Transferrin group

I thank Heather Baker, Catherine Day, Rob Evans, Peter Lindley, Clyde Smith, John Tweedie, and Harmon Zuccola for access to their unpublished data Clyde Smith for help with illustrations and Heather Baker and Andrew Brodie for their critical reading of the manuscript. I owe a particular debt to Peter Lindley, Rob Evans, and members of the Birkbeck College transferrin group for the free and rewarding collaborative interactions we have always had and to Phil Aisen for being a constant source of inspiration to all in the transferrin field. 

FIG. 15 Cellular entry and intracellular kinetics of the cationic lipid-DNA complexes. Cationic lipid-DOPE liposomes form electrostatic complexes with DNA, and, in this case, also transferrin (Tf) is incorporated. Cellular uptake by endoc5dosis and endosomal acidification can be blocked with cytochaiasin B and bafilomycin Aj, respectively. DNA is proposed to be released at the level of endosomal wall after fusion of the carrier lipids with endosomal bilayer. This process is facilitated by the formation of inverted hexagonal DOPE phase as illustrated in the lower corner on the right. After its release to the C5doplasm DNA may enter the nucleus. (From Ref. 253. By permission of Nature Publishing Group.)... 

Iron transport agents may belong to the protein or non-protein class. In the former group are found the animal proteins transferrin (25), lactoferrin (26) and conalbumin (27). The low molecular weight iron carrying compounds from microorganisms, the siderochromes, may occur with or without a bound metal ion. Typically, severe repression of biosynthesis of these substances can be expected to set in at an iron concentration of ca. 2 x 10-5 g atoms/liter (28). Most, but not all, of these substances can be described as phenolates or hydroxamates (4). 

Figure 5.5 Stereo view of the Fe3+ binding site of (a) hFBP (b) human lactoferrin, N-lobe and (c) human transferrin (N-lobe). From Bruns, 1997. Reproduced by permission of Nature Publishing Group. 

FhuA and FepA will prove to be the reference structures for a large group of bacterial outer-membrane transporters that take up bacterial Fe3+-siderophores, Fe3+ released from host transferrin and lactoferrin, haem, and haem released from haemoglobin and haemopexin. It is assumed that all iron sources are transported... 

Figure 5.3 The deduced evolutionary tree for selected members of the transferrin superfamily, based on comparisons of structures and sequences. The tree combines the transferrins with a number of prokaryotic periplasmic transport proteins. From Bruns et al., 1997. Reproduced by permission of Nature Publishing Group.

Figure 11.1 Schematic representation of iron uptake mechanisms, (a) The transferrin-mediated pathway in animals involves receptor-mediated endocytosis of diferric transferrin (Tf), release of iron at the lower pH of the endocytic vesicle and recycling of apoTf. (b) The mechanism in H. influenzae involves extraction of iron from Tf at outer membrane receptors and transport to the inner membrane permease system by a periplasmic ferric binding protein (Fbp). From Baker, 1997. Reproduced by permission of Nature Publishing Group.

FIGURE 5.8 Complex hyperfine patterns due to axes noncolinearity in a low-symmetry prosthetic group. The X-band spectrum is from 65Cu(II)-bicarbonate in human serum transferrin (a,b) experimental spectrum (c,e) simulation assuming axial symmetry (d, f) simulation assuming triclinic symmetry with the A-axes rotated with respect to the g-axes over 15° about the gz-axis and then 60° about the new y -axis. Traces b, e, and f are 5x blow-ups of traces a, c, d, respectively (Hagen 2006). (Reproduced by permisson of The Royal Society of Chemistry.)... 

Schewale, J.G., and Brew, K. (1982) Effects of Fe3+ binding on the microenvironments of individual amino groups in human serum transferrin as determined by different kinetic labeling. /. Biol. Chem. 257, 9406. 

Iron can only be resorbed by the bowel in bivalent form (i.e., as Fe " ). For this reason, reducing agents in food such as ascorbate (vitamin C see p. 368) promote iron uptake. Via transporters on the luminal and basal side of the enterocytes, Fe " enters the blood, where it is bound by transferrin. Part of the iron that is taken up is stored in the bowel in the form of ferritin (see below). Heme groups can also be resorbed by the small intestine. 

Honeychurch and Ridd [97] used chronopotentiometry to study reduction of five disulfide-containing proteins (bovine serum albumin, insulin, ribonuclease A, transferrin, and trypsin) adsorbed on HMDE. All studied proteins exhibited a reduction step at —0.6 V (versus SCE), due to reduction of disulfide groups. 

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