Recombinant human lactoferrin: A valuable protein for pharmaceutical products and functional foods

被引:56
作者
Conesa, Celia [1 ]
Calvo, Miguel [1 ]
Sanchez, Lourdes [1 ]
机构
[1] Univ Zaragoza, Fac Vet, E-50013 Zaragoza, Spain
关键词
Human lactoferrin; Recombinant lactoferrin; Rice; Aspergillus awamori; Transgenic cows; Functional foods; Pharmaceutical products; Iron-binding; Anti-bacterial activity; TRANSGENIC DAIRY-COWS; HIGH-LEVEL EXPRESSION; DOSE ORAL TOXICITY; THERMAL-DENATURATION; TALACTOFERRIN-ALPHA; ASPERGILLUS-AWAMORI; BINDING-PROPERTIES; PRETERM DELIVERY; N-GLYCOSYLATION; HUMAN LYSOZYME;
D O I
10.1016/j.biotechadv.2010.07.002
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Lactoferrin, the main iron-binding protein of milk, has biological activities that are essential for the newborn and are beneficial for adults. Given this beneficial effect, there is broad interest in exogenous sources of lactoferrin in human nutrition. Consequently, several transgenic approaches to produce lactoferrin have been achieved. However, the activity of heterologous lactoferrin cannot be assumed to identically mimic that of the homologous protein. Human lactoferrin obtained from yeast, transgenic cows, and rice has met the criteria of structural similarity, high yield, and ease of protein isolation. Human lactoferrin from Aspergillus awamori has been mainly directed to therapeutic uses with advanced phases of clinical trials currently in progress. In contrast, human lactoferrin produced in transgenic cows and rice brings the clear advantage of origins compatible with use in foods, although the approval for these applications is still in process. (C) 2010 Elsevier Inc. All rights reserved.
引用
收藏
页码:831 / 838
页数:8
相关论文
共 102 条
[1]   LACTOFERRIN AND TRANSFERRIN - COMPARATIVE STUDY [J].
AISEN, P ;
LIEBMAN, A .
BIOCHIMICA ET BIOPHYSICA ACTA, 1972, 257 (02) :314-&
[2]  
Andersen JH, 2004, CURR OPIN MOL THER, V6, P344
[3]   APOLACTOFERRIN STRUCTURE DEMONSTRATES LIGAND-INDUCED CONFORMATIONAL CHANGE IN TRANSFERRINS [J].
ANDERSON, BF ;
BAKER, HM ;
NORRIS, GE ;
RUMBALL, SV ;
BAKER, EN .
NATURE, 1990, 344 (6268) :784-787
[4]   STRUCTURE OF HUMAN LACTOFERRIN AT 3.2-A RESOLUTION [J].
ANDERSON, BF ;
BAKER, HM ;
DODSON, EJ ;
NORRIS, GE ;
RUMBALL, SV ;
WATERS, JM ;
BAKER, EN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1987, 84 (07) :1769-1773
[5]   STRUCTURE OF HUMAN LACTOFERRIN - CRYSTALLOGRAPHIC STRUCTURE-ANALYSIS AND REFINEMENT AT 2.8-A RESOLUTION [J].
ANDERSON, BF ;
BAKER, HM ;
NORRIS, GE ;
RICE, DW ;
BAKER, EN .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 209 (04) :711-734
[6]   Sub-chronic (13-week) oral toxicity study in rats with recombinant human lactoferrin produced in the milk of transgenic cows [J].
Appel, M. J. ;
van Veen, H. A. ;
Vietsch, H. ;
Salaheddine, M. ;
Nuijens, J. H. ;
Ziere, B. ;
de Loos, F. .
FOOD AND CHEMICAL TOXICOLOGY, 2006, 44 (07) :964-973
[7]   Cellular internalization of lactoferrin in intestinal epithelial cells [J].
Ashida, K ;
Sasaki, H ;
Suzuki, YA ;
Lönnerdal, B .
BIOMETALS, 2004, 17 (03) :311-315
[8]   A structural framework for understanding the multifunctional character of lactoferrin [J].
Baker, Edward N. ;
Baker, Heather M. .
BIOCHIMIE, 2009, 91 (01) :3-10
[9]   STRUCTURE, FUNCTION AND FLEXIBILITY OF HUMAN LACTOFERRIN [J].
BAKER, EN ;
ANDERSON, BF ;
BAKER, HM ;
HARIDAS, M ;
JAMESON, GB ;
NORRIS, GE ;
RUMBALL, SV ;
SMITH, CA .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 1991, 13 (03) :122-129
[10]   Molecular structure, binding properties and dynamics of lactoferrin [J].
Baker, EN ;
Baker, HM .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2005, 62 (22) :2531-2539