Siderocalin

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Siderocalin is a protein that is produced by the body in response to bacterial infection. During an infection, bacteria produce iron-chelators called siderophores, which are used for 'stealing' iron from the host. E. coli, for example, produces a catecholate type of siderophore called Enterobactin (also known as enterochelin when glycosylated) that binds iron(III) strongly (the binding constant K is approximately 1052 M−1). Siderocalin has been shown to bind ferric-catecholates, one of which is enterobactin [1] and hence prevents the iron from being delivered to the bacteria. It thus can be seen as part of an innate immune response for protection against infection.

Origin

Siderocalin (also known as neutrophil gelatinase-associated lipocalin (NGAL) or human neutrophil lipocalin) is part of a family of proteins known as lipocalins, which are small extracellular proteins that bind to small (usually hydrophobic) molecules. Many lipocalins bind to retinol (also known as vitamin A) and are involved in the transport of retinol.[2] It is only in recent years that NGAL has been recognised as a scavenger of siderophores. This discovery resulted in its new name siderocalin (sidero for siderophore, calin for lipocalin).[1]

References

  1. ↑ 1.0 1.1 D.H. Goetz, M.A. Holmes, N. Borregaard, M.E. Bluhm, M.E., K.N. Raymond, R.K. Strong. Mol. Cell, 2002, 10, 1033–1043.
  2. ↑ B. Akerstrom, D.R. Flower, J.P. Salier. Biochim. et Biophys. Acta, 2000, 1482, 1-8.
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