Comparative Immunological Studies of the Immune Globulins of Human Milk and of Blood Serum

Hanson, Lars Å.

doi:10.1159/000229177

Cited by 225 publications

(75 citation statements)

References 18 publications

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“…The immunoglobulin synthesized by colostral cells is also the principal one found in human colostrum [ 1,5,6]. While the IgA in serum is primarily a monomer comprised of two a chains and two light chains, the IgA in colostrum and other exocrine secretions usually consists of two 7S IgA molecules bound to a 4.5S protein [3,11,14,17,21,22].…”

Section: Discussionmentioning

confidence: 99%

The Cells of Human Colostrum II. Synthesis of IgA and β1c

Murillo

Goldman

1970

Pediatr Res

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Section: Discussionmentioning

confidence: 99%

The Cells of Human Colostrum II. Synthesis of IgA and β1c

Murillo

Goldman

1970

Pediatr Res

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“…Bioactive bifidus factors were identified as human milk glycans that stimulated colonization by L. bifidus. However, when 1 g/L sIgA was measured in human milk and up to 12 g/L in colostrum, concurrent with increased recognition that antibodies provide specific and robust protection, research on bioactive materials of human milk shifted to sIgA inhibition of infection by enteric pathogens (60). Enteromammary circulation of sIgA (Fig.…”

Section: Human Milkmentioning

confidence: 99%

Protection of the Neonate by the Innate Immune System of Developing Gut and of Human Milk

2007

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ABSTRACT:The neonatal adaptive immune system, relatively naïve to foreign antigens, requires synergy with the innate immune system to protect the intestine. Goblet cells provide mucins, Paneth cells produce antimicrobial peptides, and dendritic cells (DCs) present luminal antigens. Intracellular signaling by Toll-like receptors (TLRs) elicits chemokines and cytokines that modulate inflammation. Enteric neurons and lymphocytes provide paracrine and endocrine signaling. However, full protection requires human milk. Breast-feeding reduces enteric infection and may reduce chronic disease in later life. Although human milk contains significant secretory immunoglobulin A (sIgA), most of its protective factors are constitutively expressed. Multifunctional milk components are nutrients whose partial digestion products inhibit pathogens. Cytokines, cytokine receptors, TLR agonists and antagonists, hormones, antiinflammatory agents, and nucleotides in milk modulate inflammation. Human milk is rich in glycans (complex carbohydrates): As prebiotics, indigestible glycans stimulate colonization by probiotic organisms, modulating mucosal immunity and protecting against pathogens. Through structural homology to intestinal cell surface receptors, glycans inhibit pathogen binding, the essential first step of pathogenesis. Bioactive milk components comprise an innate immune system of human milk whereby the mother protects her nursing infant. Interactions between human milk glycans, intestinal microflora, and intestinal mucosa surface glycans underlie ontogeny of innate mucosal immunity, pathobiology of enteric infection, and inflammatory bowel diseases. (Pediatr Res 61: 2-8, 2007)

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“…(Received for publication 12 July 1968) It has been shown that ~,A-immunoglobulin is the major immunoglobulin present in a variety of external secretions, and it has been postulated that the capacity of this protein to enter these secretions is perhaps the most important biologic function that this class of immunoglobulins performs (1)(2)(3). Immunochemical analysis of human ~,A-myeloma proteins has led to the subdivision of ~/A-proteins into two subclasses, ~A1 and ~,A2.…”

mentioning

confidence: 99%

A SUBCLASS OF HUMAN ΓA-Globulins (ΓA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS

Grey

Abel

Yount

et al. 1968

The Journal of Experimental Medicine

211

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The γA2-subgroup of γA-globulins, previously delineated by antigenic studies, was found to differ strikingly from other immunoglobulins in the manner in which the polypeptide chains are bound together. The heavy and light chains were not linked to each other by disulfide bonds. Instead the light chains were disulfide linked to one another, and were present in the γA2-molecule as disulfide bridged L-L dimers. Antisera specific for γA2-proteins indicated the occurrence of two different antigenic types in all normal sera as well as saliva and colostrum. Both of these showed the unique interchain disulfide linkage. Quantitative analyses indicated higher levels of γA2-proteins in external secretions.

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Comparative Immunological Studies of the Immune Globulins of Human Milk and of Blood Serum

Cited by 225 publications

References 18 publications

The Cells of Human Colostrum II. Synthesis of IgA and β1c

The Cells of Human Colostrum II. Synthesis of IgA and β1c

Protection of the Neonate by the Innate Immune System of Developing Gut and of Human Milk

A SUBCLASS OF HUMAN ΓA-Globulins (ΓA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS

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