Angiotensin IV

Found 12 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
797.3873	[M+Na]+ PPM:10.5	Mus musculus	Lung	MALDI (DHB)	image1 - MTBLS2075 Resolution: 40μm, 187x165 Description Fig. 2 MALDI-MSI data from the same mouse lung tissue analyzed in Fig. 1. A: Optical image of the post-MSI, H&E-stained tissue section. B–D, F–G: Ion images of (B) m/z 796.6855 ([U13C-DPPC+Na]+), (C) m/z 756.5514 ([PC32:0+Na]+), (D) m/z 765.6079 ([D9-PC32:0+Na]+), (F) m/z 754.5359 ([PC32:1+Na]+), and (G) m/z 763.5923 ([D9-PC32:1+Na]+). E, H: Ratio images of (E) [D9-PC32:0+Na]+:[PC32:0+Na]+ and (H) [D9-PC32:1+Na]+:[PC32:1+Na]+. Part-per-million (ppm) mass errors are indicated in parentheses. All images were visualized using total-ion-current normalization and using hotspot removal (high quantile = 99%). DPPC = PC16:0/16:0. U13C-DPPC, universally 13C-labeled dipalmitoyl PC; PC, phosphatidylcholine; MSI, mass spectrometry imaging; H&E, hematoxylin and eosin. Fig 1-3, Fig S1-S3, S5
757.4167	[M+H-H2O]+ PPM:17.9	Mus musculus	Left upper arm	MALDI (CHCA)	357_l_total ion count - Limb defect imaging - Monash University Resolution: 50μm, 97x131 Description Diseased
775.4087	[M+H]+ PPM:6.5	Mus musculus	Left upper arm	MALDI (CHCA)	357_l_total ion count - Limb defect imaging - Monash University Resolution: 50μm, 97x131 Description Diseased
792.4357	[M+NH4]+ PPM:5.8	Mus musculus	Left upper arm	MALDI (CHCA)	357_l_total ion count - Limb defect imaging - Monash University Resolution: 50μm, 97x131 Description Diseased
774.422	[M-H2O+NH4]+ PPM:9.9	Mus musculus	Lung	MALDI (DHB)	image5 - MTBLS2075 Resolution: 40μm, 163x183 Description Supplementary Figure S8. MALDI-MSI data of mouse lung tissue administered with D9-choline and U 13C-DPPC–containing Poractant alfa surfactant (labels administered 18 h prior to sacrifice). Ion images of (a) m/z 796.6856 ([U13C-DPPC+Na]+), (b) m/z 756.5154 [PC32:0+Na]+ and (c) m/z 765.6079 ([D9-PC32:0+Na]+). (d) Overlay image of [U13C-DPPC+Na]+ (red) and [D9-PC32:0+Na]+ (green). Parts per million (ppm) mass errors are indicated in parentheses. All images were visualised using totalion-current normalisation and using hotspot removal (high quantile = 99%). DPPC = PC16:0/16:0.
739.3907	[M+H-2H2O]+ PPM:2.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_7 - MTBLS385 Resolution: 75μm, 69x54 Description
797.3917	[M+Na]+ PPM:5	Mus musculus	brain	MALDI (DHB)	Brain01_Bregma-3-88b_centroid - MTBLS313 Resolution: 17μm, 265x320 Description
797.3924	[M+Na]+ PPM:4.1	Mus musculus	brain	MALDI (DHB)	Brain01_Bregma1-42_02_centroid - MTBLS313 Resolution: 17μm, 434x258 Description
797.3922	[M+Na]+ PPM:4.3	Mus musculus	brain	MALDI (DHB)	Brain01_Bregma1-42_01_centroid - MTBLS313 Resolution: 17μm, 447x118 Description
797.392	[M+Na]+ PPM:4.6	Mus musculus	brain	MALDI (DHB)	Brain02_Bregma1-42_03 - MTBLS313 Resolution: 17μm, 483x403 Description
775.4035	[M+H]+ PPM:13.2	Mus musculus	brain	MALDI (DHB)	Brain02_Bregma-3-88 - MTBLS313 Resolution: 17μm, 288x282 Description
797.392	[M+Na]+ PPM:4.6	Mus musculus	brain	MALDI (DHB)	Brain02_Bregma-1-46 - MTBLS313 Resolution: 17μm, 294x399 Description

Angiotensin IV is one of the N-terminal angiotensin degradation products of angiotensin II. Angiotensin IV (AngIV) mediates important physiologic functions in the central nervous system, including blood flow regulation, processes underlying to learning and memory, and presents anticonvulsant activity. The presence of AngIV-specific binding sites has been identified in various mammalian tissues, including blood vessels, heart, kidney, and brain. Besides the presence of AngIV binding sites in the cardiovascular system, the major AngIV synthesizing enzymes aminopeptidase N (APN) and aminopeptidase B (APB) are also expressed in different cell types of this system. AngIV activates several protein kinases, including phosphatidylinositol 3 kinase, PI-dependent kinase-1, extracellular signal-related kinases (ERK), protein kinase B-α/Akt, and p70 ribosomal S6 kinase. AngIV could contribute to vascular damage, increasing the production of monocyte chemoattractant protein-1, the main chemokine involved in monocyte recruitment, and up-regulates the expression of the adhesion molecule intercellular adhesion molecule-1 that is involved in the attachment and transmigration of circulating cells into the damaged tissue. (PMID: 17210474) [HMDB] Angiotensin IV is one of the N-terminal angiotensin degradation products of angiotensin II. Angiotensin IV (AngIV) mediates important physiologic functions in the central nervous system, including blood flow regulation, processes underlying to learning and memory, and presents anticonvulsant activity. The presence of AngIV-specific binding sites has been identified in various mammalian tissues, including blood vessels, heart, kidney, and brain. Besides the presence of AngIV binding sites in the cardiovascular system, the major AngIV synthesizing enzymes aminopeptidase N (APN) and aminopeptidase B (APB) are also expressed in different cell types of this system. AngIV activates several protein kinases, including phosphatidylinositol 3 kinase, PI-dependent kinase-1, extracellular signal-related kinases (ERK), protein kinase B-α/Akt, and p70 ribosomal S6 kinase. AngIV could contribute to vascular damage, increasing the production of monocyte chemoattractant protein-1, the main chemokine involved in monocyte recruitment, and up-regulates the expression of the adhesion molecule intercellular adhesion molecule-1 that is involved in the attachment and transmigration of circulating cells into the damaged tissue. (PMID: 17210474). D006730 - Hormones, Hormone Substitutes, and Hormone Antagonists > D006728 - Hormones COVID info from COVID-19 Disease Map Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS