Dataset Information

Arginase II activity regulates cytosolic Ca²⁺ level in a p32-dependent manner that contributes to Ca²⁺-dependent vasoconstriction in native low-density lipoprotein-stimulated vascular smooth muscle cells.

ABSTRACT: Although arginase II (ArgII) is abundant in mitochondria, Ca²⁺-accumulating organelles, the relationship between ArgII activity and Ca²⁺ translocation into mitochondria and the regulation of cytosolic Ca²⁺ signaling are completely unknown. We investigated the effects of ArgII activity on mitochondrial Ca²⁺ uptake through mitochondrial p32 protein (p32m) and on CaMKII-dependent vascular smooth muscle cell (VSMC) contraction. Native low-density lipoprotein stimulation induced an increase in [Ca²⁺]m as measured by CoCl₂-quenched calcein-AM fluorescence, which was prevented by Arg inhibition in hAoSMCs and reduced in mAoSMCs from ArgII^-/- mice. Conversely, [Ca²⁺]c analyzed with Fluo-4 AM was increased by Ar

SUBMITTER: Koo BH

PROVIDER: S-EPMC6545325 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

ACCESS DATA

Dataset Information

Arginase II activity regulates cytosolic Ca²⁺ level in a p32-dependent manner that contributes to Ca²⁺-dependent vasoconstriction in native low-density lipoprotein-stimulated vascular smooth muscle cells.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Arginase II activity regulates cytosolic Ca2+ level in a p32-dependent manner that contributes to Ca2+-dependent vasoconstriction in native low-density lipoprotein-stimulated vascular smooth muscle cells.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Arginase II activity regulates cytosolic Ca²⁺ level in a p32-dependent manner that contributes to Ca²⁺-dependent vasoconstriction in native low-density lipoprotein-stimulated vascular smooth muscle cells.