Arrest of cytochrome-c oxidase synthesis coordinated with catabolic arrest in dormant Artemia embryos

1990 ◽  
Vol 258 (5) ◽  
pp. R1184-R1191 ◽  
Author(s):  
G. E. Hofmann ◽  
S. C. Hand

We have examined cytochrome-c oxidase (COX) biosynthesis in brine shrimp (Artemia franciscana) embryos during preemergence development (PED), as well as its inhibition under anaerobic dormancy, to determine whether transitions in intracellular pH (pHi) have a regulatory influence on anabolic processes. Under control aerobic conditions (embryo pHi greater than or equal to 7.9), incorporation of radiolabeled amino acids shows that substantial biosynthesis of COX occurs during 12 h of PED (500% increase when corrected for enzyme turnover). This anabolic process is blocked under anoxia, a condition known to foster intracellular acidification (pHi less than or equal to 6.8). The arrest of COX synthesis is quantitatively identical when embryos are incubated aerobically during artifical acidification with CO2 (pHi = 6.8). The data suggest that pHi, directly or indirectly, is a regulator of protein synthesis in Artemia embryos during anaerobic dormancy. Previous work has established a fundamental role for pHi in the arrest of carbohydrate catabolism under anoxia. Thus there appears to be a coordinated suppression of energy-producing and energy-utilizing events as Artemia embryos enter quiescence that involves pHi as the common intracellular signal.

1995 ◽  
Vol 270 (43) ◽  
pp. 25363-25369 ◽  
Author(s):  
Henry Speno ◽  
M. Reza Taheri ◽  
Derek Sieburth ◽  
Craig T. Martin

1983 ◽  
Vol 210 (1) ◽  
pp. 199-205 ◽  
Author(s):  
G Proteau ◽  
J M Wrigglesworth ◽  
P Nicholls

1. Oxidation of ferrocytochrome c by cytochrome c oxidase incorporated into proteoliposomes induces a transient acidification of the external medium. This change is dependent on the presence of valinomycin and can be abolished by carbonyl cyanide p-trifluoromethoxyphenylhydrazone or by nigericin. The H+/e- ratio for the initial acidification varies with the internal buffering capacity of the vesicles, and under suitable conditions approaches + 1, the pulse slowly decaying to give a net alkalinity change with H+/e- value approaching −1. 2. Inhibition of cytochrome c oxidase turnover by ferricytochrome c or by azide addition results in ferrocytochrome c-dependent H+ pulses with decreasing H+/e- ratios. The rate of the initial H+ production remains higher than the rate of equilibration of the pH gradient, indicating an intrinsic dependence of the H+/e- ratio on enzyme turnover. The final net alkalinity changes are relatively unaffected by turnover inhibition.


Sign in / Sign up

Export Citation Format

Share Document