scholarly journals Exploring the autoinhibitory domain of the electrogenic Na+ /HCO3 − transporter NBCe1-B, from residues 28 to 62

2018 ◽  
Vol 596 (16) ◽  
pp. 3637-3653 ◽  
Author(s):  
Seong-Ki Lee ◽  
Walter F. Boron
Keyword(s):  
Autoinhibitory Domain

scholarly journals Phosphorylation Sites in the Autoinhibitory Domain Participate in p70s6kActivation Loop Phosphorylation

1998 ◽  
Vol 273 (24) ◽  
pp. 14845-14852 ◽  
Author(s):  
Patrick B. Dennis ◽  
Nicholas Pullen ◽  
Richard B. Pearson ◽  
Sara C. Kozma ◽  
George Thomas
Keyword(s):  
Phosphorylation Sites ◽  
Autoinhibitory Domain

scholarly journals Identification of the Plasma Membrane Ca2+-ATPase and of Its Autoinhibitory Domain

1995 ◽  
Vol 108 (1) ◽  
pp. 105-113 ◽  
Author(s):  
F. Rasi-Caldogno ◽  
A. Carnelli ◽  
M. I. De Michelis
Keyword(s):  
Plasma Membrane ◽  
Autoinhibitory Domain

Autoinhibitory domain fragment of endothelial NOS enhances pulmonary artery vasorelaxation by the NO-cGMP pathway

2004 ◽  
Vol 286 (5) ◽  
pp. L1066-L1074 ◽  
Author(s):  
Hanbo Hu ◽  
Meiguo Xin ◽  
Leonid L. Belayev ◽  
Jianliang Zhang ◽  
Edward R. Block ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Pulmonary Artery ◽  
Lung Perfusion ◽  
Time Dependent ◽  
Autoinhibitory Domain ◽  
Cgmp Production ◽  
Enos Activity ◽  
Isolated Lung ◽  
Enos Protein

Catalytic activity of eNOS is regulated by multiple posttranscriptional mechanisms, including a 40-amino acid (604-643) autoinhibitory domain (AID) located in the reductase domain of the eNOS protein. We examined whether an exogenous synthetic AID, an 11-amino acid (626-636) fragment of AID (AAF), or scrambled AAF (AAF-SR), enhanced eNOS activity and NO-cGMP-mediated vasorelaxation using pulmonary artery (PA) endothelial/smooth muscle cell (PAEC/PASM) coculture, isolated PA segment, and isolated lung perfusion models. Incubation of isolated total membrane fraction of PAEC with AID or AAF resulted in concentration-dependent loss of eNOS activity. In contrast, incubation of intact PAEC with AID or AAF but not AAF-SR caused concentration- and time-dependent activation of eNOS. Because AID and AAF had similar effects on activation of eNOS, AAF and AAF-SR were used for further evaluation. Although AAF stimulation increased catalytic activity of PKC-α in PAEC, AAF-mediated activation of eNOS was independent of phosphorylation of Ser1177 or Thr495 and/or expression of eNOS protein. AAF stimulation of PAEC increased NO and cGMP production, which were attenuated by pretreatment with the eNOS inhibitor l-NAME. AAF caused time-dependent vasodilation of U-46619-precontracted endothelium-intact but not endothelium-denuded PA segments, and this response was attenuated by l-NAME. AAF, but not AAF-SR, also caused vasorelaxation in an ex vivo isolated mouse lung perfusion model precontracted with U-46619. Incubation with fluorescence-labeled AAF demonstrated translocation of AAF in PAEC in culture, isolated PA, and isolated intact lungs. These results demonstrate that AAF-stimulated vasodilation is mediated via activation of eNOS and enhanced NO-cGMP production in PA and intact lung.

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