Lactoferrin

Baker, Edward N.; Baker, Heather M.

doi:10.1007/s00018-005-5368-9

Cited by 326 publications

(141 citation statements)

References 53 publications

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“…In adults, higher levels of lactoferrin are present in milk and colostrum (Masson and Heremans, 1971;Brock, 1980). It is also found in most mucosal secretions such as uterine fluid, vaginal secretion, seminal fluid, saliva, bile, pancreatic juice, small intestine secretions, nasal secretion, and tears (Masson et al, 1966;Baker, 1994;Levay and Viljoen, 1995;Lonnerdal and Iyer, 1995;Kikuchi et al, 2003;Baker and Baker, 2005).…”

Section: Sources Of Lactoferrin In the Organismmentioning

confidence: 99%

Lactoferrin: a review

Adlerova¹,

Bartošková²,

Faldyna³

2008

Vet. Med.

267

217

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This review discusses the biological properties of the glycoprotein lactoferrin. Lactoferrin has been identified in secretions from exocrine glands and in specific granules of neutrophils. After degranulation, neutrophils become the main source of lactoferrin in blood plasma. Lactoferrin possesses various biological functions, including roles in iron metabolism, cell proliferation and differentiation, and antibacterial, antiviral, and antiparasitic activity. Many of these functions do not appear to be connected with its iron binding ability. Of late, lactoferrin concentrations have been measured mostly in humans but also in some other species. However, the relationship between its concentration and physiological or pathological effects on body functions is not yet well characterised.

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Section: Sources Of Lactoferrin In the Organismmentioning

confidence: 99%

Lactoferrin: a review

Adlerova¹,

Bartošková²,

Faldyna³

2008

Vet. Med.

267

217

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“…Thus, compared with Lf, its secretory counterpart, ⌬Lf is a 73-kDa cytoplasmic protein able to enter the nucleus (30). Potential DNA-binding domains have been suggested for Lf, implicating the strong concentration of positive charges at the C-terminal end of the first helix, which is truncated in ⌬Lf, and at the interlobe region (31,32).…”

Section: And O-glcnacase (Oga) Disruption Of ␤-O-linkedmentioning

confidence: 99%

“…Surprisingly, this deletion did not affect ⌬Lf transcriptional activity (Fig. 5B), suggesting that the ⌬Lf DNA-binding domain must be located at the hinge region (31,32). Because O-GlcNAcylation and phosphorylation might occur on neighboring sites, we screened the vicinity of Ser 10 and identified Ser 16 that might be used as a replacement target by kinases.…”

Section: S472ϩmentioning

confidence: 99%

O-GlcNAcylation/Phosphorylation Cycling at Ser10 Controls Both Transcriptional Activity and Stability of Δ-Lactoferrin

Hardivillé

Hoedt

Mariller

et al. 2010

Journal of Biological Chemistry

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⌬-Lactoferrin (⌬Lf) is a transcription factor that up-regulates DcpS, Skp1, and Bax genes, provoking cell cycle arrest and apoptosis. It is post-translationally modified either by O-GlcNAc or phosphate, but the effects of the O-GlcNAc/phosphorylation interplay on ⌬Lf function are not yet understood. Here, using a series of glycosylation mutants, we showed that Ser 10 is O-GlcNAcylated and that this modification is associated with increased ⌬Lf stability, achieved by blocking ubiquitin-dependent proteolysis, demonstrating that O-GlcNAcylation protects against polyubiquitination. We highlighted the 391 KSQQSSDPDPNCVD 404 sequence as a functional PEST motif responsible for ⌬Lf degradation and defined Lys 379 as the main polyubiquitin acceptor site. We next investigated the control of ⌬Lf transcriptional activity by the O-GlcNAc/phosphorylation interplay. Reporter gene analyses using the Skp1 promoter fragment containing a ⌬Lf response element showed that O-GlcNAcylation at Ser 10 negatively regulates ⌬Lf transcriptional activity, whereas phosphorylation activates it. Using a chromatin immunoprecipitation assay, we showed that O-GlcNAcylation inhibits DNA binding. Deglycosylation leads to DNA binding and transactivation of the Skp1 promoter at a basal level. Basal transactivation was markedly enhanced by 2-3-fold when phosphorylation was mimicked at Ser 10 by aspartate. Moreover, using double chromatin immunoprecipitation assays, we showed that the ⌬Lf transcriptional complex binds to the ⌬Lf response element and is phosphorylated and/or ubiquitinated, suggesting that ⌬Lf transcriptional activity and degradation are concomitant events. Collectively, our results indicate that reciprocal occupancy of Ser 10 by either O-phosphate or O-GlcNAc coordinately regulates ⌬Lf stability and transcriptional activity.

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“…Lactoferrin is a glycoprotein (80 kDa) of the transferrin family with a high affinity for iron(III) [1,2]. Lactoferrin possesses various biological functions, including antibacterial, antiviral, and antiparasitic activities [3].…”

Section: Introductionmentioning

confidence: 99%

Monitoring lactoferrin iron levels by fluorescence resonance energy transfer: a combined chemical and computational study

et al. 2014

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Abstract.Three forms of lactoferrin (Lf) that differed in their levels of iron loading (Lf, LfFe, and LfFe 2 ) were simultaneously labeled with the fluorophores AF350 and AF430. All three resulting fluorescent lactoferrins exhibited fluorescence resonance energy transfer (FRET), but they all presented different FRET patterns. Whereas only partial FRET was observed for Lf and LfFe, practically complete FRET was seen for the holo form (LfFe 2 ). For each form of metal-loaded lactoferrin, the AF350-AF430 distance varied depending on the protein conformation, which in turn depended on the level of iron loading. Thus, the FRET patterns of these lactoferrins were found to correlate with their iron loading levels. In order to gain greater insight into the number of fluorophores and the different FRET patterns observed (i.e., their iron levels), a computational analysis was performed. The results highlighted a number of lysines that have the greatest influence on the FRET profile. Moreover, despite the lack of an X-ray structure for any LfFe species, our study also showed that this species presents modified subdomain organization of the N-lobe, which narrows its iron-binding site. Complete domain rearrangement occurs during the LfFe to LfFe 2 transition. This latter study demonstrated that lactoferrin supplies iron to this bacterium, and suggested that this process occurs with no protein internalization.

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Lactoferrin

Cited by 326 publications

References 53 publications

Lactoferrin: a review

Lactoferrin: a review

O-GlcNAcylation/Phosphorylation Cycling at Ser10 Controls Both Transcriptional Activity and Stability of Δ-Lactoferrin

Monitoring lactoferrin iron levels by fluorescence resonance energy transfer: a combined chemical and computational study

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