The selective extraction of iron-binding glycoprotein lactoferrin via a “deferrization-restoring” SPE strategy

2020 ◽  
Vol 253 ◽  
pp. 117522
Author(s):  
Yunhang Fan ◽  
Junlan Jiang ◽  
Shunfen Song ◽  
Xuwei Chen
Keyword(s):  
Selective Extraction ◽  
Iron Binding ◽  
Binding Glycoprotein

scholarly journals Distribution of Lactoferrin Is Related with Dynamics of Neutrophils in Bacterial Infected Mice Intestine

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1496 ◽  
Author(s):  
Li Liang ◽  
Zhen-Jie Wang ◽  
Guang Ye ◽  
Xue-You Tang ◽  
Yuan-Yuan Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antimicrobial Activity ◽  
Mucosal Immunity ◽  
Mrna Levels ◽  
Iron Binding ◽  
E Coli ◽  
New Knowledge ◽  
Activated Neutrophils ◽  
Binding Glycoprotein

Lactoferrin (Lf) is a conserved iron-binding glycoprotein with antimicrobial activity, which is present in secretions that recover mucosal sites regarded as portals of invaded pathogens. Although numerous studies have focused on exogenous Lf, little is known about its expression of endogenous Lf upon bacterial infection. In this study, we investigated the distribution of Lf in mice intestine during Escherichia coli (E. coli) K88 infection. PCR and immunohistology staining showed that mRNA levels of Lf significantly increased in duodenum, ileum and colon, but extremely decreased in jejunum at 8 h and 24 h after infection. Meanwhile, endogenous Lf was mostly located in the lamina propria of intestine villi, while Lf receptor (LfR) was in the crypts. It suggested that endogenous Lf-LfR interaction might not be implicated in the antibacterial process. In addition, it was interesting to find that the infiltration of neutrophils into intestine tissues was changed similarly to Lf expression. It indicated that the variations of Lf expression were rather due to an equilibrium between the recruitment of neutrophils and degranulation of activated neutrophils. Thus, this new knowledge will pave the way to a more effective understanding of the role of Lf in intestinal mucosal immunity.

scholarly journals Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

2021 ◽  
Vol 22 (20) ◽  
pp. 11264
Author(s):  
Špela Gruden ◽  
Nataša Poklar Ulrih
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Molecular Level ◽  
Antioxidant Activities ◽  
Antimicrobial Activities ◽  
Iron Binding ◽  
Primary Focus ◽  
Binding Glycoprotein

Lactoferrins are an iron-binding glycoprotein that have important protective roles in the mammalian body through their numerous functions, which include antimicrobial, antitumor, anti-inflammatory, immunomodulatory, and antioxidant activities. Among these, their antimicrobial activity has been the most studied, although the mechanism behind antimicrobial activities remains to be elucidated. Thirty years ago, the first lactoferrin-derived peptide was isolated and showed higher antimicrobial activity than the native lactoferrin lactoferricin. Since then, numerous studies have investigated the antimicrobial potencies of lactoferrins, lactoferricins, and other lactoferrin-derived peptides to better understand their antimicrobial activities at the molecular level. This review defines the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactoferrin-derived peptides. The primary focus is on their different mechanisms of activity against bacteria, viruses, fungi, and parasites. The role of their structure, amino-acid composition, conformation, charge, hydrophobicity, and other factors that affect their mechanisms of antimicrobial activity are also reviewed.

scholarly journals Lactoferrin: A Modulator for Immunity against Tuberculosis Related Granulomatous Pathology

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Jeffrey K. Actor
Keyword(s):  
Therapeutic Efficacy ◽  
Therapeutic Agent ◽  
Iron Binding ◽  
Therapeutic Tool ◽  
Cord Factor ◽  
Pulmonary Pathology ◽  
Mucosal Secretions ◽  
Binding Glycoprotein ◽  
Promising Avenue

There is great need for a therapeutic that would limit tuberculosis related pathology and thus curtail spread of disease between individuals by establishing a “firebreak” to slow transmission. A promising avenue to increase current therapeutic efficacy may be through incorporation of adjunct components that slow or stop development of aggressive destructive pulmonary pathology. Lactoferrin, an iron-binding glycoprotein found in mucosal secretions and granules of neutrophils, is just such a potential adjunct therapeutic agent. The focus of this review is to explore the utility of lactoferrin to serve as a therapeutic tool to investigate “disruption” of the mycobacterial granuloma. Proposed concepts for mechanisms underlying lactoferrin efficacy to control immunopathology are supported by data generated based onin vivomodels using nonpathogenic trehalose 6,6′-dimycolate (TDM, cord factor).

Theoretical insights into the competitive metal bioaffinity of lactoferrin as a metal ion carrier: a DFT study

2019 ◽  
Vol 43 (41) ◽  
pp. 16374-16384 ◽  
Author(s):  
Bahareh Honarparvar ◽  
Suvardhan Kanchi ◽  
Krishna Bisetty
Keyword(s):  
Metal Ion ◽  
Protein Complexes ◽  
Body Fluids ◽  
Pivotal Role ◽  
Dft Study ◽  
Iron Binding ◽  
Ion Carrier ◽  
Living Organisms ◽  
Binding Glycoprotein

Metal–protein complexes, specifically lactoferrin (Lf), an iron-binding glycoprotein found naturally in milk and several other body fluids play a pivotal role in all living organisms.

scholarly journals Occurrence, structure, biochemical properties and technological characteristics of lactoferrin

2000 ◽  
Vol 84 (S1) ◽  
pp. 11-17 ◽  
Author(s):  
Jan M. Steijns ◽  
A. C. M. van Hooijdonk
Keyword(s):  
Protein Structure ◽  
Iron Metabolism ◽  
Three Dimensional ◽  
Biochemical Properties ◽  
Bovine Lactoferrin ◽  
Heat Sensitivity ◽  
Iron Binding ◽  
Exocrine Secretions ◽  
Technological Characteristics ◽  
Binding Glycoprotein

The structure of the iron-binding glycoprotein lactoferrin, present in milk and other exocrine secretions, has been elucidated in great detail, both the three-dimensional protein structure and the attached N-glycans. Structure–function relationships are being established. From these studies a function for lactoferrin in host defence and modulation of iron metabolism emerges. This paper describes in some detail how iron and other cations may be bound by lactoferrins from human or bovine sources and elucidates parts of the molecule that are critical for interactions with cells and biomolecules. Furthermore, the technological aspects, more specifically the heat-sensitivity, of bovine lactoferrin in different matrices are described.

scholarly journals Antimicrobial Lactoferrin Peptides: The Hidden Players in the Protective Function of a Multifunctional Protein

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Mau Sinha ◽  
Sanket Kaushik ◽  
Punit Kaur ◽  
Sujata Sharma ◽  
Tej P. Singh
Keyword(s):  
Antimicrobial Peptides ◽  
Cationic Peptides ◽  
Iron Binding ◽  
Antimicrobial Drugs ◽  
Protective Function ◽  
Interspecies Comparison ◽  
Multifunctional Protein ◽  
Antimicrobial Function ◽  
Current Scenario ◽  
Binding Glycoprotein

Lactoferrin is a multifunctional, iron-binding glycoprotein which displays a wide array of modes of action to execute its primary antimicrobial function. It contains various antimicrobial peptides which are released upon its hydrolysis by proteases. These peptides display a similarity with the antimicrobial cationic peptides found in nature. In the current scenario of increasing resistance to antibiotics, there is a need for the discovery of novel antimicrobial drugs. In this context, the structural and functional perspectives on some of the antimicrobial peptides found in N-lobe of lactoferrin have been reviewed. This paper provides the comparison of lactoferrin peptides with other antimicrobial peptides found in nature as well as interspecies comparison of the structural properties of these peptides within the native lactoferrin.

scholarly journals Commercial Production of Lactoferrin, a Multifunctional Iron-binding Glycoprotein

1997 ◽  
Vol 14 (1) ◽  
pp. 303-320 ◽  
Author(s):  
Pauline P. Ward ◽  
Grainne A. Cunningham ◽  
Orla M. Conneely
Keyword(s):  
Commercial Production ◽  
Iron Binding ◽  
Binding Glycoprotein

Characterization of Lactoferrin Interaction with Streptococcus mutans

1987 ◽  
Vol 66 (2) ◽  
pp. 480-485 ◽  
Author(s):  
M.O. Lassiter ◽  
A.L. Newsome ◽  
L.D. Sams ◽  
R.R. Arnold
Keyword(s):  
Bactericidal Activity ◽  
Bactericidal Effect ◽  
Radical Mechanism ◽  
Second Phase ◽  
Iron Binding ◽  
Bacterial Surface ◽  
Hydroxy Radical ◽  
Radical Generation ◽  
Binding Glycoprotein

Lactoferrin (LF) is an iron-binding glycoprotein common to exocrine secretions and the specific granules of neutrophils. Each molecule is capable of high-affinity coordinate-binding of two ferric ions with two bicarbonate or carbonic anions. The initial aspect of the present study was directed at determining the nature of anion involvement in LF bactericidal activity. It was found that selective anions were capable of inhibiting the expression of bactericidal activity by LF on S. mutans 10449. The ability to block LF expression was directly related to the capacity of the anion to serve as a coordinate ion in iron-binding by the transferrin molecules. These data support the hypothesis that the LF target site on the bacterial surface is anionic. There has been controversy in the literature regarding LF involvement in hydroxy radical generation. The second phase of these studies indicated that treatment of S. mutans with LF under anaerobic conditions abrogated the bactericidal effect of this molecule. LF-killing could be enhanced by the presence of thiocyanate and inhibited by catalase and lactoperoxidase; however, bovine serum albumin was equally effective as an inhibitor. The apparent requirement for oxygen in LF bactericidal effect on S. mutans is not inconsistent with a hydroxy radical mechanism.

Sign in / Sign up

Export Citation Format

Share Document