Enkephalin L

Found 9 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
556.2802	[M+H]+ PPM:6.5	Bathymodiolus	epithelial host cells	MALDI (DHB)	MPIBremen_Bputeoserpentis_MALDI-FISH_DHB_233x233pixel_3um_mz400-1200_240k@200 - MTBLS744 Resolution: 3μm, 233x233 Description The Bathymodiolus puteoserpentis specimen used for high resolution AP-MALDI-MSI was collected during the RV Meteor M126 cruise in 2016 at the Logatchev hydrothermal vent field on the Mid-Atlantic Ridge. The specimen was retrieved with the MARUM-Quest remotely operated vehicle (ROV) at the Irina II vent site at 3038 m depth, 14°45’11.01”N and 44°58’43.98”W, and placed in an insulated container to prevent temperature changes during recovery. Gills were dissected from the mussel as soon as brought on board after ROV retrieval, submerged in precooled 2% w/v carboxymethyl cellulose gel (CMC, Mw ~ 700,000, Sigma-Aldrich Chemie GmbH) and snap-frozen in liquid N2. Samples were stored at -80 °C until use. The CMC-embedded gills were cross-sectioned at 10 µm thickness with a cryostat (Leica CM3050 S, Leica Biosystems Nussloch GmbH) at a chamber temperature of -35 °C and object holder at -22 °C. Individual sections were thaw-mounted onto coated Polysine slides (Thermo Scientific) and subsequently frozen in the cryostat chamber. Slides with tissue sections were stored in slide containers with silica granules, to prevent air moisture condensation on the tissue upon removal from the freezer. Before AP-MALDI matrix application, the sample was warmed to room temperature under a dry atmosphere in a sealed slide container (LockMailer microscope slide jar, Sigma-Aldrich, Steinheim, Germany), filled with silica granules (Carl Roth GmbH) to avoid condensation on the cold glass slide. The sample glass slide was marked with white paint around the tissue for orientation during image acquisition as previously described[1]. Additionally, optical images of the tissue section were acquired with a digital microscope (VHX-5000 Series, Keyence, Neu-Isenburg, Germany) prior to matrix application. To apply the matrix, we used an ultrafine pneumatic sprayer system with N2 gas (SMALDIPrep, TransMIT GmbH, Giessen, Germany)[2], to deliver 100 μl of a 30 mg/ml solution of 2,5-dihydroxybenzoic acid (DHB; 98% 574 purity, Sigma-Aldrich, Steinheim, Germany) dissolved in acetone/water (1:1 v/v) containing 0.1% trifluoroacetic acid (TFA). To locate the field of view and facilitate laser focusing, a red marker was applied adjacent to the matrix-covered tissue section. Ref: [1] Kaltenpoth M, Strupat K, Svatoš A Linking metabolite production to taxonomic identity in environmental samples by (MA)LDI-FISH. ISME J. 2016 Feb;10(2):527-31. doi: 10.1038/ismej.2015.122. PMID:26172211 [2] Kompauer M, Heiles S, Spengler B. Atmospheric pressure MALDI mass spectrometry imaging of tissues and cells at 1.4-μm lateral resolution. Nat Methods. 2017 Jan;14(1):90-96. doi: 10.1038/nmeth.4071. PMID:27842060 High-resolution AP-MALDI-MSI measurements were carried out at an experimental ion source setup [1][2], coupled to a Fourier transform orbital trapping mass spectrometer (Q Exactive HF, Thermo Fisher Scientific GmbH, Bremen, Germany). The sample was rastered with 233 x 233 laser spots with a step size of 3 µm without oversampling, resulting in an imaged area of 699 x 699 µm. AP-MALDI-MSI measurements were performed in positive mode for a mass detection range of 400–1200 Da and a mass resolving power of 240,000 (at 200 m/z). After AP-MALDI-MSI, the measured sample surface was recorded using a stereomicroscope (SMZ25, Nikon, Düssedorf, Germany). Ref: [1] Kompauer M, Heiles S, Spengler B. Atmospheric pressure MALDI mass spectrometry imaging of tissues and cells at 1.4-μm lateral resolution. Nat Methods. 2017 Jan;14(1):90-96. doi: 10.1038/nmeth.4071. PMID:27842060 [2] Kompauer M, Heiles S, Spengler B. Autofocusing MALDI mass spectrometry imaging of tissue sections and 3D chemical topography of nonflat surfaces. Nat Methods. 2017 Dec;14(12):1156-1158. doi:10.1038/nmeth.4433. PMID:28945703
556.2802	[M+H]+ PPM:6.5	Bathymodiolus	epithelial host cells	MALDI (DHB)	MPIMM_054_QE_P_BP_CF_Bputeoserpentis_MALDI-FISH8_Sl16_s1_DHB_233x233_3um - MTBLS744 Resolution: 3μm, 233x233 Description
556.2802	[M+H]+ PPM:6.5	Bathymodiolus	epithelial host cells	MALDI (DHB)	MPIMM_039_QE_P_BP_CF_Bputeoserpentis_MALDI-FISH8_Sl14_s1_DHB_233x233_3um - MTBLS744 Resolution: 3μm, 233x234 Description
556.2694	[M+H]+ PPM:12.9	Homo sapiens	esophagus	DESI ()	LNTO22_1_3 - MTBLS385 Resolution: 75μm, 121x68 Description
556.2696	[M+H]+ PPM:12.5	Homo sapiens	esophagus	DESI ()	LNTO22_1_5 - MTBLS385 Resolution: 75μm, 135x94 Description
556.2692	[M+H]+ PPM:13.2	Homo sapiens	esophagus	DESI ()	LNTO22_1_8 - MTBLS385 Resolution: 75μm, 69x61 Description
556.269	[M+H]+ PPM:13.6	Homo sapiens	esophagus	DESI ()	LNTO22_2_1 - MTBLS385 Resolution: 75μm, 89x88 Description
556.2691	[M+H]+ PPM:13.4	Homo sapiens	esophagus	DESI ()	LNTO26_16_1 - MTBLS385 Resolution: 75μm, 95x88 Description
556.2685	[M+H]+ PPM:14.5	Homo sapiens	colorectal adenocarcinoma	DESI ()	240TopL, 210TopR, 230BottomL, 220BottomR-centroid - MTBLS176 Resolution: 50μm, 142x141 Description

Enkephalin L is an opioid peptide. Opioid peptides are a group of neuropeptides which include enkephalins, endorphins and dynorphins. In addition to their central and peripheral antinociceptive function, opioids can modulate immune activity and cell proliferation. Enkephalins typically have a turnover rate measured in seconds to minutes, both in vivo and in vitro, and this stability is related to the age of the cell system under study. It is noteworthy that the residues most essential to enkephalin function are also either neurotransmitters themselves (glycine) or immediate precursors of L-Dopa, dopamine and norepinephrine (tyrosine and phenylalanine). The variable fifth amino acid leucine (leu5) or methionine (met5) has not yet been assigned any neurotransmitter candidacy. Again, this suggests that enkephalin is polyfunctional in that, in its intact state it elicits binding to the same sites in the brain as morphine and other opiates, and its degradation products have a potential for follow-up accessory functions by reacting as signaling entities themselves, or as the immediate precursors to inhibitory or metabotropic neurotransmitters. Enkephalins are present in macrophages infiltrating the dermal papillae in involved psoriatic skin and that the amount of enkephalin is significantly increased in involved psoriatic skin. Major enkephalin pathways in the brain involve the extrapyramidal system, including motor pathways controlled by the basal ganglia, the limbic system that governs emotional and behavioral control, and the hypothalamic-neuroendocrine axis. The apparent overlap of localization within the central nervous system of dopaminergic, glycinergic, and enkephalinergic pathways is speculated to be of neurophysiological significance, especially in light of the relatively short half-life of the enkephalins and the immediate precursor-product relationship between tyrosine and dopamine, and glycinergic signaling. Enkephalins are released into the bloodstream of mammals by the adrenal medulla. Once they are in the blood, these peptides undergo a fairly rapid hydrolysis by several plasma-contained enzymes. However, a fraction of the enkephalins present in the plasma are bound to the serum albumin, and the bound peptides are almost completely intact even after a long incubation in the presence of serum enzymes. (PMID: 9450624, 16802191, 4069309) [HMDB] Enkephalin L is an opioid peptide. Opioid peptides are a group of neuropeptides which include enkephalins, endorphins and dynorphins. In addition to their central and peripheral antinociceptive function, opioids can modulate immune activity and cell proliferation. Enkephalins typically have a turnover rate measured in seconds to minutes, both in vivo and in vitro, and this stability is related to the age of the cell system under study. It is noteworthy that the residues most essential to enkephalin function are also either neurotransmitters themselves (glycine) or immediate precursors of L-Dopa, dopamine and norepinephrine (tyrosine and phenylalanine). The variable fifth amino acid leucine (leu5) or methionine (met5) has not yet been assigned any neurotransmitter candidacy. Again, this suggests that enkephalin is polyfunctional in that, in its intact state it elicits binding to the same sites in the brain as morphine and other opiates, and its degradation products have a potential for follow-up accessory functions by reacting as signaling entities themselves, or as the immediate precursors to inhibitory or metabotropic neurotransmitters. Enkephalins are present in macrophages infiltrating the dermal papillae in involved psoriatic skin and that the amount of enkephalin is significantly increased in involved psoriatic skin. Major enkephalin pathways in the brain involve the extrapyramidal system, including motor pathways controlled by the basal ganglia, the limbic system that governs emotional and behavioral control, and the hypothalamic-neuroendocrine axis. The apparent overlap of localization within the central nervous system of dopaminergic, glycinergic, and enkephalinergic pathways is speculated to be of neurophysiological significance, especially in light of the relatively short half-life of the enkephalins and the immediate precursor-product relationship between tyrosine and dopamine, and glycinergic signaling. Enkephalins are released into the bloodstream of mammals by the adrenal medulla. Once they are in the blood, these peptides undergo a fairly rapid hydrolysis by several plasma-contained enzymes. However, a fraction of the enkephalins present in the plasma are bound to the serum albumin, and the bound peptides are almost completely intact even after a long incubation in the presence of serum enzymes. (PMID: 9450624, 16802191, 4069309). D018377 - Neurotransmitter Agents > D018847 - Opioid Peptides D018377 - Neurotransmitter Agents > D004745 - Enkephalins [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors. [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors. [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors.