The physiology of lactoferrin

2002 ◽  
Vol 80 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Jeremy H Brock
Keyword(s):  
Current Knowledge ◽  
Binding Protein ◽  
Biochemical Properties ◽  
Structure And Function ◽  
Iron Nutrition ◽  
Future Research ◽  
Iron Binding ◽  
Physiological Functions ◽  
Iron Binding Protein ◽  
And Function

This paper reviews our current knowledge of the structure and function of the iron-binding protein lactoferrin. In particular, it attempts to relate the various proposed physiological functions of lactoferrin to its most characteristic biochemical properties, i.e. its ability to bind iron and its highly basic nature. The extent to which various physiological functions can be considered as definitely established is critically reviewed, and suggestions for future research are proposed.Key words: lactoferrin, iron, nutrition, immunology, infection, inflammation.

Lactoferrin – 50 years on

2012 ◽  
Vol 90 (3) ◽  
pp. 245-251 ◽  
Author(s):  
Jeremy H. Brock
Keyword(s):  
Gastrointestinal Tract ◽  
Antimicrobial Agent ◽  
Iron Transport ◽  
Iron Absorption ◽  
Structure And Function ◽  
Transport Protein ◽  
Future Research ◽  
Iron Binding ◽  
Plasma Iron ◽  
And Function

It is now some 50 years since iron-binding lactoferrin was first isolated and purified, an event that opened the way to subsequent extensive research on lactoferrin structure and function. The initial recognition that lactoferrin closely resembled the plasma iron-transport protein transferrin meant that lactoferrin was first thought to mediate intestinal iron absorption or to act as an antimicrobial agent. It was also suggested that it could mediate the hyposideraemia of inflammation. This paper will assess to what extent early proposals have stood the test of time and also suggest possible mechanisms by which lactoferrin can mediate the large number of potential functions that have subsequently been proposed. It will also review the ability of lactoferrin to resist digestion in the gastrointestinal tract and identify areas for future research.

scholarly journals Structure and Function of the CFTR Chloride Channel

1999 ◽  
Vol 79 (1) ◽  
pp. S23-S45 ◽  
Author(s):  
DAVID N. SHEPPARD ◽  
MICHAEL J. WELSH
Keyword(s):  
Cystic Fibrosis ◽  
Chloride Channel ◽  
Atp Hydrolysis ◽  
Current Knowledge ◽  
Structure And Function ◽  
Binding Domains ◽  
Transporter Family ◽  
Membrane Spanning ◽  
And Function ◽  
R Domain

Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79 , Suppl.: S23–S45, 1999. — The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl− channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.

scholarly journals Structure and function of renin binding protein

1994 ◽  
Vol 46 (6) ◽  
pp. 1525-1527 ◽  
Author(s):  
Saori Takahashi ◽  
Hiroyasu Inoue ◽  
Kiyoshi Fukui ◽  
Yoshihiro Miyake
Keyword(s):  
Binding Protein ◽  
Structure And Function ◽  
And Function

scholarly journals Lactoferrin-an iron binding protein in synovial fluid

1973 ◽  
Vol 16 (2) ◽  
pp. 186-190 ◽  
Author(s):  
Robert M Bennett ◽  
A C Eddie-Quartey ◽  
P J L Holt
Keyword(s):  
Synovial Fluid ◽  
Binding Protein ◽  
Iron Binding ◽  
Iron Binding Protein
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