Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Michael T. Wilson"'
Publikováno v:
Free Radical Biology & Medicine
Covalent hemoglobin binding to membranes leads to band 3 (AE1) clustering and the removal of erythrocytes from the circulation; it is also implicated in blood storage lesions. Damaged hemoglobin, with the heme being in a redox and oxygen-binding inac
Autor:
Rebecca S. Silkstone, Gary Silkstone, Kristian Kallberg, Leif Bülow, Khuanpiroon Ratanasopa, Michael T. Wilson, Brandon J. Reeder, Chris E. Cooper, Michelle Simons, Andrea Mozzarelli, Luca Ronda
Publikováno v:
Biochemical Journal
Hemoglobin (Hb)-based oxygen carriers (HBOC) have been engineered to replace or augment the oxygen-carrying capacity of erythrocytes. However, clinical results have generally been disappointing due to adverse side effects linked to intrinsic heme-med
Autor:
Brandon J. Reeder, Michael T. Wilson
Publikováno v:
Chemical Research in Toxicology. 18:1004-1011
The heme group of myoglobin can form a covalent bond to the protein when met (ferric) myoglobin is reacted with peroxides under acidic conditions. This heme to protein cross-linked species is highly pro-oxidant and found in the urine of patients with
Publikováno v:
The Biochemical journal. 434(3)
Cytoglobin is a recently discovered hexa-co-ordinate haemoglobin that does not appear to function as a classical oxygen-binding protein. Its function is unknown and studies on the effects of changes in its expression have not decisively determined it
Autor:
Francesca Cutruzzolà, Brandon J. Reeder, Michael T. Wilson, Nicholas J. Watmough, Maria Giulia Bigotti
Publikováno v:
IUBMB life. 59(8-9)
Peroxide-induced oxidative modifications of haem proteins such as myoglobin and haemoglobin can lead to the formation of a covalent bond between the haem and globin. These haem to protein cross-linked forms of myoglobin and haemoglobin are cytotoxic
Publikováno v:
Free radical biologymedicine. 44(3)
Iron chelators such as desferrioxamine have been shown to ameliorate oxidative damage in vivo. The mechanism of this therapeutic action under non-iron-overload conditions is, however, complex, as desferrioxamine has properties that can impact on oxid
Autor:
Béatrice Faivre, Michael T. Wilson, Abdu I. Alayash, Jacqueline Dunne, Radu Silaghi-Dumitrescu, Alexis Caron, Chris E. Cooper, Patrick Menu, Paul W. Buehler
Publikováno v:
The Biochemical journal. 399(3)
Haemoglobin initiates free radical chemistry. In particular, the interactions of peroxides with the ferric (met) species of haemoglobin generate two strong oxidants: ferryl iron and a protein-bound free radical. We have studied the endogenous defence
Publikováno v:
Biochemistry. 41(1)
At acidic pH values heme-protein cross-linked myoglobin (Mb-H) forms as a product of a peroxide-induced ferric-ferryl redox cycle. There is evidence that this molecule acts as a marker for heme-protein-induced oxidative stress in vivo and may exacerb