N-acetylglucosamine/N-acetylgalactosamine

Found 16 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
221.1175	[M-H2O+NH4]+ PPM:19.5	Marker Pen	NA	DESI (None)	3ul_0.8Mpa_RAW_20241016-PAPER PNMK - MEMI_test Resolution: 30μm, 315x42 Description By writing the four English letters “PNMK” on white paper with a marker pen, and then scanning with a DESI ion source to obtain the scanning result. The signal of the chemical substances on the marker pen used appears on the channel with an m/z value of 322.1918, 323.1953, 546.4010, and etc, from the single cell deconvolution sampling layer class_4. This test data was tested by chuxiaoping from PANOMIX’s R&D laboratory.
221.1176	[M-H2O+NH4]+ PPM:19.9	Homo sapiens	esophagus	DESI ()	LNTO22_1_4 - MTBLS385 Resolution: 17μm, 82x80 Description
239.127	[M+NH4]+ PPM:13.6	Homo sapiens	esophagus	DESI ()	LNTO29_16_2 - MTBLS385 Resolution: 17μm, 95x101 Description
244.0776	[M+Na]+ 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.
221.0855	[M]+ PPM:17.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_9 - MTBLS385 Resolution: 75μm, 89x74 Description
221.0854	[M]+ PPM:18	Homo sapiens	colorectal adenocarcinoma	DESI ()	439TopL, 409TopR, 429BottomL, 419BottomR-profile - MTBLS415 Resolution: 17μm, 157x136 Description The human colorectal adenocarcinoma sample was excised during a surgical operation performed at the Imperial College Healthcare NHS Trust. The sample and procedures were carried out in accordance with ethical approval (14/EE/0024).
239.1271	[M+NH4]+ PPM:14	Homo sapiens	colorectal adenocarcinoma	DESI ()	439TopL, 409TopR, 429BottomL, 419BottomR-profile - MTBLS415 Resolution: 17μm, 157x136 Description The human colorectal adenocarcinoma sample was excised during a surgical operation performed at the Imperial College Healthcare NHS Trust. The sample and procedures were carried out in accordance with ethical approval (14/EE/0024).
239.1273	[M+NH4]+ PPM:14.8	Homo sapiens	NA	DESI ()	160TopL,130TopR,150BottomL,140BottomR-profile - MTBLS415 Resolution: 17μm, 142x136 Description
239.1268	[M+NH4]+ PPM:12.7	Homo sapiens	esophagus	DESI ()	LNTO29_16_3 - MTBLS385 Resolution: 17μm, 108x107 Description
221.0855	[M]+ PPM:17.6	Homo sapiens	esophagus	DESI ()	LNTO26_7_2 - MTBLS385 Resolution: 17μm, 135x101 Description
239.1271	[M+NH4]+ PPM:14	Homo sapiens	esophagus	DESI ()	LNTO30_17_2 - MTBLS385 Resolution: 75μm, 82x54 Description
221.0854	[M]+ PPM:18	Homo sapiens	esophagus	DESI ()	LNTO22_1_5 - MTBLS385 Resolution: 75μm, 135x94 Description
221.0856	[M]+ PPM:17.1	Homo sapiens	esophagus	DESI ()	LNTO22_2_1 - MTBLS385 Resolution: 75μm, 89x88 Description
221.086	[M]+ PPM:15.3	Homo sapiens	esophagus	DESI ()	LNTO22_2_2 - MTBLS385 Resolution: 75μm, 135x94 Description
239.127	[M+NH4]+ PPM:13.6	Homo sapiens	esophagus	DESI ()	LNTO29_18_2 - MTBLS385 Resolution: 75μm, 62x68 Description
239.1273	[M+NH4]+ PPM:14.8	Homo sapiens	colorectal adenocarcinoma	DESI ()	160TopL,130TopR,150BottomL,140BottomR-centroid - MTBLS176 Resolution: 50μm, 142x136 Description

N-Acetylgalactosamine, also known as GalNAc, belongs to the class of organic compounds known as N-acyl-alpha-hexosamines. These are carbohydrate derivatives containing a hexose moiety in which the oxygen atom is replaced by an N-acyl group. N-Acetylgalactosamine is also classified as an amino sugar derivative of galactose. In humans GalNAc functions as the terminal carbohydrate forming the antigen of blood group A. GalNAc is typically the first monosaccharide that connects serine or threonine during protein O-glycosylation and the formation of glycoproteins. This is often referred to as mucin-type O-glycosylation, as the mucins (a class of a family of high molecular weight, heavily glycosylated proteins produced by epithelial tissues in most animals which have an ability to form gels) are heavily O-GalNAc modified. Interestingly, mammals have genes encoding for approximately 20 different polypeptide-N-acetylgalactosaminyltransferases (ppGalNAcTs), all of which transfer GalNAc from UDP-GalNAc to a hydroxyl-containing amino acids such as serine or threonine. N- O-GalNAc-containing glycoproteins appear to play a variety of essential roles. Among these is the ability of the mucins to hydrate and protect tissues by trapping bacteria. These O-glycans can also significantly alter the conformation of the protein and on the heavily modified proteins may protect the polypeptide from proteolytic digestion. O-GalNAc structures also appear to play an essential role in sperm–egg interactions. From a pathophysiological perspective, O-GalNAc modification appears to play a critical role in the immune system, cell–cell interactions, and cancer. N-Acetylgalactosamine is an important constituent of brain heteropolysaccharides (glycoproteins). The concentration of the N-acetylgalactosamine-containing glycoproteins in the 3-year-old cerebral gray matter from human brain is 7-15 times greater than in 8-year old tissue and 15-30 times greater than in 72-year-old tissue. Outside of the human body, N-Acetylgalactosamine has been detected, but not quantified in, several different foods, such as prickly pears, italian sweet red peppers, wheats, silver lindens, and sour cherries. This could make N-acetylgalactosamine a potential biomarker for the consumption of these foods. N-acetylgalactosamine, also known as alpha-galnac or tn, is a member of the class of compounds known as N-acyl-alpha-hexosamines. N-acyl-alpha-hexosamines are carbohydrate derivatives containing a hexose moiety in which the oxygen atom is replaced by an n-acyl group. N-acetylgalactosamine is soluble (in water) and a very weakly acidic compound (based on its pKa). N-acetylgalactosamine can be found in a number of food items such as colorado pinyon, common bean, mulberry, and jostaberry, which makes N-acetylgalactosamine a potential biomarker for the consumption of these food products. N-acetylgalactosamine can be found primarily in feces and saliva, as well as throughout most human tissues. N-Acetylgalactosamine (GalNAc), is an amino sugar derivative of galactose . D-N-Acetylgalactosamine is an endogenous metabolite.