The physiology of lactoferrin

Brock, Jeremy H.

doi:10.1139/o01-212

Cited by 351 publications

(254 citation statements)

References 54 publications

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“…Lactoferrin is known to have bactericidal, fungicidal, and antiviral activity as well as antitumor, anti-inflammatory and immunoregulatory properties as described in several review articles [27,28,29,30]. Most of these activities reside in the N-domain of lactoferrin [31].…”

Section: Resultsmentioning

confidence: 99%

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

et al. 2009

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Bovine lactoferrin (bLf) is a multifunctional iron-binding glycoprotein secreted mainly in milk and other secretory fluids. Bovine lactoferrin is reported to promote the growth of bifidobacteria and binding of bLf to bifidobacteria cell is thought to be involved. After separation of bLf half molecule and extraction of surface proteins from bifidobacteria, binding profiles were observed by immunoblotting. No binding was appeared when bLf C-lobe was being reacted with cell surface proteins on PVDF membrane. Conversely, a 50-kDa band was appeared when reacted with either intact bLf or nicked bLf. This result strongly suggests that binding region could be N-lobe.Moreover, blot, probed with nicked bLf, reacted with anti-lactoferricin antibody also produced a 50-kDa band that indicates the binding occurred at lactoferricin region of bLf molecule. Interestingly, despite absence of binding, bLf C-lobe can stimulate the growth of bifidobacteria.

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Section: Resultsmentioning

confidence: 99%

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

et al. 2009

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“…Lactoferrin (LF) is an 80 kg·mol −1 member of the transferrin family of iron-binding glycoproteins, which was originally found in mammalian exocrine secretions and in specific granules of polymorphonuclear leukocytes [3,11]. Human LF (hLF) is present at high concentrations (average 1 to 3.2 mg·mL −1 ) and plays a significant protective role in human milk.…”

Section: Introductionmentioning

confidence: 99%

High-level expression and production of human lactoferrin in Pichia pastoris

Jiang

Chen

Jia

et al. 2008

Dairy Sci. Technol.

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-Lactoferrin (LF) is a multifunctional iron-binding glycoprotein which is found in high concentrations in milk. Recombinant human LF (rhLF) may provide health benefits. In the present study, we report an optimization of the production system of recombinant human lactoferrin that has enabled the production of recombinant protein at levels up to 1200 mg·L −1 . The hLF was expressed in the methylotrophic yeast Pichia pastoris using the pPIC9K vector. The expression level of recombinant hLF (rhLF) was improved significantly by mixed methanol/glycerol feeding at the ratio of 4:1 during the induction phase of high cell-density fermentation. A yield of approximately 1200 mg·L −1 was obtained in fed-batch fermentation with this system, which was much higher than the reported values for other systems (1 mg·L −1 to 115 mg·L −1 ). The rhLF was purified via ionexchange chromatography using SP Sepharose TM Fast Flow and has a similar molecular mass of 80 kg·mol −1 to native hLF. The level of glycosylation of the recombinant protein is similar to that of the native protein.human lactoferrin / Pichia pastoris / high cell-density fermentation / glycosylationRésumé -Haut niveau d'expression et de production de lactoferrine humaine par Pichia pastoris. La lactoferrine (LF) est une glycoprotéine multifonctionnelle liant le fer, qui se trouve en concentration élevée dans le lait. La lactoferrine humaine recombinante (rhLF) peut être bénéfique pour la santé. Dans cette étude, nous présentons une optimisation du système de production de rhLF permettant d'obtenir des niveaux de production élevés. La lactoferrine humaine était exprimée dans la levure méthylotrophe Pichia pastoris à l'aide du vecteur pPIC9K. Le niveau d'expression de rhLF était amélioré significativement lorsque le milieu était alimenté d'un mélange méthanol/glycérol dans un ratio de 4:1 pendant la phase d'induction de la fermentation à haute densité cellulaire.

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“…Lactoferrin possesses a wide range of immunomodulatory activities [17][18][19] [20] [21] including promotion of the T-cell dominated DTH response towards BCG antigens [22,23], The ability of lactoferrin to enhance the generation of antigen specific DTH responses suggests that lactoferrin could promote development of specific T-cell responses against a complex antigen, such as BCG [24,25] The development of T-cell helper type 1 (T H 1) immunity is, in part, regulated by production of IL-12 [26,27]. A variety of in vivo studies have shown lactoferrin capable of increasing production of IL-12 [28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Lactoferrin enhanced efficacy of the BCG vaccine to generate host protective responses against challenge with virulent Mycobacterium tuberculosis

Hwang

Wilk

Budnicka

et al. 2007

Vaccine

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Tuberculosis (TB), caused by Mycobacterium tuberculosis (MTB), is a disease with world wide consequences, affecting nearly a third of the world's population. The established vaccine for TB, an attenuated strain of Mycobacterium bovis Calmette Guerin (BCG), has existed since 1921. Lactoferrin, an iron binding protein found in mucosal secretions and granules of neutrophils was hypothesized to be an ideal adjuvant to enhance the efficacy of the BCG vaccine, specifically because of previous reports of lactoferrin enhancement of IL-12 production from macrophages infected with BCG. Different vaccination protocols were investigated for generation of host protective responses against MTB infection using lactoferrin admixed to the BCG vaccine. Resulting effects demonstrate that BCG/lactoferrin increased host protection against MTB infection by decreasing organ bacterial load and reducing lung histopathology; significant reduction in tissue CFUs and pathology were observed post challenge compared to those seen with BCG alone. Addition of lactoferrin to the vaccine led to reduced pathological damage upon subsequent infection with virulent MTB, with positive results demonstrated when admixed in oil-based vehicle (incomplete Freund's adjuvant; IFA) or when given with BCG in saline. The observed post-challenge results paralleled increasing production of IFN-γ and IL-6, but only limited changes to proinflammatory mediators TNF-α or IL-1β from BCG stimulated splenocytes. Overall, these studies indicate that lactoferrin is a useful and effective adjuvant to improve efficacy of the BCG vaccine, with potential to reduce related tissue damage and pulmonary histopathology.

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The physiology of lactoferrin

Cited by 351 publications

References 54 publications

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

Bovine lactoferrin region responsible for binding to bifidobacterial cell surface proteins

High-level expression and production of human lactoferrin in Pichia pastoris

Lactoferrin enhanced efficacy of the BCG vaccine to generate host protective responses against challenge with virulent Mycobacterium tuberculosis

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