The nitration of proteins in platelets.
Nitric oxide has many important physiological functions, but it may also form an important oxidant, peroxynitrite, as a consequence of its reaction with superoxide anions. Peroxynitrite is capable of nitrating the aromatic amino acids in proteins, particularly tyrosine. Nitrated proteins are found in tissues of a variety of diseases where inflammation occurs. However, our recent work suggests that more selective nitration of specific proteins may occur during normal physiological processes, such as platelet activation by collagen. It is not yet clear what role this may play in the normal cell biology, but there is potential to be a role in signal transduction mechanisms, possibly by influencing tyrosine phosphorylation or dephosphorylation.
Bruckdorfer
K R
KR
Department of Biochemistry and Molecular Biology, University College London (Royal Free Campus), Rowland Hill Street, London NW3 2PF, United Kingdom. bruckd@rfc.ucl.ac.uk
D000818:Animals; D001792:Blood Platelets / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D006801:Humans; D007249:Inflammation / Q000097:blood; D009569:Nitric Oxide / Q000097:blood*; D030421:Peroxynitrous Acid / Q000097:blood; D015539:Platelet Activation; D013481:Superoxides / Q000097:blood
D001798:Blood Proteins; D013481:Superoxides; D030421:Peroxynitrous Acid; D009569:Nitric Oxide