N-Oleoyl Cysteine

Found 15 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
386.2727	[M+H]+ PPM:1	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_17 - MTBLS58 Resolution: 17μm, 208x108 Description 1 male adult wild-type rat was obtained from Inserm U1085 - Irset Research Institute (University of Rennes1, France). Animals were age 60 days and were reared under ad-lib conditions. Care and handling of all animals complied with EU directive 2010/63/EU on the protection of animals used for scientific purposes. The whole epididymis was excised from each animal immediately post-mortem, loosely wrapped rapidly in an aluminum foil and a 2.5% (w/v) carboxymethylcellulose (CMC) solution was poured to embed the epididymis to preserve their morphology. To remove air bubbles, the filled aluminum molds was gently freezed by depositing it on isopentane or dry ice, then on the nitrogen vapors and finally by progressively dipping the CMC/sample coated with aluminum foil into liquid nitrogen (or only flush with liquid nitrogen). Frozen tissues were stored at -80 °C until use to avoid degradation.
386.2728	[M+H]+ PPM:1.2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_18 - MTBLS58 Resolution: 17μm, 208x104 Description
386.2727	[M+H]+ PPM:1	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_43 - MTBLS58 Resolution: 17μm, 298x106 Description
386.2728	[M+H]+ PPM:1.2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_44 - MTBLS58 Resolution: 17μm, 299x111 Description
386.2729	[M+H]+ PPM:1.5	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_46 - MTBLS58 Resolution: 17μm, 298x106 Description
386.2729	[M+H]+ PPM:1.5	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_47 - MTBLS58 Resolution: 17μm, 301x111 Description
386.2731	[M+H]+ PPM:2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito08_48 - MTBLS58 Resolution: 17μm, 294x107 Description
386.273	[M+H]+ PPM:1.7	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_04 - MTBLS58 Resolution: 17μm, 178x91 Description
386.2731	[M+H]+ PPM:2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_03 - MTBLS58 Resolution: 17μm, 159x110 Description
386.273	[M+H]+ PPM:1.7	Rattus norvegicus	normal	MALDI (DHB)	epik_dhb_head_ito01_05 - MTBLS58 Resolution: 17μm, 183x105 Description
386.273	[M+H]+ PPM:1.7	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito01_06 - MTBLS58 Resolution: 17μm, 183x103 Description
386.2731	[M+H]+ PPM:2	Rattus norvegicus	Epididymis	MALDI (DHB)	epik_dhb_head_ito03_14 - MTBLS58 Resolution: 17μm, 205x103 Description
386.2748	[M+H]+ PPM:6.4	Mus musculus	Liver	MALDI (CHCA)	Salmonella_final_pos_recal - MTBLS2671 Resolution: 17μm, 691x430 Description A more complete and holistic view on host–microbe interactions is needed to understand the physiological and cellular barriers that affect the efficacy of drug treatments and allow the discovery and development of new therapeutics. Here, we developed a multimodal imaging approach combining histopathology with mass spectrometry imaging (MSI) and same section imaging mass cytometry (IMC) to study the effects of Salmonella Typhimurium infection in the liver of a mouse model using the S. Typhimurium strains SL3261 and SL1344. This approach enables correlation of tissue morphology and specific cell phenotypes with molecular images of tissue metabolism. IMC revealed a marked increase in immune cell markers and localization in immune aggregates in infected tissues. A correlative computational method (network analysis) was deployed to find metabolic features associated with infection and revealed metabolic clusters of acetyl carnitines, as well as phosphatidylcholine and phosphatidylethanolamine plasmalogen species, which could be associated with pro-inflammatory immune cell types. By developing an IMC marker for the detection of Salmonella LPS, we were further able to identify and characterize those cell types which contained S. Typhimurium. [dataset] Nicole Strittmatter. Holistic Characterization of a Salmonella Typhimurium Infection Model Using Integrated Molecular Imaging, metabolights_dataset, V1; 2022. https://www.ebi.ac.uk/metabolights/MTBLS2671.
386.2725	[M+H]+ PPM:0.4	Mus musculus	brain	MALDI (DHB)	Brain01_Bregma1-42_02_centroid - MTBLS313 Resolution: 17μm, 434x258 Description
386.2715	[M+H]+ PPM:2.1	Mus musculus	brain	MALDI (DHB)	Brain01_Bregma1-42_01_centroid - MTBLS313 Resolution: 17μm, 447x118 Description

N-oleoyl cysteine belongs to the class of compounds known as N-acylamides. These are molecules characterized by a fatty acyl group linked to a primary amine by an amide bond. More specifically, it is an Oleic acid amide of Cysteine. It is believed that there are more than 800 types of N-acylamides in the human body. N-acylamides fall into several categories: amino acid conjugates (e.g., those acyl amides conjugated with amino acids), neurotransmitter conjugates (e.g., those acylamides conjugated with neurotransmitters), ethanolamine conjugates (e.g., those acylamides conjugated to ethanolamine), and taurine conjugates (e.g., those acyamides conjugated to taurine). N-Oleoyl Cysteine is an amino acid conjugate. N-acylamides can be classified into 9 different categories depending on the size of their acyl-group: 1) short-chain N-acylamides; 2) medium-chain N-acylamides; 3) long-chain N-acylamides; and 4) very long-chain N-acylamides; 5) hydroxy N-acylamides; 6) branched chain N-acylamides; 7) unsaturated N-acylamides; 8) dicarboxylic N-acylamides and 9) miscellaneous N-acylamides. N-Oleoyl Cysteine is therefore classified as a long chain N-acylamide. N-acyl amides have a variety of signaling functions in physiology, including in cardiovascular activity, metabolic homeostasis, memory, cognition, pain, motor control and others (PMID: 15655504). N-acyl amides have also been shown to play a role in cell migration, inflammation and certain pathological conditions such as diabetes, cancer, neurodegenerative disease, and obesity (PMID: 23144998; PMID: 25136293; PMID: 28854168).N-acyl amides can be synthesized both endogenously and by gut microbiota (PMID: 28854168). N-acylamides can be biosynthesized via different routes, depending on the parent amine group. N-acyl ethanolamines (NAEs) are formed via the hydrolysis of an unusual phospholipid precursor, N-acyl-phosphatidylethanolamine (NAPE), by a specific phospholipase D. N-acyl amino acids are synthesized via a circulating peptidase M20 domain containing 1 (PM20D1), which can catalyze the bidirectional the condensation and hydrolysis of a variety of N-acyl amino acids. The degradation of N-acylamides is largely mediated by an enzyme called fatty acid amide hydrolase (FAAH), which catalyzes the hydrolysis of N-acylamides into fatty acids and the biogenic amines. Many N-acylamides are involved in lipid signaling system through interactions with transient receptor potential channels (TRP). TRP channel proteins interact with N-acyl amides such as N-arachidonoyl ethanolamide (Anandamide), N-arachidonoyl dopamine and others in an opportunistic fashion (PMID: 23178153). This signaling system has been shown to play a role in the physiological processes involved in inflammation (PMID: 25136293). Other N-acyl amides, including N-oleoyl-glutamine, have also been characterized as TRP channel antagonists (PMID: 29967167). N-acylamides have also been shown to have G-protein-coupled receptors (GPCRs) binding activity (PMID: 28854168). The study of N-acylamides is an active area of research and it is likely that many novel N-acylamides will be discovered in the coming years. It is also likely that many novel roles in health and disease will be uncovered for these molecules.