Infrared Spectrum of Hydrogen Sulfide from 2200–2800 cm−1

1956 ◽  
Vol 24 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Harry C. Allen ◽  
L. R. Blaine ◽  
Earle K. Plyer ◽  
Paul C. Cross
1955 ◽  
Vol 23 (3) ◽  
pp. 541-543 ◽  
Author(s):  
Girard L. Ordway ◽  
Paul C. Cross ◽  
Edward J. Bair

1992 ◽  
Vol 96 (3) ◽  
pp. 2044-2047 ◽  
Author(s):  
T. Daniel Crawford ◽  
Neil A. Burton ◽  
Henry F. Schaefer

1957 ◽  
Vol 27 (1) ◽  
pp. 179-181 ◽  
Author(s):  
Carleton M. Savage ◽  
T. Harvey Edwards

1954 ◽  
Vol 22 (6) ◽  
pp. 1104-1107 ◽  
Author(s):  
Harry C. Allen ◽  
Earle K. Plyler

1969 ◽  
Vol 73 (10) ◽  
pp. 3518-3520 ◽  
Author(s):  
William C. Waggener ◽  
Arthur J. Weinberger ◽  
Raymond W. Stoughton

1956 ◽  
Vol 25 (6) ◽  
pp. 1132-1136 ◽  
Author(s):  
Harry C. Allen ◽  
Earle K. Plyler

2019 ◽  
Vol 133 (20) ◽  
pp. 2045-2059 ◽  
Author(s):  
Da Zhang ◽  
Xiuli Wang ◽  
Siyao Chen ◽  
Selena Chen ◽  
Wen Yu ◽  
...  

Abstract Background: Pulmonary artery endothelial cell (PAEC) inflammation is a critical event in the development of pulmonary arterial hypertension (PAH). However, the pathogenesis of PAEC inflammation remains unclear. Methods: Purified recombinant human inhibitor of κB kinase subunit β (IKKβ) protein, human PAECs and monocrotaline-induced pulmonary hypertensive rats were employed in the study. Site-directed mutagenesis, gene knockdown or overexpression were conducted to manipulate the expression or activity of a target protein. Results: We showed that hydrogen sulfide (H2S) inhibited IKKβ activation in the cell model of human PAEC inflammation induced by monocrotaline pyrrole-stimulation or knockdown of cystathionine γ-lyase (CSE), an H2S generating enzyme. Mechanistically, H2S was proved to inhibit IKKβ activity directly via sulfhydrating IKKβ at cysteinyl residue 179 (C179) in purified recombinant IKKβ protein in vitro, whereas thiol reductant dithiothreitol (DTT) reversed H2S-induced IKKβ inactivation. Furthermore, to demonstrate the significance of IKKβ sulfhydration by H2S in the development of PAEC inflammation, we mutated C179 to serine (C179S) in IKKβ. In purified IKKβ protein, C179S mutation of IKKβ abolished H2S-induced IKKβ sulfhydration and the subsequent IKKβ inactivation. In human PAECs, C179S mutation of IKKβ blocked H2S-inhibited IKKβ activation and PAEC inflammatory response. In pulmonary hypertensive rats, C179S mutation of IKKβ abolished the inhibitory effect of H2S on IKKβ activation and pulmonary vascular inflammation and remodeling. Conclusion: Collectively, our in vivo and in vitro findings demonstrated, for the first time, that endogenous H2S directly inactivated IKKβ via sulfhydrating IKKβ at Cys179 to inhibit nuclear factor-κB (NF-κB) pathway activation and thereby control PAEC inflammation in PAH.


Sign in / Sign up

Export Citation Format

Share Document