020, 47(4):3019-3024]

Cited: 2 times

View full text PDF listing >>



Amyloid-β Fosters p35/CDK5 Signaling Contributing to Changes of Inhibitory Synapses in Early Stages of Cerebral Amyloidosis.

Eva Kiss, Femke Groeneweg, Karin Gorgas, Andrea Schlicksupp, Stefan Kins, Joachim Kirsch, Jochen Kuhse,

Early changes in inhibitory synapse connectivities are thought to contribute to the excitation/inhibition imbalance preceding neurodegeneration in Alzheimer's disease (AD). Recently, we reported a robust increase in the level of different key-proteins of inhibitory synapses in hippocampal subregions of pre-symptomatic APPswe-PS1 mice, a model of cerebral amyloidosis. Besides increased inhibitory ... Read more >>

J Alzheimers Dis (Journal of Alzheimer's disease : JAD)
[2020, 74(4):1167-1187]

Cited: 1 time

View full text PDF listing >>



A fluorescent protein-readout for transcriptional activity reveals regulation of APP nuclear signaling by phosphorylation sites.

Uwe Konietzko, Manuel T Gersbacher, Jeremy Streuli, Maik Krüger, Sarina Thöni, Stefan Kins, Roger M Nitsch,

Signaling pathways that originate at the plasma membrane, including regulated intramembrane proteolysis (RIP), enable extracellular cues to control transcription. We modified the yeast Gal4 transcription system to study the nuclear translocation of transcriptionally active complexes using the fluorescent protein citrine (Cit) as a reporter. This enabled highly sensitive quantitative analysis ... Read more >>

Biol Chem (Biological chemistry)
[2019, 400(9):1191-1203]

Cited: 1 time

View full text PDF listing >>



Amyloidosis causes downregulation of SorLA, SorCS1 and SorCS3 expression in mice.

Guido Hermey, Sabine A Hoffmeister-Ullerich, Barbara Merz, Dagmar Groß, Dietmar Kuhl, Stefan Kins,

Accumulation of β-amyloid peptide (Aβ) is regarded as a primary cause of Alzheimer's disease (AD). Aβ is derived by sequential cleavage of the amyloid precursor protein (APP). Alterations in the subcellular targeting of APP are thought to affect the degree of Aβ production. Sorting receptors, such as SorLA, convey subcellular ... Read more >>

Biol Chem (Biological chemistry)
[2019, 400(9):1181-1189]

Cited: 2 times

View full text PDF listing >>



Copper and zinc ions govern the trans-directed dimerization of APP family members in multiple ways.

Alexander August, Nadine Schmidt, Johannes Klingler, Frederik Baumkötter, Marius Lechner, Jessica Klement, Simone Eggert, Carolyn Vargas, Klemens Wild, Sandro Keller, Stefan Kins,

The amyloid precursor protein (APP) and its homologs amyloid precursor-like protein 1 (APLP1) and APLP2 have central physiological functions in transcellular adhesion that depend on copper and zinc mediated trans-directed dimerization of the extracellular domains E1 and E2. Copper binds to three distinct sites in APP, one in the copper binding ... Read more >>

J Neurochem (Journal of neurochemistry)
[2019, 151(5):626-641]

Cited: 0 times

View full text PDF listing >>



Early alterations in hippocampal perisomatic GABAergic synapses and network oscillations in a mouse model of Alzheimer's disease amyloidosis.

Jan-Oliver Hollnagel, Shehabeldin Elzoheiry, Karin Gorgas, Stefan Kins, Carlo Antonio Beretta, Joachim Kirsch, Jochen Kuhse, Oliver Kann, Oliver Kann, Eva Kiss,

Several lines of evidence imply changes in inhibitory interneuron connectivity and subsequent alterations in oscillatory network activities in the pathogenesis of Alzheimer's Disease (AD). Recently, we provided evidence for an increased immunoreactivity of both the postsynaptic scaffold protein gephyrin and the GABAA receptor γ2-subunit in the hippocampus of young (1 ... Read more >>

PLoS One (PloS one)
[2019, 14(1):e0209228]

Cited: 11 times

View full text PDF listing >>



Dimerization leads to changes in APP (amyloid precursor protein) trafficking mediated by LRP1 and SorLA.

Simone Eggert, A C Gonzalez, C Thomas, S Schilling, S M Schwarz, C Tischer, V Adam, P Strecker, V Schmidt, T E Willnow, G Hermey, C U Pietrzik, E H Koo, Stefan Kins,

Proteolytic cleavage of the amyloid precursor protein (APP) by α-, β- and γ-secretases is a determining factor in Alzheimer's disease (AD). Imbalances in the activity of all three enzymes can result in alterations towards pathogenic Aβ production. Proteolysis of APP is strongly linked to its subcellular localization as the secretases ... Read more >>

Cell Mol Life Sci (Cellular and molecular life sciences : CMLS)
[2018, 75(2):301-322]

Cited: 13 times

View full text PDF listing >>



Trafficking in Alzheimer's Disease: Modulation of APP Transport and Processing by the Transmembrane Proteins LRP1, SorLA, SorCS1c, Sortilin, and Calsyntenin.

Simone Eggert, Carolin Thomas, Stefan Kins, Guido Hermey,

The amyloid precursor protein (APP), one key player in Alzheimer's disease (AD), is extensively processed by different proteases. This leads to the generation of diverging fragments including the amyloid β (Aβ) peptide, which accumulates in brains of AD patients. Subcellular trafficking of APP is an important aspect for its proteolytic ... Read more >>

Mol Neurobiol (Molecular neurobiology)
[2018, 55(7):5809-5829]

Cited: 16 times

View full text PDF listing >>



APLP1 Is a Synaptic Cell Adhesion Molecule, Supporting Maintenance of Dendritic Spines and Basal Synaptic Transmission.

Sandra Schilling, Annika Mehr, Susann Ludewig, Jonathan Stephan, Marius Zimmermann, Alexander August, Paul Strecker, Martin Korte, Edward H Koo, Ulrike C Müller, Stefan Kins, Simone Eggert,

The amyloid precursor protein (APP), a key player in Alzheimer's disease, belongs to the family of synaptic adhesion molecules (SAMs) due to its impact on synapse formation and synaptic plasticity. These functions are mediated by both the secreted APP ectodomain that acts as a neurotrophic factor and full-length APP forming ... Read more >>

J Neurosci (The Journal of neuroscience : the official journal of the Society for Neuroscience)
[2017, 37(21):5345-5365]

Cited: 18 times

View full text PDF listing >>



APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.

Suzanne Guénette, Paul Strecker, Stefan Kins,

Understanding the molecular mechanisms underlying amyloid precursor protein family (APP/APP-like proteins, APLP) function in the nervous system can be achieved by studying the APP/APLP interactome. In this review article, we focused on intracellular APP interacting proteins that bind the YENPTY internalization motif located in the last 15 amino acids of ... Read more >>

Front Mol Neurosci (Frontiers in molecular neuroscience)
[2017, 10:87]

Cited: 10 times

View full text PDF listing >>



Fe65-PTB2 Dimerization Mimics Fe65-APP Interaction.

Lukas P Feilen, Kevin Haubrich, Paul Strecker, Sabine Probst, Simone Eggert, Gunter Stier, Irmgard Sinning, Uwe Konietzko, Stefan Kins, Bernd Simon, Klemens Wild,

Physiological function and pathology of the Alzheimer's disease causing amyloid precursor protein (APP) are correlated with its cytosolic adaptor Fe65 encompassing a WW and two phosphotyrosine-binding domains (PTBs). The C-terminal Fe65-PTB2 binds a large portion of the APP intracellular domain (AICD) including the GYENPTY internalization sequence fingerprint. AICD binding to ... Read more >>

Front Mol Neurosci (Frontiers in molecular neuroscience)
[2017, 10:140]

Cited: 5 times

View full text PDF listing >>



LRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric State.

Uta-Mareike Herr, Paul Strecker, Steffen E Storck, Carolin Thomas, Verena Rabiej, Anne Junker, Sandra Schilling, Nadine Schmidt, C Marie Dowds, Simone Eggert, Claus U Pietrzik, Stefan Kins,

The low-density lipoprotein receptor-related protein 1, LRP1, interacts with APP and affects its processing. This is assumed to be mostly caused by the impact of LRP1 on APP endocytosis. More recently, also an interaction of APP and LRP1 early in the secretory pathway was reported whereat retention of LRP1 in ... Read more >>

Front Mol Neurosci (Frontiers in molecular neuroscience)
[2017, 10:118]

Cited: 4 times

View full text PDF listing >>



Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.

Klemens Wild, Alexander August, Claus U Pietrzik, Stefan Kins,

Alzheimer's disease (AD) is ultimately linked to the amyloid precursor protein (APP). However, current research reveals an important synaptic function of APP and APP-like proteins (APLP1 and 2). In this context various neurotrophic and neuroprotective functions have been reported for the APP proteolytic fragments sAPPα, sAPPβ and the monomeric amyloid-beta ... Read more >>

Front Mol Neurosci (Frontiers in molecular neuroscience)
[2017, 10:21]

Cited: 12 times

View full text PDF listing >>



Biphasic Alteration of the Inhibitory Synapse Scaffold Protein Gephyrin in Early and Late Stages of an Alzheimer Disease Model.

Eva Kiss, Karin Gorgas, Andrea Schlicksupp, Dagmar Groß, Stefan Kins, Joachim Kirsch, Jochen Kuhse,

The pathogenesis of Alzheimer disease (AD) is thought to begin many years before the diagnosis of dementia. Accumulating evidence indicates the involvement of GABAergic neurotransmission in the physiopathology of AD. However, in comparison to excitatory synapses, the structural and functional alterations of inhibitory synapses in AD are less well characterized. ... Read more >>

Am J Pathol (The American journal of pathology)
[2016, 186(9):2279-2291]

Cited: 7 times

View full text PDF listing >>



Conventional kinesin: Biochemical heterogeneity and functional implications in health and disease.

Gerardo Morfini, Nadine Schmidt, Carina Weissmann, Gustavo Pigino, Stefan Kins,

Intracellular trafficking events powered by microtubule-based molecular motors facilitate the targeted delivery of selected molecular components to specific neuronal subdomains. Within this context, we provide a brief review of mechanisms underlying the execution of axonal transport (AT) by conventional kinesin, the most abundant kinesin-related motor protein in the mature nervous ... Read more >>

Brain Res Bull (Brain research bulletin)
[2016, 126(Pt 3):347-353]

Cited: 28 times

View full text PDF listing >>



FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.

Paul Strecker, Susann Ludewig, Marco Rust, Tabea A Mundinger, Andreas Görlich, Elisa G Krächan, Christina Mehrfeld, Joachim Herz, Martin Korte, Suzanne Y Guénette, Stefan Kins,

The FE65 adaptor proteins (FE65, FE65L1 and FE65L2) bind proteins that function in diverse cellular pathways and are essential for specific biological processes. Mice lacking both FE65 and FE65L1 exhibit ectopic neuronal positioning in the cortex and muscle weakness. p97FE65-KO mice, expressing a shorter FE65 isoform able to bind amyloid ... Read more >>

Sci Rep (Scientific reports)
[2016, 6:25652]

Cited: 10 times

View full text PDF listing >>



Modulation of BAG3 Expression and Proteasomal Activity by sAPPα Does Not Require Membrane-Tethered Holo-APP.

Arpita Kundu, Nelli Milosch, Patrick Antonietti, Frederik Baumkötter, Andreas Zymny, Ulrike C Müller, Stefan Kins, Parvana Hajieva, Christian Behl, Donat Kögel,

Maintenance of intracellular proteostasis is essential for neuronal function, and emerging data support the view that disturbed proteostasis plays an important role in brain aging and the pathogenesis of age-related neurodegenerative disorders such as Alzheimer's disease (AD). sAPPalpha (sAPPα), the extracellularly secreted N-terminal alpha secretase cleavage product of the amyloid ... Read more >>

Mol Neurobiol (Molecular neurobiology)
[2016, 53(9):5985-5994]

Cited: 5 times

View full text PDF listing >>



SorCS1 variants and amyloid precursor protein (APP) are co-transported in neurons but only SorCS1c modulates anterograde APP transport.

Guido Hermey, Nadine Schmidt, Björn Bluhm, Daniel Mensching, Kristina Ostermann, Carsten Rupp, Dietmar Kuhl, Stefan Kins,

Processing of amyloid precursor protein (APP) into amyloid-β peptide (Aβ) is crucial for the development of Alzheimer's disease (AD). Because this processing is highly dependent on its intracellular itinerary, altered subcellular targeting of APP is thought to directly affect the degree to which Aβ is generated. The sorting receptor SorCS1 ... Read more >>

J Neurochem (Journal of neurochemistry)
[2015, 135(1):60-75]

Cited: 8 times

View full text PDF listing >>



Advertisement


Disclaimer

0.9991 s