Proteolytic degradation of exocrine and serum immunoglobulins

Brown, William R.; Newcomb, Richard W.; Ishizaka, Kimishige

doi:10.1172/jci106354

Cited by 162 publications

(46 citation statements)

References 24 publications

(12 reference statements)

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“…For trypsin and chymotrypsin digestion of PS protein, concentrations of the enzymes were adjusted to be roughly equivalent to the proteolytic activity of intestinal fluids as estimated by casein digestion [Brown et al, 1970], The enzyme: substrate ratio therefore was very high (about 50:1). After 24 h incubation with trypsin, the majority of protein detectable by anti-ND in Sephadex G-150 eluates was in a peak with molecular weight about that of IgG, but a smaller peak of material similar in molecular weight to that described above was also recovered (fig.…”

Section: Resultsmentioning

confidence: 99%

Studies on IgE in Human Intestinal Fluids

Brown¹,

Lee²

1976

Int Arch Allergy Immunol

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A fragment of IgE with molecular weight of about 40,000 was identified by radioimmunoassay in human small intestinal fluid after fractionation by gel filtration chromatography. Digestion of E myeloma protein PS by pooled intestinal fluid, trypsin or chymotrypsin yielded a degradation product of similar molecular weight that probably consisted principally of ε₁determinant-containing fragments. These findings suggest that IgE is secreted into the intestinal lumen and degraded there by pancreatic proteolytic enzymes, producing an enzyme-resistant portion of the amino-terminal part of the Fc region.

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Section: Resultsmentioning

confidence: 99%

Studies on IgE in Human Intestinal Fluids

Brown¹,

Lee²

1976

Int Arch Allergy Immunol

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“…Irrespective of the putative transport role of secretory component (described above), there is no doubt that secretory component confers protection from proteolytic degradation to the secretory IgA molecule (Cederblad et al 1966;Tomasi and Czerwinski 1968;Shim et al 1969;Brown et al 1970;Tax and Korngold 1971). Thus, secretory IgA in milk is better equipped than other immunoglobulins to withstand enzymatic attack in the stomach and intestine and to carry out a protective role in the alimentary tract of the suckling infant.…”

Section: Protective Role Of Milk Igamentioning

confidence: 99%

Immunological Functions of the Mammary Gland and Its Secretion-Comparative Review

Dl¹

1980

Aust. Jnl. Of Bio. Sci.

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The mammary gland performs vitally important immunological roles, both in providing passive immune protection to the suckling infant and in immunological defence of its own tissues against infection with microorganisms. These immunological functions differ greatly between species of mammals in both nature and magnitude. In ungulates the mammary gland is singularly responsible for transfer of immunoglobulin (IgG) from mother to young. This process is dependent on a highly selective mechanism which results in the transport of blood-borne IgG molecules across secretory epithelial cells of the colostrum-forming mammary gland and into secretion. Upon ingestion of colostrum by the young ungulate this immunoglobulin is absorbed across the wall of the small intestine and thence into the bloodstream.In other species, including rodents and primates, there is a well-developed local IgA system operating in the mammary gland. In this situation, plasma cells located near the basal membranes of secretory epithelial cells secrete IgA which passes through the epithelial cells and into colostrum or milk. In these species the IgA in mammary secretions is not absorbed into the circulation of the suckling infant; because of its unique property of resisting proteolytic degradation, it may mediate a local protective role in the lumen of the intestine of the suckling infant.Specific immunological protection of mammary tissue may be mediated through blood-derived antibody (particularly IgG), locally synthesized antibody (particularly IgA) or phagocytic cells. Neutrophils arrive in mammary tissue and secretions in very large numbers following bacterial invasion of the gland. It has been established recently that these cells carry cytophilic antibody on their cell membrane. This cytophilic antibody can play an important functional role in enhancing the phagocytic capacity of neutrophils in the mammary gland.

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“…Dimeric IgA and IgM are transported across the epithelial barrier by the polymeric immunoglobulin receptor, and a portion of the receptor, termed the secretory component, remains bound to the dimeric IgA or IgM after proteolytic cleavage from the apical membrane, forming secretory IgA and IgM (23). The secretory component increases the resistance of IgA to proteases present within mucosal secretions (5,6,20).…”

Section: Vol 11 2004 Immunoglobulin Concentrations In Feces Of Healmentioning

confidence: 99%

Measurement of Immunoglobulin Concentrations in the Feces of Healthy Dogs

Peters

Calvert

Hall

et al. 2004

Clin Vaccine Immunol

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Selective immunoglobulin A (IgA) deficiency is the most common primary immunodeficiency in humans and may be associated with chronic gastrointestinal disease. This observation has led to the suggestion that the high susceptibility of German shepherd dogs (GSD) to chronic enteropathies is related to a deficiency in mucosal IgA production. Relative deficiencies of IgA has been reported in the serum, saliva, tears, and feces of GSD both with and without alimentary disease; however, the findings of different studies are not consistent. The aim of this study was to confirm whether a relative deficiency of IgA exists in the feces of GSD. Feces were collected from healthy GSD (n ‫؍‬ 209), Labrador retrievers (n ‫؍‬ 96), beagles (n ‫؍‬ 19), and miniature schnauzers (n ‫؍‬ 32). Fecal IgA, IgM, and IgG were measured by capture enzyme-linked immunosorbent assays. Fecal IgG concentrations in the four breed groups were not significantly different. IgA concentrations were significantly greater in miniature schnauzers than in GSD (P ‫؍‬ 0.0003) and Labradors (P ‫؍‬ 0.0004) but not significantly different from those in beagles. IgM concentrations were significantly greater in miniature schnauzers than in GSD (P < 0.0001), Labradors (P < 0.0001), and beagles (P ‫؍‬ 0.0098). These findings do not support the hypothesis that GSD have a relative deficiency in fecal IgA. The differences in immunoglobulin concentrations measured from a single defecation, between individuals of the same breed and between breeds, as well as the lack of an internal control molecule, make the determination of a normal reference range for all dogs impossible. Therefore, the usefulness of fecal immunoglobulin quantification for the assessment of intestinal immunoglobulin secretion in dogs is limited.

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Proteolytic degradation of exocrine and serum immunoglobulins

Cited by 162 publications

References 24 publications

Studies on IgE in Human Intestinal Fluids

Studies on IgE in Human Intestinal Fluids

Immunological Functions of the Mammary Gland and Its Secretion-Comparative Review

Measurement of Immunoglobulin Concentrations in the Feces of Healthy Dogs

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