Proteomic Studies on the Swim Bladder of the European Eel (<i>Anguilla anguilla</i>)

Sialana, Fernando J.; Schneebauer, Gabriel; Paunkov, Ana; Pelster, Bernd; Lübec, Gert

doi:10.1002/pmic.201700445

Cited by 11 publications

(5 citation statements)

References 21 publications

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“…Methods for sample preparation for liquid chromatography followed by tandem mass spectrometry (LC-MS/MS) were implemented as previously described [33]. Peptide analyses were performed using a single-shot LC-MS/MS approach with a 4-hour gradient using a Dionex Ultimate 3000 system (Thermo Fisher Scientific) coupled to a Q-Exactive Plus mass spectrometer (Thermo Fisher Scientific, Germany) with LCMS parameters, as described previously [49]. All MS-MS2 spectra were searched against UniProtKB/Swiss-Prot rat protein database version v 2016.04.14.…”

Section: Methodsmentioning

confidence: 99%

“…All MS-MS2 spectra were searched against UniProtKB/Swiss-Prot rat protein database version v 2016.04.14. Parameters for protein identification and label-free quantification workflow were based on the Minora algorithm through Proteome Discoverer 2.2 platform, as previously described [49]. Abundances are scaled according to the mean abundance of the samples.…”

Section: Methodsmentioning

confidence: 99%

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Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

et al. 2019

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Bardet-Biedl syndrome (BBS), a ciliopathy, is a rare genetic condition characterised by retinal degeneration, obesity, kidney failure, and cognitive impairment. In spite of progress made in our general understanding of BBS aetiology, the molecular and cellular mechanisms underlying cognitive impairment in BBS remain elusive. Here, we report that the loss of BBS proteins causes synaptic dysfunction in principal neurons, providing a possible explanation for the cognitive impairment phenotype observed in BBS patients. Using synaptosomal proteomics and immunocytochemistry, we demonstrate the presence of Bbs proteins in the postsynaptic density (PSD) of hippocampal neurons. Loss of Bbs results in a significant reduction of dendritic spines in principal neurons of Bbs mouse models. Furthermore, we show that spine deficiency correlates with events that destabilise spine architecture, such as impaired spine membrane receptor signalling, known to be involved in the maintenance of dendritic spines. Our findings suggest a role for BBS proteins in dendritic spine homeostasis that may be linked to the cognitive phenotype observed in BBS.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

et al. 2019

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“…In these cells Aqp1ab staining was localized to the apical membrane region; therefore, the authors assume it is located in the apical membranes of gas gland cells. This assumption is also supported by the detection of Aqp1 protein in the membrane fraction of European eel gas gland cells (Sialana et al ., 2018). Because CO 2 is produced in gas gland cell metabolism (Pelster et al ., 1994; Walsh & Milligan, 1993), the highest PCO 2 is expected in gas gland cells, providing a diffusion gradient not only into the blood but also into the swimbladder lumen.…”

Section: Discussionmentioning

confidence: 99%

Aquaporin expression and cholesterol content in eel swimbladder tissue

Drechsel

Schneebauer

Fiechtner

et al. 2021

Journal of Fish Biology

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Leakiness of the swimbladder wall of teleost fishes must be prevented to avoid diffusional loss of gases out of the swimbladder. Guanine incrustation as well as high concentrations of cholesterol in swimbladder membranes in midwater and deep‐sea fish has been connected to a reduced gas permeability of the swimbladder wall. On the contrary, the swimbladder is filled by diffusion of gases, mainly oxygen and CO2, from the blood and the gas gland cells into the swimbladder lumen. In swimbladder tissue of the zebrafish and the Japanese eel, aquaporin mRNA has been detected, and the aquaporin protein has been considered important for the diffusion of water, which may accidentally be gulped by physostome fish when taking an air breath. In the present study, the expression of two aquaporin 1 genes (Aqp1aa and Aqp1ab) in the swimbladder tissue of the European eel, a functional physoclist fish, was assessed using immunohistochemistry, and the expression of both genes was detected in endothelial cells of swimbladder capillaries as well as in basolateral membranes of gas gland cells. In addition, Aqp1ab was present in apical membranes of swimbladder gas gland cells. The authors also found high concentrations of cholesterol in these membranes, which were several fold higher than in muscle tissue membranes. In yellow eels the cholesterol concentration exceeded the concentration detected in silver eel swimbladder membranes. The authors suggest that aquaporin 1 in swimbladder gas gland cells and endothelial cells facilitates CO2 diffusion into the blood, enhancing the switch‐on of the Root effect, which is essential for the secretion of oxygen into the swimbladder. It may also facilitate CO2 diffusion into the swimbladder lumen along the partial gradient established by CO2 production in gas gland cells. Cholesterol has been shown to reduce the gas permeability of membranes and thus could contribute to the gas tightness of swimbladder membranes, which is essential to avoid diffusional loss of gas out of the swimbladder.

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“…Methods for sample preparation for liquid chromatography followed by tandem mass spectrometry (LC-MS/MS) were implemented as previously described (28). Peptide analyses were performed using a single-shot LC-MS/MS approach with a 4-hr gradient using a Dionex Ultimate 3000 system (Thermo Fisher Scientific) coupled to a Q-Exactive Plus mass spectrometer (Thermo Fisher Scientific, Germany) with LCMS parameters as described previously (43).…”

Section: Data Availabilitymentioning

confidence: 99%

“…All MS-MS2 spectra were searched against UniProtKB/Swiss-Prot rat protein database version v 2016.04.14. Parameters for protein identification and label-free quantification workflow based on the Minora algorithm through Proteome Discoverer 2.2 platform as previously described (43). Abundances are scaled according to the mean abundance of the samples.…”

Section: Data Availabilitymentioning

confidence: 99%

Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

Haq

Schmidt-Hieber

Sialana

et al. 2019

Preprint

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Bardet-Biedl syndrome (BBS), a ciliopathy, is a rare genetic condition characterised by retina degeneration, obesity, kidney failure and cognitive impairment. In spite of a progress made in general understanding of BBS aetiology, the molecular mechanism of cognitive impairment remains elusive. Here we report that loss of Bardet-Biedl syndrome proteins causes synaptic dysfunction in principal neurons providing possible explanation for cognitive impairment phenotype in BBS patients. Using synaptosomal proteomics and immunocytochemistry we demonstrate the presence of Bbs in postsynaptic density of hippocampal neurons. Loss of Bbs results in the significant reduction of dendritic spines in principal neurons of Bbs mice models. Furthermore, we demonstrate that spine deficiency correlates with events that destabilize spine architecture, such as, impaired spine membrane receptors signalling known to be involved in the maintenance of dendritic spines. Finally, we show that voluntary exercise rescues spine deficiency in the neurons. Based on our data, we propose a model in which Bbs proteins, similar to their function in primary cilia, regulate trafficking of signalling receptors into and out of the membrane of dendritic spines, thus providing the basis for synaptic plasticity.

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Proteomic Studies on the Swim Bladder of the European Eel (Anguilla anguilla)

Cited by 11 publications

References 21 publications

Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

Aquaporin expression and cholesterol content in eel swimbladder tissue

Loss of Bardet-Biedl syndrome proteins causes synaptic aberrations in principal neurons

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