Lactotransferrin mouse

Since these first discoveries, lactotransferrin has been isolated from milk of numerous mammals goat [40], mare [41], monkey [42], mouse [43,44], rabbit [45] and sow [46,47]. 

Fig. 4. Location of the glycosylation sites on the peptide chain of human variants 1 [74] and 2 [ 117], mouse [121], cow [118], mare, goat [81] and swine [80,120] lactotransferrins (a), mapping not determined solid circles on bars, glycosylated sites heavy bars, non-glycosylated sites. In cow lactotransferrin, glycans are of the oligomannosidic type at positions 233 and 545, of the oligomannosidic or iV-acetyllactosaminic type at positions 368 and 476. Only the glycans of the Af-acetyllactosaminic type at position 476 contain one Af-acetylgalactosamine residue.

Iron transport. Experiments in vitro carried out in 1979 by Cox et al. [164] and using human intestinal biopsies demonstrated that human lactotransferrin can donate iron to intestinal mucosal cells. The characterization of a specific intestinal lactotransferrin receptor in rabbit [48], mouse [165,166], Rhesus monkey [167] and human foetal intestinal brush border membranes [168] reinforces the concept of the role of lactotransferrin in intestinal iron absorption. However, despite these findings, the nutritional activity of lactotransferrin is still a subject of controversy (for a review, see ref. [7]). 

Lactotransferrin receptors. The existence of a lactotransferrin receptor was first demonstrated by Van Snick and Masson in 1976 [191] at the surface of mouse peritoneal macrophages and lymphocytes. Since this discovery, the presence of lactotransferrin receptors has been demonstrated at the surface of various cells (for reviews, see refs. [156,158,192,193]) rabbit [48], mouse [165,166], monkey [167] and human [168] enterocytes human HT29 and Caco-2 enterocyte cell lines [194] human monocytes (reviewed in ref. [195]), human alveolar macrophages [196], human neutrophils [195,197], human resting lymphocytes [197], human activated lymphocytes [189], human Jurkat T cell line [190], human epithelial mammary cell line [198], human platelets [199,200] and megakaryocytes [201], hepatocytes [202,203] and in bacteria (for a review see refs. [204,205]). 

Serotransferrin glycans are generally non-fucosylated except in human cerebrospinal fluid (trace amounts) [246,247], rat (20-30% of the molecules) [221], pig (100% of the molecules) [220] and the serotransferrin-like glycoprotein from mouse milk [218,219] in which this protein co-exists with a lactotransferrin. None of the serotransferrin glycans... 

Fig. 11. Primary structure of the glycans from human leukocyte lactotransferrin (A) [226] and human (B,C,D) [211,227-230], Rhesus monkey (A) [231], sheep (A) [232], goat (B,C) [119,228,232], and mouse (B,C)[119, 218,233] milk lactotransferrins. E, human recombinant lactotransferrin expressed in BHK cells [234],...

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