Functional Switching ofAmphitrite ornataDehaloperoxidase from O2-Binding Globin to Peroxidase Enzyme Facilitated by Halophenol Substrate and H2O2

Biochemistry ◽  
2010 ◽  
Vol 49 (29) ◽  
pp. 6064-6069 ◽  
Author(s):  
Jing Du ◽  
Masanori Sono ◽  
John H. Dawson
Author(s):  
Sunmi Lee ◽  
Eun-Kyung Lee ◽  
Dong Hoon Kang ◽  
Jiyoung Lee ◽  
Soo Hyun Hong ◽  
...  

AbstractGlutathione peroxidase (GPx) is a selenocysteine-containing peroxidase enzyme that defends mammalian cells against oxidative stress, but the role of GPx signaling is poorly characterized. Here, we show that GPx type 1 (GPx1) plays a key regulatory role in the apoptosis signaling pathway. The absence of GPx1 augmented TNF-α-induced apoptosis in various RIPK3-negative cancer cells by markedly elevating the level of cytosolic H2O2, which is derived from mitochondria. At the molecular level, the absence of GPx1 led to the strengthened sequential activation of sustained JNK and caspase-8 expression. Two signaling mechanisms are involved in the GPx1-dependent regulation of the apoptosis pathway: (1) GPx1 regulates the level of cytosolic H2O2 that oxidizes the redox protein thioredoxin 1, blocking ASK1 activation, and (2) GPx1 interacts with TRAF2 and interferes with the formation of the active ASK1 complex. Inducible knockdown of GPx1 expression impaired the tumorigenic growth of MDA-MB-231 cells (>70% reduction, P = 0.0034) implanted in mice by promoting apoptosis in vivo. Overall, this study reveals the apoptosis-related signaling function of a GPx family enzyme highly conserved in aerobic organisms.


Author(s):  
Sotaro Yamasaki ◽  
Mitsuo Shoji ◽  
Megumi Kayanuma ◽  
Vladimir Sladek ◽  
Daniel Ken Inaoka ◽  
...  

Author(s):  
Navneet Singh Khetrapal ◽  
David Deibert ◽  
Rhitankar Pal ◽  
Ling Fung Cheung ◽  
Lai-Sheng Wang ◽  
...  

2019 ◽  
Vol 305 ◽  
pp. S32
Author(s):  
A. Schenkmayerova ◽  
G. Pinto ◽  
M. Marek ◽  
M. Toul ◽  
L. Hernychova ◽  
...  
Keyword(s):  

1999 ◽  
Vol 121 (47) ◽  
pp. 11006-11007 ◽  
Author(s):  
Masahito Kodera ◽  
Kou Katayama ◽  
Yoshimitsu Tachi ◽  
Koji Kano ◽  
Shun Hirota ◽  
...  

1982 ◽  
Vol 99 (1) ◽  
pp. 447-467
Author(s):  
MICHÈLE G. WHEATLY ◽  
B. R. MCMAHON

The effect of 48 h of hypersaline exposure (25, 50 and 75% SW) on haemocyanin oxygenation properties in the euryhaline crayfish Pacifastacus leniusculus was investigated in vitro and in vivo. In vitro significant increases in affinity and cooperativity were measured, although the magnitude of the Bohr shift was unaffected. In vitro dialysis of haemolymph against physiological salines of variable ionic composition proved that these changes were only partly attributable to altered levels of haemolymph ions, implicating the existence of modulators other than H+ and inorganic ions, the possible identities of which are discussed. Significant depressions of both pre- and postbranchial oxygen tensions (Pv, Ov, O2 and Pa, Oa, O2) were observed, but O2 delivery was maintained by utilization of the venous reserve and by an increase in haemocyanin O2 affinity. This occurred despite a concomitant acidosis whose effect on O2 affinity was directly opposed by the ‘salt’ effect. Under hypersaline conditions, haemocyanin played an increasingly important role in O2 delivery in vivo. Despite a reduction in the concentration of combined O2 at complete saturation of the pigment (CmaxHCyOHCyO2). indicating lowered haemocyanin concentration, compensatory changes in O2-binding and cardiac output precluded an impairment to O2 transfer. Equilibration at the tissues (Et,Ot,O2) in FW was less effective than at the gills (Eb,Ob,O2 but progressively improved with hypersaline exposure reversing this trend. Although effects of increased salinity on O2 equilibrium characteristics were qualitatively similar in vivo and in vitro, some interesting quantitative differences are discussed.


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