Interaction of Lactoferrin with Ceruloplasmin

Захарова, Е. М.; Shavlovski, Mikhail M.; Bass, Mikhail G.; Gridasova, Anastasia A.; Pulina, M. O.; Filippis, Vincenzo De; Beltramini, Mariano; Muro, Paolo Di; Salvato, Benedetto; Fontana, Angelo; Vasilyev, V. B.; Gaitskhoki, V. S.

doi:10.1006/abbi.1999.1559

Cited by 43 publications

(42 citation statements)

References 28 publications

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“…In the case of CERU, FGN, and HSA, the large (Ͼ460 kDa) species containing these proteins detected in control plasma probably result from interactions between them and other plasma proteins. Many examples of such interactions are known; for example, lactoferrin (36), protein C (37), and myeloperoxidase (38) interact with CERU; at least 11 proteins are known to interact with FGN including vitronectin (39), histidine-rich glycoprotein (40), and apolipoprotein(a) (41); and over 60 different proteins are believed to interact with HSA (42). Self-aggregation, which has been reported for both FGN (43) and HSA (44), may also account for the detection of these proteins as larger species.…”

Section: Discussionmentioning

confidence: 99%

Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

Wyatt¹,

Wilson

2010

Journal of Biological Chemistry

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Clusterin (CLU) is an extracellular chaperone that is likely to play an important role in protein folding quality control. This study identified three deposition disease-associated proteins as major plasma clients for clusterin by studying CLU-client complexes formed in response to physiologically relevant stress (shear stress, ϳ36 dynes/cm 2 at 37°C). Analysis of plasma samples by size exclusion chromatography indicated that (i) relative to control plasma, stressed plasma contained proportionally more soluble protein species of high molecular weight, and (ii) high molecular weight species were far more abundant when proteins purified by anti-CLU immunoaffinity chromatography from stressed plasma were compared with those purified from control plasma. SDS-PAGE and Western blot analyses indicated that a variety of proteins co-purified with CLU from both stressed and control plasma; however, several proteins were uniquely present or much more abundant when plasma was stressed. These proteins were identified by mass spectrometry as ceruloplasmin, fibrinogen, and albumin. Immunodot blot analysis of size exclusion chromatography fractionated plasma suggested that CLU-client complexes generated in situ are very large and may reach >4 ؋ 10 7 Da. Lastly, sandwich enzymelinked immunosorbent assay detected complexes containing CLU and ceruloplasmin, fibrinogen, or albumin in stressed but not control plasma. We have previously proposed that CLUclient complexes serve as vehicles to dispose of damaged misfolded extracellular proteins in vivo via receptor-mediated endocytosis. A better understanding of these mechanisms is likely to ultimately lead to the identification of new therapies for extracellular protein deposition disorders.

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Section: Discussionmentioning

confidence: 99%

Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

Wyatt¹,

Wilson

2010

Journal of Biological Chemistry

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“…Human LF was isolated from breast milk by ion exchange chromatography on carboxymethyl sephadex and by gel fi ltration on sephadex G-100 [10].…”

Section: Methodsmentioning

confidence: 99%

“…We showed in vitro that CP ferroxidase activity is stimulated by lactoferrin (LF; a milk transferrin) in both the apo-form and iron-saturated form [1]. Normally, LF and CP form a stable complex; other proteins do not prevent the complex formation [8,10]. These data suggested that LF can modify CP ferroxidase activity in vivo, thus preventing iron defi ciency.…”

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confidence: 90%

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Effect of Lactoferrin on Consequences of Acute Experimental Hemorrhagic Anemia in Rats

et al. 2010

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The effect of human lactoferrin on the arrest of experimental hemorrhagic anemia consequences was studied in rats. After six blood losses (days 1-4 and 7-8 of the experiment), the rats developed acute anemia: hemoglobin concentration decreased to 59% of the initial level, serum iron level decreased 3-fold. Intraperitoneal injections of lactoferrin (10 mg/day) for 4 days starting from day 7 led to an increase in hemoglobin level to 109% and of serum iron to 125% on day 14. In controls, hemoglobin level on day 14 was 70% and iron content 49% of the initial level. Ferroxidase activity of ceruloplasmin in blood serum decreased after 5 blood losses returned to normal only in rats receiving lactoferrin. The results indicate that lactoferrin modified ceruloplasmin activity in vivo, promoting normalization of iron metabolism.

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“…LF is also highly basic with a pI of 8-9, probably due to a unique basic region in the N-terminal region of the molecule that is not found in transferrin. One important consequence of this property is that LF can bind in a "pseudospecifi c" way to many acidic molecules, including heparin and various cell surface molecules [Lampreave et al, 1990;Gasymov et al, 1999;Zakharova et al, 2000]. As discussed below, these interactions may be relevant to the physiological function of LF.…”

Section: Structure Tissue Distribution and Catabolism Of Lactoferrinmentioning

confidence: 99%

Healthy Multifunctional Spectra of Milk Glycoproteins and Their Fragments – a Review Article

Fayed¹

2012

Pol. J. Food Nutr. Sci.

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Interaction of Lactoferrin with Ceruloplasmin

Cited by 43 publications

References 28 publications

Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

Identification of Human Plasma Proteins as Major Clients for the Extracellular Chaperone Clusterin

Effect of Lactoferrin on Consequences of Acute Experimental Hemorrhagic Anemia in Rats

Healthy Multifunctional Spectra of Milk Glycoproteins and Their Fragments – a Review Article

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