Proteomics

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Identification of NOS3 interacting proteins

ABSTRACT: The endothelial nitric oxide (NO) synthase (eNOS, or NOS3) can be activated in response to fluid shear stress and numerous agonists via cellular events such as increased intracellular Ca2+, interaction with substrate, co-factors as well as adaptor and regulatory proteins, protein phosphorylation and S-glutathionylation in addition to shuttling between distinct sub-cellular domains. While some protein interactors modulate enzymatic activity, others can be S-nitrosation targets, which are brought in close proximity to the NO source under specific conditions. The identification of proteins interacting with eNOS in human endothelial cells stimulated with serum and growth factors may provide new insight into the regulation of eNOS activity as well as NO signaling via S-nitrosation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Ilka Wittig  

LAB HEAD: Ingrid Fleming

PROVIDER: PXD013755 | Pride | 2021-09-08

REPOSITORIES: Pride

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Dataset's files

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Action DRS
161028_A16_Wdh_Mauro_eNOS_01.raw Raw
161028_A16_Wdh_Mauro_eNOS_02.raw Raw
161028_A16_Wdh_Mauro_eNOS_03.raw Raw
161028_A16_Wdh_Mauro_eNOS_10.raw Raw
161028_A16_Wdh_Mauro_eNOS_11.raw Raw
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Publications

Decreased nitric oxide (NO) bioavailability and oxidative stress are hallmarks of endothelial dysfunction and cardiovascular diseases. Although numerous proteins are S-nitrosated, whether and how changes in protein S-nitrosation influence endothelial function under pathophysiological conditions remains unknown. We report that active endothelial NO synthase (eNOS) interacts with and S-nitrosates pyruvate kinase M2 (PKM2), which reduces PKM2 activity. PKM2 inhibition increases substrate flux throu  ...[more]

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