ZFIN ID: ZDB-PUB-030106-6
Partial sequence of a transferrin homolog from Danio rerio (zebrafish)
Moczydlowski, E., Berliner, N., Benz, E.J. Jr., Zon, L., Blakaj, D., Barnes, B., Ruck, B., and Leach, T.M.
Date: 1999
Source: Bull. Mt. Desert Isl. Biol. Lab.   38: 3-4 (Other)
Registered Authors: Moczydlowski, Edward, Zon, Leonard I.
Keywords: Proteins; Blood; Iron; Disease resistance; Danio rerio, transferrins; Zebra danio
MeSH Terms: none
PubMed: none
Transferrin (Tf) is a vertebrate plasma protein that binds two Fe super(3+) ions in a bicarbonate dependent fashion. Tf functions in the transport and delivery of iron to cells via transferrin receptor-mediated endocytosis. As iron is required for the growth of many bacteria and free Fe super(3+)/Fe super(2+) is involved in the generation of chemically damaging hydroxyl free radicals, Tf also functions to limit bacterial infections and protect against iron toxicity. Lactoferrin (Lf) is an Fe super(3+)-binding homolog of Tf present in milk and secretions that bathe mucosal surfaces. Lf is also secreted by neutrophils and is believed to play a role in modulation of immune and inflammatory responses.