Faculty Opinions recommendation of HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing.

Author(s):  
Patrick H. O'Farrell
Science ◽  
2001 ◽  
Vol 292 (5516) ◽  
pp. 464-468 ◽  
Author(s):  
M. Ivan ◽  
K. Kondo ◽  
H. Yang ◽  
W. Kim ◽  
J. Valiando ◽  
...  

2017 ◽  
Vol 595 (18) ◽  
pp. 6091-6120 ◽  
Author(s):  
Lin Gao ◽  
Victoria Bonilla-Henao ◽  
Paula García-Flores ◽  
Ignacio Arias-Mayenco ◽  
Patricia Ortega-Sáenz ◽  
...  

1982 ◽  
Vol 79 (23) ◽  
pp. 7180-7184 ◽  
Author(s):  
R. K. Chopra ◽  
V. S. Ananthanarayanan

2021 ◽  
Vol 111 ◽  
pp. 189-200
Author(s):  
Gioele Capillo ◽  
Giacomo Zaccone ◽  
Camila Cupello ◽  
Jorge Manuel Oliveira Fernandes ◽  
Kiron Viswanath ◽  
...  
Keyword(s):  

2006 ◽  
Vol 128 (4) ◽  
pp. 405-411 ◽  
Author(s):  
Patricia Ortega-Sáenz ◽  
Alberto Pascual ◽  
Raquel Gómez-Díaz ◽  
José López-Barneo

Hemeoxygenase-2 (HO-2) is an antioxidant enzyme that can modulate recombinant maxi-K+ channels and has been proposed to be the acute O2 sensor in the carotid body (CB). We have tested the physiological contribution of this enzyme to O2 sensing using HO-2 null mice. HO-2 deficiency leads to a CB phenotype characterized by organ growth and alteration in the expression of stress-dependent genes, including the maxi-K+ channel α-subunit. However, sensitivity to hypoxia of CB is remarkably similar in HO-2 null animals and their control littermates. Moreover, the response to hypoxia in mouse and rat CB cells was maintained after blockade of maxi-K+ channels with iberiotoxin. Hypoxia responsiveness of the adrenal medulla (AM) (another acutely responding O2-sensitive organ) was also unaltered by HO-2 deficiency. Our data suggest that redox disregulation resulting from HO-2 deficiency affects maxi-K+ channel gene expression but it does not alter the intrinsic O2 sensitivity of CB or AM cells. Therefore, HO-2 is not a universally used acute O2 sensor.


2004 ◽  
Vol 385 (3-4) ◽  
Author(s):  
S. L. Archer ◽  
X.-C. Wu ◽  
B. Thébaud ◽  
R. Moudgil ◽  
K. Hashimoto ◽  
...  

Author(s):  
Vanessa D. Chaplin ◽  
Alexandra N. Barbato ◽  
Michael J. Knapp
Keyword(s):  

1981 ◽  
Vol 8 (2) ◽  
pp. 121
Author(s):  
PC Pollard ◽  
GB Fincher

Suspension-cultured endosperm cells from L. multiflorum secrete into the medium an arabinogalactan-protein in which the protein moiety is rich in hydroxyproline. When cells are grown in the presence of proline labelled with 14C or 3H, the imino acid is rapidly removed from the medium and radio- activity can subsequently be detected in extracellular trichloracetic acid-soluble, ethanol-insoluble material. In this fraction, which contains the arabinogalactan-protein and other polysaccharides, radioactive label is distributed between proline and hydroxyproline. α,α'-Dipyridyl, a chelator of ferrous ion, has no effect on the total radioactivity secreted but markedly alters the distribution of radioactivity in favour of peptidyl proline. Although this inhibition of peptidyl proline hydroxylation can be reversed by ferrous or zinc ions, it is not possible to conclude that ferrous ion, which is required for hydroxylation in other systems, participates specifically in the reaction in ryegrass endosperm cells. Concomitant with the inhibition of proline hydroxylation, α,α'-dipyridyl suppresses the biosynthesis or secretion of extracellular arabinogalactan-protein and arabinoxylan.


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