Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Memory-enhancing effects of Origanum majorana essential oil in an Alzheimer's amyloid beta1-42 rat model: a molecular and behavioral study

ABSTRACT: Origanum L. (Lamiaceae) is an important genus of medicinal and aromatic plants used in the traditional medicine since ancient times as culinary herbs and remedies. The effects of Origanum majorana-based aromatherapy was investigated in an Alzheimer's amyloid beta1-42 rat model. Protein extracts from brain tissue containing hippocampi were analyzed by label-free quantitative LC-HDMSE. Proteins whose expression seemed influenced by Origanum majorana-based aromatherapy were assigned as representatives of biological processes, which were further targeted using well established biochemical/molecular assays.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Brain, Regional Part Of Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Stefan Mikkat

LAB HEAD: Michael O. Glocker

PROVIDER: PXD021082 | Pride | 2020-09-29

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Memory-Enhancing Effects of Origanum majorana Essential Oil in an Alzheimer's Amyloid beta1-42 Rat Model: A Molecular and Behavioral Study.

Postu Paula Alexandra PA Gorgan Dragos Lucian DL Cioanca Oana O Russ Manuela M Mikkat Stefan S Glocker Michael Otto MO Hritcu Lucian L

Antioxidants (Basel, Switzerland) 20200926 10

Origanum L. (Lamiaceae) is an important genus of medicinal and aromatic plants used in traditional medicine since ancient times as culinary herbs and remedies. The aim of the present study was to evaluate the chemical composition, as well as the biochemical and cellular activities of freshly prepared Origanum majorana L. essential oil (OmEO) in an Alzheimer's disease (AD) amyloid beta1-42 (Aβ1-42) rat model. OmEO (1% and 3%) was inhaled for 21 consecutive days, while Aβ1-42 was adm ...[more]

PMID: 32993114

Similar Datasets

Periodontal pathogens do not exacerbate macroscopic arthritis but alter the synovial proteome

Project description:Rheumatoid arthritis (RA) and periodontitis (PD) are chronic inflammatory diseases that appear to occur in tandem. Autoantibodies against citrullinated peptide antigens linked pathogeneses with PD preceding RA. However, the mutual impact PD exerts on RA and vice versa has not yet been defined. To address this issue, we set up an animal model and analyzed how the prime inducers of citrullination - Porphyromonas gingivalis and Aggregatibacter actinomycetemcomitans ÃƒÂ¢Ã¢â€šÂ¬Ã¢â‚¬Å“ differ in their pathogenic potential. Our experimental setup included collagen induced arthritis (CIA) in the mouse, oral inoculation with P. gingivalis or A. actinomycetemcomitans to induce alveolar bone loss and the combination of both diseases in inverted orders of events. Label-free quantitative proteome analysis revealed that P. gingivalis and A. actinomycetemcomitans led to differential expression patterns in the synovial membranes that were reminiscent of cellular and humoral immune responses, respectively. The P. gingivalis and A. actinomycetemcomitans specific signatures in the synovial proteomes suggest a role for oral pathogens in shaping disease subtypes and setting the stage for subsequent therapy response.

2020-12-04 | PXD020397 | Pride

Chronic pancreatitis vs pancreatic cancer LC-MS

Project description:Age-standardized incidence rates for pancreatic cancer (PC) in men have increased by 25% from 1957 to 2011 in Finland. The average age of diagnosis for PC is 69 years in Nordic males, whereas the average age of diagnosis of chronic pancreatitis (CP) is 40-50 years, but the cases overlap in age. By radiology the evaluation of a pancreatic mass, i.e. the differential diagnosis between CP and PC is often difficult. Preoperative needle biopsies are difficult to obtain and are demanding to interpret. New blood based biomarkers are needed. The accuracy of the only established biomarker for PC, CA 19-9 is rather poor in differentiating between benign and malignant mass of the pancreas. In this study, we have performed mass spectrometry HDMSE analysis of serum samples from patients with chronic pancreatitis and pancreatic cancer. We have quantified 652 proteins and performed detailed statistical analysis such as principal component analysis, orthogonal partial least square discriminant analysis and receiver operating curve analysis.

2017-06-09 | PXD005144 | Pride

Stoichiometry of two plant glycine decarboxylase complexes and comparison with a cyanobacterial glycine cleavage system

Project description:The multienzyme glycine cleavage system (GCS) converts glycine and tetrahydrofolate to the one-carbon compound 5,10-methylenetetrahydrofolate, which is of vital importance for most if not all organisms. Photorespiring plant mitochondria contain very high levels of GCS proteins organized as a fragile glycine decarboxylase complex (GDC). The aim of this study is to provide mass spectrometry-based stoichiometric data for the plant leaf GDC and examine whether complex formation could be a general property of the GCS in photosynthesizing organisms. To this end, we investigated the mitochondrial content, the stoichiometry and the isoprotein composition of the Arabidopsis thaliana leaf GDC in comparison with that of Pisum sativum using stable-isotope-labeled peptides (QconCAT and synthetic labeled peptides) and compared the results to label-free, Hi3 peptide quantification.

2020-04-23 | PXD018211 | Pride

Differential proteomics of human seminal fluid Normo Vs Astehnozoospermia

Project description:Scarcely understood defects lead to asthenozoospermia which results in poor fertility outcomes. Incomplete knowledge of these defects hinders the development of new therapies and reliance on interventional therapies, such as in vitro fertilization, increases. Sperm cells, being transcriptionally and translationally silent, necessitate the proteomic approach to study the sperm funnction. We have performed a differential proteomics analysis of human sperm and seminal fluid and identified over 1,700 proteins. We have included 667 proteins in sperm and 430 proteins in seminal plasma dataset for further analysis. Statistical and mathematical analysis combined with pathway analysis and self organizing maps clustering and correlation was performed on the dataset. It was found that sperm proteomic signature combined with statistical analysis as opposed to the seminal plasma proteomic signature can differentiate the normozoospermic versus the asthenozoospermic sperm samples.

2016-12-13 | PXD004098 | Pride

Label-free quantitative proteomic analysis of DNA methyltransferase mutants of the cyanobacterium Synechocystis sp. PCC 6803 – Analysis of total protein extracts

Project description:Total protein and membrane-enriched fractions of Synechocystis sp. PCC 6803 wild type (WT) and mutant strains affected with inactivated DNA methyltransferase genes were analyzed by LC-HDMSE. The mutation of the DNA methyltransferase gene sll0729 encoding M.Ssp6803II initially led to a strong phenotype, including a lowered chlorophyll/phycocyanin ratio, impaired growth, and alterations in gene expression. Prolonged cultivation revealed instability of the initially obtained phenotype. Colonies showing normal pigmentation and WT-like growth appeared regularly and in high frequencies on agar plates. These colonies represent suppressor mutants, since the sll0729 gene is still completely inactivated and methylation of the M.Ssp6803II target GGCC sites does not occur. The proteomic analysis comprises the WT, two strains of suppressor mutants sll0729_1 and sll0729_15 as well as mutants of the DNA methyltransferase genes slr6095 and sll8009. For each of these five strains we investigated three biological replicates. Comparisons between the WT and these two suppressor mutant strains, but also between them and the slr6095 and sll8009 mutants enabled the detection of expression differences, which are specifically linked to the absence of M.Ssp6803II-related DNA methylation.

2019-06-26 | PXD012751 | Pride

Label-free quantitative proteomic analysis of DNA methyltransferase mutants of the cyanobacterium Synechocystis sp. PCC 6803 – Analysis of the membrane-enriched fraction

2019-06-26 | PXD012698 | Pride

Patients with early stage oropharyngeal squamous cell carcinoma can be identified with label-free serum proteomics

Project description:Increased incidence of oropharyngeal squamous cell carcinoma (OPSCC) is mainly related to Human Papilloma Virus (HPV) infection. As OPSCCs are often diagnosed at an advanced stage, mortality and morbidity remain high. There are no diagnostic biomarkers for early stage detection of OPSCC. Serum from 25 patients with stage I-II OPSCC and 12 disease- individuals were studied with quantitative label-free proteomics using ultra-definition MSE. Statistical analyses were performed to identify proteins most reliably distinguishing early stage OPSCCs from controls. P16 was used as a surrogate marker for HPV. P16-positive and -negative tumours were also analysed separately. With two or more unique proteins per identification, 176 proteins were quantified. A clear separation between patients with early-stage tumours and controls was seen in principal component analysis. Latent structures discriminant analysis identified 96 proteins most reliably differentiating OPSCC patients from controls, with 13 upregulated and 83 downregulated in study cases. The set of proteins was studied further with network, pathway and protein-protein interaction analyses, and found to participate in e.g. lipid metabolism. We identified patients with early stage OPSCC from controls based on their serum proteome, and suggest a protein set for further evaluation as a diagnostic biomarker panel for OPSCC.

2018-07-11 | PXD008445 | Pride

A snapshot of blood plasma proteomics in clinical response to atypical antipsychotics in schizophrenia – An exploratory study

Project description:Antipsychotics are usually the first option to treat schizophrenia; however, for a considerable fraction of patients, it lacks efficacy. Furthermore, there are no known biomarkers to indicate a treatment’s efficacy in a patient. Schizophrenia causes a large socioeconomic burden on countries along with an unquestionable impairment of the quality of life of patients and their relatives. As proteomics can identify, quantify, and characterize proteins in different conditions, it is a powerful tool to study complex diseases such as schizophrenia, also capable of revealing potential biomarkers. To improve treatment efficacy during the early stages of schizophrenia, a critical time period, molecular markers for a positive treatment response were sought. Blood plasma samples were collected in vivo from 26 patients before treatment with the atypical antipsychotics olanzapine and risperidone; they were then classified as good (GR) and poor (PR) responders. We were able to identify a potential panel of proteins that may predict a positive outcome to olanzapine and risperidone treatment. Although still exploratory, this data will assist in the development of personalized medicine strategies with potential clinical implementation

2020-06-01 | PXD015213 | Pride

Proteomic landscape of atypical antipsychotics clinical response in blood plasma from schizophrenia patients

Project description:Antipsychotics are the main line of treatment for schizophrenia, despite being effective only in about 50% of patients. Additionally, serious side effects may cause medication drop-out, aggravated by a lack of understanding about how these drugs act at molecular level. As proteomics is a suitable tool for studying multifactorial disorders, the main goal was to unravel signaling pathways in blood plasma associated with a positive treatment outcome for the atypical antipsychotics olanzapine and risperidone. Blood plasma was collected from schizophrenia patients six weeks after treatment (T6), and patients were classified as good or poor responders to olanzapine or risperidone, and then samples were compared to each patient's baseline (T0). All samples were analyzed using label-free quantitative shotgun proteomics. Samples were depleted of the 14 most abundant proteins in plasma, were digested, and then submitted to M-Class two-dimensional nano-liquid chromatography, coupled online to a Synapt G2-Si mass spectrometer. Data was obtained in MSE mode (data- independent acquisition) in combination with ion-mobility (HDMSE). The proteins found to be differentially abundant in good responders compared to poor responders for risperidone and olanzapine were functionally analyzed in silico using Ingenuity® Pathway Analysis and were found to be mostly involved with immune system functions. This data can contribute to better understand the biochemical signaling peripherally triggered by antipsychotic medication, and can eventually be used to help improve treatment outcome by predicting patient response as well as through the development of new medication or a combination of drugs that act on the immune system to reduce the duration of poor response periods in patients suffering with schizophrenia.

2020-06-01 | PXD015049 | Pride

Structural basis for DNA recognition and allosteric control of the Retinoic Acid Receptors RAR-RXR

Project description:Retinoic Acid Receptors (RARs) as a functional heterodimer with Retinoid X Receptors (RXRs), bind a diverse series of RA-response elements (RAREs) in regulated genes. Among them, the non-canonical DR0 elements are bound by RXR-RAR with comparable affinities to DR5 elements but DR0 elements do not act transcriptionally as independent RAREs. In this work, we present structural insight for the recognition of DR5 and DR0 elements by RXR-RAR heterodimer using x-ray crystallography, small angle x-ray scattering, and hydrogen/deuterium exchange coupled to mass spectrometry. We solved the crystal structure of RXR-RAR DNA-binding domain in complex with the Rarb2 DR5 and RXR DNA-binding domain in complex with Hoxb13 DR0. While cooperative binding was observed on DR5, on DR0 the two molecules bound non-cooperatively on opposite sides of the DNA. In addition, our data unveil the structural organization and dynamics of the multi-domain RXR-RAR DNA complexes providing evidence for DNA-dependent allosteric communication between domains. Differential binding mode between DR0 and DR5 were observed leading to differences in the conformation and structural dynamics of the multi-domain RXR-RAR DNA complex. These results reveal that the topological organization of the RAR binding element confer regulatory information by modulating the overall topology and structural dynamics of the RXR-RAR heterodimers.

2021-02-10 | PXD018172 | Pride