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Tytuł pozycji:

p32-Dependent p38 MAPK Activation by Arginase II Downregulation Contributes to Endothelial Nitric Oxide Synthase Activation in HUVECs.

Tytuł:
p32-Dependent p38 MAPK Activation by Arginase II Downregulation Contributes to Endothelial Nitric Oxide Synthase Activation in HUVECs.
Autorzy:
Koo BH; Department of Biological Sciences, Kangwon National University, Chuncheon, Gangwon 24341, Korea.
Won MH; Department of Neurobiology, School of Medicine, Kangwon National University, Chuncheon, Gangwon 24341, Korea.
Kim YM; Department of Molecular and Cellular Biochemistry, School of Medicine, Kangwon National University, Chuncheon, Gangwon 24341, Korea.
Ryoo S; Department of Biological Sciences, Kangwon National University, Chuncheon, Gangwon 24341, Korea.
Źródło:
Cells [Cells] 2020 Feb 08; Vol. 9 (2). Date of Electronic Publication: 2020 Feb 08.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Original Publication: Basel, Switzerland : MDPI
MeSH Terms:
Down-Regulation*/drug effects
Arginase/*genetics
Human Umbilical Vein Endothelial Cells/*metabolism
Mitochondrial Proteins/*metabolism
Nitric Oxide Synthase Type III/*metabolism
p38 Mitogen-Activated Protein Kinases/*metabolism
Animals ; Aorta/metabolism ; Arginase/metabolism ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Carrier Proteins ; Cholesterol, Dietary ; Enzyme Activation/drug effects ; Human Umbilical Vein Endothelial Cells/drug effects ; Humans ; Mice, Inbred C57BL ; Nitric Oxide/biosynthesis ; Phosphorylation/drug effects ; Phosphoserine/metabolism ; Protein Kinase Inhibitors/pharmacology ; Proto-Oncogene Proteins c-akt/metabolism ; Reactive Oxygen Species/metabolism ; Vasodilation/drug effects
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Contributed Indexing:
Keywords: arginase II; calcium; endothelial nitric oxide synthase; p32; p38 MAPK
Substance Nomenclature:
0 (C1QBP protein, human)
0 (Carrier Proteins)
0 (Cholesterol, Dietary)
0 (Mitochondrial Proteins)
0 (Protein Kinase Inhibitors)
0 (Reactive Oxygen Species)
17885-08-4 (Phosphoserine)
31C4KY9ESH (Nitric Oxide)
EC 1.14.13.39 (Nitric Oxide Synthase Type III)
EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
EC 3.5.3.1 (Arginase)
SY7Q814VUP (Calcium)
Entry Date(s):
Date Created: 20200213 Date Completed: 20210210 Latest Revision: 20211204
Update Code:
20240105
PubMed Central ID:
PMC7072651
DOI:
10.3390/cells9020392
PMID:
32046324
Czasopismo naukowe
Arginase II reciprocally regulates endothelial nitric oxide synthase (eNOS) through a p32-dependent Ca 2+ control. We investigated the signaling pathway of arginase II-dependent eNOS phosphorylation. Western blot analysis was applied for examining protein activation and [Ca 2+ ]c was analyzed by microscopic and FACS analyses. Nitric oxide (NO) and reactive oxygen species (ROS) productions were measured using specific fluorescent dyes under microscopy. NO signaling pathway was tested by measuring vascular tension. Following arginase II downregulation by chemical inhibition or gene knockout (KO, ArgII -/- ), increased eNOS phosphorylation at Ser1177 and decreased phosphorylation at Thr495 was depend on p38 MAPK activation, which induced by CaMKII activation through p32-dependent increase in [Ca 2+ ]c. The protein amount of p32 negatively regulated p38 MAPK activation. p38 MAPK contributed to Akt-induced eNOS phosphorylation at Ser1177 that resulted in accelerated NO production and reduced reactive oxygen species production in aortic endothelia. In vascular tension assay, p38 MAPK inhibitor decreased acetylcholine-induced vasorelaxation responses and increased phenylephrine-dependent vasoconstrictive responses. In ApoE -/- mice fed a high cholesterol diet, arginase II inhibition restored p32/CaMKII/p38 MAPK/Akt/eNOS signaling cascade that was attenuated by p38 MAPK inhibition. Here, we demonstrated a novel signaling pathway contributing to understanding of the relationship between arginase II, endothelial dysfunction, and atherogenesis.
Competing Interests: The authors declare no conflict of interest.
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