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Insect transferrins: Multifunctional proteins

期刊

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1820, 期 3, 页码 437-451

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ELSEVIER
DOI: 10.1016/j.bbagen.2011.07.011

关键词

Development; Ferritin; Immunity; Insect; Oxidative stress; Transferrin

资金

  1. Agricultural Experiment Station
  2. College of Agriculture and Life Sciences at the University of Arizona

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Background: Many studies have been done evaluating transferrin in insects. Genomic analyses indicate that insects could have more than one transferrin. However, the most commonly studied insect transferrin, Tsf1, shows greatest homology to mammalian blood transferrin. Scope of review: Aspects of insect transferrin structure compared to mammalian transferrin and the roles transferrin serves in insects are discussed in this review. Major conclusions: Insect transferrin can have one or two lobes, and can bind iron in one or both. The iron binding ligands identified for the lobes of mammalian blood transferrin are generally conserved in the lobes of insect transferrins that have an iron binding site. Available information supports that the form of dietary iron consumed influences the regulation of insect transferrin. Although message is expressed in several tissues in many insects, fat body is the likely source of hemolymph transferrin. Insect transferrin is a vitellogenic protein that is down-regulated by Juvenile Hormone. It serves a role in transporting iron to eggs in some insects, and transferrin found in eggs appears to be endowed from the female. In addition to the roles of transferrin in iron delivery, this protein also functions to reduce oxidative stress and to enhance survival of infection. General significance: Future studies in Tsfl as well as the other insect transferrins that bind iron are warranted because of the roles of transferrin in preventing oxidative stress, enhancing survival to infections and delivering iron to eggs for development. This article is part of a Special Issue entitled Transferrins: Molecular mechanisms of iron transport and disorders. (C) 2011 Elsevier B.V. All rights reserved.

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