Inhibition of Adhesion of S-Fimbriated Escherichia coli to Epithelial Cells by Meconium and Feces of Breast-Fed and Formula-Fed Newborns

Schroten, Horst; Lethen, A.; Hanisch, Franz‐Georg; Plogmann, R; Hacker, Jörg; Nobis-Bosch, R.; Wahn, V.

doi:10.1097/00005176-199208000-00009

Cited by 51 publications

(33 citation statements)

References 32 publications

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“…This inhibitory activity appeared to be dependent on the presence of neuraminic acid containing glycoproteins. In addition, the mucin fractions from meconium and from feces from human milk-fed infants were also found to have inhibitory activity, while mucin from feces from formula-fed infants was less effective [21]. Skim milk was also found to have inhibitory activity, the greatest being in colostrum compared to mature milk, and the activity was associated with high molecular weight material (1200 kD) characteristic of mucins [22].…”

Section: Clinical Findings For Mucinmentioning

confidence: 98%

Glycoproteins of the Human Milk Fat Globule in the Protection of the Breast-Fed Infant against Infections

Peterson¹,

1998

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Nonimmunological components in human milk can protect breast-fed infants against infection by microorganisms. The structural and functional characteristics of four such components are discussed. The mucin inhibits binding of S-fimbriated Escherichia coli to bucal epithelial cells; lactadherin prevents symptomatic rotavirus-induced infection; glycoaminoglycans inhibit binding of human immunodeficiency virus gp120 to its host cell CD4 receptor, and oligosaccharides provide protection against several pathogens and their toxins.

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Section: Clinical Findings For Mucinmentioning

confidence: 98%

Glycoproteins of the Human Milk Fat Globule in the Protection of the Breast-Fed Infant against Infections

Peterson¹,

1998

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“…Milk mucins have been suggested to be involved in the protection of the newborn through the binding of microorganisms (21,24). Two different types of milk mucins have been described (21).…”

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Rossi¹,

McNeer²,

Price‐Schiavi³

et al. 1996

Journal of Biological Chemistry

108

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Ascites 13762 rat mammary adenocarcinoma cells express abundantly on their cell surfaces a heterodimeric glycoprotein complex composed of a sialomucin ascites sialoglycoprotein (ASGP)-1 and a transmembrane subunit ASGP-2. The latter, which contains two epidermal growth factor-like domains, binds the receptor tyrosine kinase p185 neu , suggesting that the complex is bifunctional as well as heterodimeric. Immunoblot analyses using monoclonal antibodies prepared against the complex demonstrate high levels of expression in rat lactating mammary gland and colon. Immunolocalization studies with anti-ASGP-2 indicate that ASGP-2 is present in these two tissues in the apical regions of secretory epithelial cells. Both mammary gland and colon contain a soluble, secretable form of ASGP-2, which is not found in the ascites cells; milk and mammary gland also have the membrane form. Immunoblot analyses using a COOH-terminal-specific polyclonal antibody indicate that the soluble form of ASGP-2 is missing its COOHterminal domains. Both the soluble and membrane forms of ASGP-2 are similar to the membrane-associated form from the 13762 adenocarcinoma with respect to M r , antigenicity, and association with ASGP-1. The presence of ASGP-1 in milk suggests that it is a candidate for the uncharacterized high M r milk mucin, MUCX. ASGP-2 expression is up-regulated in mammary gland during pregnancy, because it is undetectable in virgin and early pregnant rats but abundant in the gland from late pregnant and lactating animals. However, compared with the lactating mammary gland, the 13762 ascites cells overexpress ASGP-2 by more than 100-fold, which may contribute to their malignancy. These combined results indicate that sialomucin complex is a unique secreted product in the mammary gland and colon, whose behavior is different from that in the mammary ascites tumors, and which may play important roles in mammary and intestinal physiology.

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“…Since the biological significance of many of them is not yet exactly known, new physiological functions can be expected [12][13][14]. Currently of high interest are the glycoconjugates in HM, which can either not be detected in the milk of other species or they are only present at low concentrations or their glycosylation pattern is different [15][16][17]. Examples of these are the large numbers of lactose-derived oligosaccharides which are present in HM but, most of them, not in bovine milk, and hence, not in infant formula [18].…”

Section: Discussionmentioning

confidence: 99%

Glycosylphosphatidylinositol-Anchored Proteins in Human and Pig’s Milk

et al. 1998

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Glycosylphosphatidylinositols (GPIs) are a recently discovered class of glycoconjugates that anchor either proteins, polysaccharides or small oligosaccharides to cellular membranes via a covalent linkage. To investigate the presence of soluble GPIs, individual human milk samples and mature pig’s milk were defatted and casein removed by acid precipitation and ultracentrifugation. Soluble proteins were subjected to FPLC gel filtration (Superdex 200) and high molecular weight proteins were separated into fractions I–V. Immunological studies have been performed using Western blotting of whole milk, casein and whey fractions, and Superdex fractions I–V followed by incubation with a monoclonal antibody against the purified GPI anchor of the variant surface glycoprotein from Trypanosoma brucei brucei. We found that significant amounts of GPI-anchored proteins are secreted into human milk and pig’s milk. The antibody which reacted only with components in the whey fractions bound to 5 different human milk proteins with a molecular weight of ≥200 (at least 3 components), 90 and 80 kD. In pig’s milk, the staining pattern was found to be different from human milk. Similar to other GPI-anchored cell structures the functions of GPI-containing proteins in human milk and pig’s milk as well as the specific components carrying these anchors remain to be investigated.

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Inhibition of Adhesion of S-Fimbriated Escherichia coli to Epithelial Cells by Meconium and Feces of Breast-Fed and Formula-Fed Newborns

Cited by 51 publications

References 32 publications

Glycoproteins of the Human Milk Fat Globule in the Protection of the Breast-Fed Infant against Infections

Glycoproteins of the Human Milk Fat Globule in the Protection of the Breast-Fed Infant against Infections

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Glycosylphosphatidylinositol-Anchored Proteins in Human and Pig’s Milk

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