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Homocitrulline: An Analog and Confounder Related to Citrulline

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Protein Deimination in Human Health and Disease

Abstract

A structural homolog to citrulline, homocitrulline, can be present in proteins and peptides as a product of posttranslational modification. Homocitrulline is formed nonenzymatically from lysine residues in the polypeptide chain by the action of cyanate. The latter compound is derived either from urea or, via a reaction catalyzed by the enzyme myeloperoxidase (MPO), from thiocyanate. The formation of homocitrulline is known as carbamoylation or carbamylation. In humans, this process takes place predominantly in two types of situations: uremia and inflammation. Smoking increases the circulating thiocyanate concentration and thus enhances carbamoylation of proteins.

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Authors and Affiliations

  1. Department of Clinical Chemistry, Institute of Diagnostics, University of Oulu, Oulu, FI-90014, Finland

    Sanna Turunen, Marja-Kaisa Koivula, Leila Risteli & Juha Risteli

  2. Nordlab Oulu, Oulu University Hospital, Oulu, Finland

    Marja-Kaisa Koivula, Leila Risteli & Juha Risteli

  3. Department of Neurology, University of Alabama at Birmingham and the Birmingham Veterans Administration Medical Center, Birmingham, AL, USA

    Anthony P. Nicholas

Authors
  1. Sanna Turunen
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  2. Marja-Kaisa Koivula
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  3. Anthony P. Nicholas
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  4. Leila Risteli
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  5. Juha Risteli
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Corresponding author

Correspondence to Juha Risteli .

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Editors and Affiliations

  1. Department of Neurology, University of Alabama at Birmingham and The Birmingham Veterans Administration Medical Center, Birmingham, Alabama, USA

    Anthony P. Nicholas

  2. Bascom Palmer Eye Institute, University of Miami, MIAMI, Florida, USA

    Sanjoy K. Bhattacharya

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Turunen, S., Koivula, MK., Nicholas, A.P., Risteli, L., Risteli, J. (2014). Homocitrulline: An Analog and Confounder Related to Citrulline. In: Nicholas, A., Bhattacharya, S. (eds) Protein Deimination in Human Health and Disease. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-8317-5_20

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