Abstract
Lactoferrin is a 77-kDa iron-binding protein to which a wide variety of divergent biologic functions have been ascribed. It has recently been reported that lactoferrin interacts with bacterial lipopolysaccharide (LPS) in such a fashion as to affect the binding of lactoferrin to myeloid cells. Two other potential interactions of LPS and lactoferrin were explored. Lactoferrin prevents hydroxyl radical formation by binding iron, even at low pH. Lactoferrin inhibited iron- catalyzed formation of hydroxyl radical in the presence of LPS at pH 7.4 and 4.5. Low concentrations of LPS can be used to “prime” neutrophils toward enhanced function, such as formation of stimulated superoxide anion. Lactoferrin inhibited LPS priming of neutrophils if LPS contamination of the protein (provided by commercial suppliers) was first reduced. Inhibition of LPS priming was observed whether apolactoferrin or iron-saturated lactoferrin was used. Similar inhibition of LPS priming was observed when neutrophils were incubated with other serum proteins (e.g., albumin, apotransferrin, or iron-saturated transferrin). These results show that LPS should not be expected to affect the free radical biology of lactoferrin, which is a crucial physiologic function of this protein. However, lactoferrin inhibits LPS priming, and this effect requires consideration in experimental models of inflammation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1375-1378 |
| Number of pages | 4 |
| Journal | Journal of Infectious Diseases |
| Volume | 166 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jan 1 1992 |
Fingerprint
ASJC Scopus subject areas
- Immunology and Allergy
- Infectious Diseases
Cite this
Interaction of Lactoferrin and Lipopolysaccharide (LPS) : Effects on the Antioxidant Property of Lactoferrin and the Ability of LPS to Prime Human Neutrophils for Enhanced Superoxide Formation. / Cohen, Myron S.; Mao, Jinghe; Rasmussen, George T.; Serody, Jonathan S.; Britigan, Bradley E.
In: Journal of Infectious Diseases, Vol. 166, No. 6, 01.01.1992, p. 1375-1378.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Interaction of Lactoferrin and Lipopolysaccharide (LPS)
T2 - Effects on the Antioxidant Property of Lactoferrin and the Ability of LPS to Prime Human Neutrophils for Enhanced Superoxide Formation
AU - Cohen, Myron S.
AU - Mao, Jinghe
AU - Rasmussen, George T.
AU - Serody, Jonathan S.
AU - Britigan, Bradley E
PY - 1992/1/1
Y1 - 1992/1/1
N2 - Lactoferrin is a 77-kDa iron-binding protein to which a wide variety of divergent biologic functions have been ascribed. It has recently been reported that lactoferrin interacts with bacterial lipopolysaccharide (LPS) in such a fashion as to affect the binding of lactoferrin to myeloid cells. Two other potential interactions of LPS and lactoferrin were explored. Lactoferrin prevents hydroxyl radical formation by binding iron, even at low pH. Lactoferrin inhibited iron- catalyzed formation of hydroxyl radical in the presence of LPS at pH 7.4 and 4.5. Low concentrations of LPS can be used to “prime” neutrophils toward enhanced function, such as formation of stimulated superoxide anion. Lactoferrin inhibited LPS priming of neutrophils if LPS contamination of the protein (provided by commercial suppliers) was first reduced. Inhibition of LPS priming was observed whether apolactoferrin or iron-saturated lactoferrin was used. Similar inhibition of LPS priming was observed when neutrophils were incubated with other serum proteins (e.g., albumin, apotransferrin, or iron-saturated transferrin). These results show that LPS should not be expected to affect the free radical biology of lactoferrin, which is a crucial physiologic function of this protein. However, lactoferrin inhibits LPS priming, and this effect requires consideration in experimental models of inflammation.
AB - Lactoferrin is a 77-kDa iron-binding protein to which a wide variety of divergent biologic functions have been ascribed. It has recently been reported that lactoferrin interacts with bacterial lipopolysaccharide (LPS) in such a fashion as to affect the binding of lactoferrin to myeloid cells. Two other potential interactions of LPS and lactoferrin were explored. Lactoferrin prevents hydroxyl radical formation by binding iron, even at low pH. Lactoferrin inhibited iron- catalyzed formation of hydroxyl radical in the presence of LPS at pH 7.4 and 4.5. Low concentrations of LPS can be used to “prime” neutrophils toward enhanced function, such as formation of stimulated superoxide anion. Lactoferrin inhibited LPS priming of neutrophils if LPS contamination of the protein (provided by commercial suppliers) was first reduced. Inhibition of LPS priming was observed whether apolactoferrin or iron-saturated lactoferrin was used. Similar inhibition of LPS priming was observed when neutrophils were incubated with other serum proteins (e.g., albumin, apotransferrin, or iron-saturated transferrin). These results show that LPS should not be expected to affect the free radical biology of lactoferrin, which is a crucial physiologic function of this protein. However, lactoferrin inhibits LPS priming, and this effect requires consideration in experimental models of inflammation.
UR - http://www.scopus.com/inward/record.url?scp=0026463507&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026463507&partnerID=8YFLogxK
U2 - 10.1093/infdis/166.6.1375
DO - 10.1093/infdis/166.6.1375
M3 - Article
VL - 166
SP - 1375
EP - 1378
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
SN - 0022-1899
IS - 6
ER -