The mechanism of action of angiotensin II is dependent on direct activation of vascular smooth muscle carbonic anhydrase I

Puşcaş, I; Coltâu, Marcela; Gilau, L.; Baican, M; Pasca, R; Domuţa, Gabriela; Hecht, A

doi:10.1007/s005990070010

Cited by 3 publications

(2 citation statements)

References 20 publications

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“…Initially, angiotensinogen is produced and released into the plasma from the liver. It is cleaved by renin, which is produced by the kidneys, to form angiotensin I. Angiotensin-converting enzyme, which is distributed on the pulmonary capillary endothelium, cleaves angiotensin I to produce the octapeptide angiotensin II, which is equipped with several biological effects to mediate vasoconstriction via the specific angiotensin II receptor type 1 and type 2 [ 120 , 121 ]. Angiotensin-converting enzyme plays a critical role in regulating vasoconstriction and vessel permeability.…”

Section: Therapeutic and Molecular Interventionsmentioning

confidence: 99%

New Insights into the Immune Molecular Regulation of the Pathogenesis of Acute Respiratory Distress Syndrome

Yang

Chen

Yiang

et al. 2018

IJMS

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Acute respiratory distress syndrome is an inflammatory disease characterized by dysfunction of pulmonary epithelial and capillary endothelial cells, infiltration of alveolar macrophages and neutrophils, cell apoptosis, necroptosis, NETosis, and fibrosis. Inflammatory responses have key effects on every phase of acute respiratory distress syndrome. The severe inflammatory cascades impaired the regulation of vascular endothelial barrier and vascular permeability. Therefore, understanding the relationship between the molecular regulation of immune cells and the pulmonary microenvironment is critical for disease management. This article reviews the current clinical and basic research on the pathogenesis of acute respiratory distress syndrome, including information on the microenvironment, vascular endothelial barrier and immune mechanisms, to offer a strong foundation for developing therapeutic interventions.

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Section: Therapeutic and Molecular Interventionsmentioning

confidence: 99%

New Insights into the Immune Molecular Regulation of the Pathogenesis of Acute Respiratory Distress Syndrome

Yang

Chen

Yiang

et al. 2018

IJMS

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“…), suggesting the extracellular space subproteome is more reflective of aging effects than that of other parts of the aorta. Interestingly, 26 of these proteins are directly linked to the Ang II signaling cascade . Although, proteins with abundance changes also play significant roles in other cellular pathways, including a network of cell movement with a group of secreted extracellular proteins, apoptosis/cell cycle/proliferation, cytoskeletal, and extracellular structure, etc., which are important for vascular remodeling in aging .…”

Section: Proteomics Of Aging Aortamentioning

confidence: 99%

Can proteomics yield insight into aging aorta?

Wang

Lakatta

et al. 2013

Proteomics Clinical Apps

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The aging aorta exhibits structural and physiological changes that are reflected in the proteome of its component cells types. The advance in proteomic technologies has made it possible to analyze the quantity of proteins associated with the natural history of aortic aging. These alterations reflect the molecular and cellular mechanisms of aging and could provide an opportunity to predict vascular health. This paper focuses on whether discoveries stemming from the application of proteomic approaches of the intact aging aorta or vascular smooth muscle cells can provide useful insights. Although there have been limited studies to date, a number of interesting proteins have been identified that are closely associated with aging in the rat aorta. Such proteins, including milk fat globule-EGF factor 8(MFG-E8), matrix metalloproteinase type-2 (MMP2), and vitronectin, could be used as indicators of vascular health, or even explored as therapeutic targets for aging-related vascular diseases.

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Between‐gel reproducibility of the human cerebrospinal fluid proteome

Terry¹,

Desiderio²

2003

Proteomics

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This manuscript describes the between-gel reproducibility of the two-dimensional gel electrophoresis analysis of the human lumbar cerebrospinal fluid (CSF) proteome. This reproducibility study is a necessary component for our long-term research program that uses comparative proteomics to analyze lumbar CSF samples in a study of human idiopathic low back pain. A Protein-Plus Dodeca Cell electrophoresis apparatus and PDQuest software were used to measure the level of between-gel reproducibility of the CSF proteome. One pooled CSF sample was used to evaluate the level of within-sample, between-gel reproducibility, and a set of seven different CSF samples (CSF-1 to 7) was used to test the level of within-group and between-group variability. Differentially expressed proteins (six CSF samples versus the designated control, CSF-3) were characterized with mass spectrometry. The number of spots found in the pooled CSF sample was 490 +/- 30 (n = 10 gels); the percentage of protein spots found in those 10 gels was 92 +/- 6%, with a coefficient of variation of 6%; and a positive coefficient of correlation (r = 0.82) was found. In order to test the proof-of-principle, that set of seven CSF samples served as a test of our ability to perform reproducibility comparative proteomics, and to detect differentially expressed proteins within that set of test samples. One sample (CSF-3) served as the control for the other six to locate the differentially expressed proteins. A comparison of fifteen differentially expressed proteins found in that set of test CSF samples correlated with pathology. Matrix-assisted laser desorption/ionization-time-of-flight and electrospray ionization quadrupole ion trap mass spectrometry were used to characterize thirteen of those fifteen differentially expressed proteins. These results (reproducibility, protein characterization, set of test samples, and proof-of-principle) suggest that the analysis of human CSF two-dimensional gels can achieve a high level of within-sample and between-sample reproducibility, and that PDQuest software can measure the relative protein abundance in the human CSF proteome.

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The mechanism of action of angiotensin II is dependent on direct activation of vascular smooth muscle carbonic anhydrase I

Cited by 3 publications

References 20 publications

New Insights into the Immune Molecular Regulation of the Pathogenesis of Acute Respiratory Distress Syndrome

New Insights into the Immune Molecular Regulation of the Pathogenesis of Acute Respiratory Distress Syndrome

Can proteomics yield insight into aging aorta?

Between‐gel reproducibility of the human cerebrospinal fluid proteome

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