Heme-binding ability of bovine milk proteins

Orino, Koichi

doi:10.1007/s10534-020-00252-2

Cited by 2 publications

(6 citation statements)

References 17 publications

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“…Binding of horse ferritin and its apoferritin form, and bovine spleen ferritin to CasB Firstly, in this study, the binding analysis of horse spleen ferritin and its apoferritin, which lacks iron and heme, with PLB was performed whether due to its heme-binding capacity (9) as in CasB (2,8) (Supplementary Data 1). Puri ed commercial horse spleen ferritin is composed almost exclusively of L subunit, with an apparent molecular mass of 19 kDa, as described previously (12).…”

Section: Resultsmentioning

confidence: 99%

“…CasB has a possibility to detect heme-binding ferritin because Cas binds bovine ferritin but not its apoferritin, which lacks iron and heme, by hememediated binding (8,17). Although PL binds heme (9), horse spleen ferritin and its apoferritin form bind to PLB different from Cas, suggesting that PLB binds ferritin directly, likely through hydrophobic interactions, similar to the binding of PLB and bovine lactoferrin (10). On the other hand, CasB partly bound horse ferritin but did not bind the apoferritin form.…”

Section: Discussionmentioning

confidence: 99%

“…Poly-L-lysine (PL) also binds hemin and iron (9), but it remains unclear whether PL binds ferritin or not.…”

Section: Introductionmentioning

confidence: 99%

“…In bead methods, metal-binding protein and protein-protein interactions can be studied using beads with immobilized metal ions, brinogen, α-casein (CasB) or PL (PLB) (9,10). This study, rstly, conducted the binding analysis with PLB using commercial available horse spleen ferritin and it's apoferritin, but these bindings are independent on the iron because PLB bound apoferritin as well as holoferritin different from CasB only binding with holoferritin.…”

Section: Introductionmentioning

confidence: 99%

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Binding analysis of horse and bovine ferritins using beads immobilized with alpha-casein-: detection of ferritin binding or nonbinding with heme using alpha-casein-immobilized beads

Hasegawa¹,

Takahashi

Yoshikawa

et al. 2023

Preprint

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Ferritin, iron storage protein, binds heme on its surface although it’s physiological role has not been elucidated yet. Firstly, this study analyzed the bindings of bovine and horse spleen ferritins to beads immobilized with α-casein (CasB) with the heme-mediated ferritin-binding capacity of α-casein (Cas). These spleen ferritins were added to solutions containing CasB, and the supernatant and beads obtained by centrifugation was subjected to polyacrylamide gel electrophoresis (SDS-PAGE or Native-PAGE) to detect ferritin. In case of horse spleen ferritin, CasB partly bound ferritin, and CasB-bound ferritin was detected only in the pelleted beads before the second addition of CasB to the first supernatant obtained before washing the beads, while the amount of ferritin detected in the first and second supernatants was similar. After addition of bovine spleen ferritin to CasB, some ferritin was also detected in the pelleted beads as CasB-binding protein, and the other ferritin was also detected in the supernatant as ferritin with no heme. On the other hand, the serum ferritin in fetal bovine serum showed little binding in the binding with CasB. These results suggest the following: CasB selectively detects heme-binding ferritin in tissue and serum ferritin, circulating ferritin contains little heme, and ferritin is intracellularly compartmented in heme catabolism as well as protection against its oxidative stress.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…Poly-L-lysine (PL) also binds hemin and iron (9), but it remains unclear whether PL binds ferritin or not.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Binding analysis of horse and bovine ferritins using beads immobilized with alpha-casein-: detection of ferritin binding or nonbinding with heme using alpha-casein-immobilized beads

Hasegawa¹,

Takahashi

Yoshikawa

et al. 2023

Preprint

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“…Each examined transferrin type inhibited hemozoin formation. While both bLF and TF bind to heme, this potentially involves different mechanisms 26,27 , which may influence their respective capabilities.…”

Section: Rodent Malaria Challengementioning

confidence: 99%

Bovine lactoferrin inhibits Plasmodium berghei growth by binding to heme

Obayashi,

Kimura,

Haraguchi

et al. 2024

Preprint

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Bovine lactoferrin (bLF) is a 77 kDa glycoprotein that is abundant in bovine breast milk and exerts various bioactive functions, including antibacterial and antiviral functions. Few studies have explored bLF activity against parasites. We found that bLF affects hemozoin synthesis by binding to heme, inhibiting heme iron polymerization necessary for Plasmodium berghei ANKA survival in infected erythrocytes, and also binds to hemozoin, causing it to disassemble. In a challenge test, bLF administration inhibited the growth of murine malaria parasites compared to untreated group growth. To determine whether the iron content of bLF affects the inhibition of malaria growth, we tested bLFs containing different amounts of iron (apo-bLF, native-bLF, and holo-bLF), but found no significant difference in their effects. This indicated that the active sites were located within the bLFs themselves. Further studies showed that the C-lobe domain of bLF can inhibit hemozoin formation and the growth of P. berghei ANKA. Evaluation of pepsin degradation products of the C-lobe identified a 47-amino-acid section, C-1, as the smallest effective region that could inhibit hemozoin formation. This study highlights bLF’s potential as a novel therapeutic agent against malaria, underscoring the importance of its non-iron-dependent bioactive sites in combating parasite growth.

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Heme-binding ability of bovine milk proteins

Cited by 2 publications

References 17 publications

Binding analysis of horse and bovine ferritins using beads immobilized with alpha-casein-: detection of ferritin binding or nonbinding with heme using alpha-casein-immobilized beads

Binding analysis of horse and bovine ferritins using beads immobilized with alpha-casein-: detection of ferritin binding or nonbinding with heme using alpha-casein-immobilized beads

Bovine lactoferrin inhibits Plasmodium berghei growth by binding to heme

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