The Origin of Monomeric and Polymeric Forms of IgA in Man

Rádl, J.; Schuit, H. R. E.; Městecký, Jiří; Hijmans, W.

doi:10.1007/978-1-4613-4550-3_7

Cited by 35 publications

(23 citation statements)

References 10 publications

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“…3 (33) at similar concentrations as in other mammals (2), but large additional amounts of m-IgA, not found in most mammals (34) make it the minor component of IgA in human serum. The higher proportions of plasma cells staining for p-IgA (35,36) or for IgA2 (37) in mucosae than in bone marrow (35,38), and the higher proportions of p-IgA (1, 2) or of IgA2 (6, 7) in secretions than in serum, led some authors to regard serum p-IgA and/or IgA2 as being mainly of mucosal origin (2,10,13). In contrast, mIgA and IgAl in serum are likely to originate predominantly from bone marrow (39) where IgAl plasmacytes predominate and are the largest producers of m-IgA in vitro (40).…”

Section: Resultsmentioning

confidence: 98%

Changes in size, subclass, and metabolic properties of serum immunoglobulin A in liver diseases and in other diseases with high serum immunoglobulin A.

et al. 1983

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A B ST R A CT We have studied the relative contributions of monomeric (m-) and polymeric IgA (p-IgA) and of IgAl and IgA2 to total serum IgA in healthy adults and patients with liver disease (LD) or with other diseases and high serum IgA. Serum concentration of total secretory component (SC) was also determined. In addition, fractional catabolic rates (FCR) and synthetic rates for both m-and p-IgA were measured in nine controls and nine cirrhotics. Our results support four main conclusions: (a) In healthy adults, intravascular p-IgA contributes to only 4-22% (mean 12%) of serum IgA, because its FCR and synthetic rate are approximately two times higher and four times smaller, respectively, than those of intravascular mIgA. (b) In LD, biliary obstruction does not result in a significant increase in serum p-IgA unlike in rats and rabbits, indicating that in humans the SC-dependent biliary transport of p-IgA plays a much less significant role in selective removal of p-IgA from plasma than in rats and rabbits. (c) In contrast to biliary obstruction, parenchymal LD results in a significant and preferential increase in serum p-IgA, which in cirrhotics correlates with a selective reduction of the p-IgA-FCR. This supports a role for the human liver in selective removal of p-IgA from plasma, but another mechanism than the SC-dependent biliary transport should be considered. (d) Total SC, p-IgA, and IgA2 in serum are unlinked parameters, not necessarily reflecting mucosal events. A marked increase in serum SC occurs Address reprint requests to Dr. Delacroix, ICP-MEXP, Brussels, Belgium.

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Section: Resultsmentioning

confidence: 98%

Changes in size, subclass, and metabolic properties of serum immunoglobulin A in liver diseases and in other diseases with high serum immunoglobulin A.

et al. 1983

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“…Jejunal biopsy was obtained after perfusion under endoscopic control. Two of these patients were also injected intravenously with [5][6][7][8][9][10] …”

Section: Methodsmentioning

confidence: 99%

“…Over half of this IgA is in polymeric form (9)(10)(11), and -35% ofit is IgA2 (12). In contrast, plasma IgA is predominately monomeric (m-IgA), and of the IgA I subclass (5,13), and is mostly produced in the bone marrow (I 1, 14).…”

Section: Introductionmentioning

confidence: 99%

Secretion of immunoglobulins and plasma proteins from the jejunal mucosa. Transport rate and origin of polymeric immunoglobulin A.

Jonard¹,

Rambaud²,

Dive³

et al. 1984

J. Clin. Invest.

130

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This closely corresponds to the 35 and 24% of IgA2 plasmocytes in jejunal mucosa and peripheral lymph nodes, respectively. (b) For each protein, a relative coefficient of excretion (RCE) was calculated (jejunum to serum concentration ratio expressed relative to that of albumin). RCEs of 1.41 for orosomucoid, 1.0 for albumin, 0.83 for IgG, and 0.74 for IgE and, in the deficient patient, of 0.64 for m-IgA and 0.016 for IgM were obtained. This was inversely related to the molecular weight of these proteins and indicated their predominantly passive transport into the jejunum.

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“…Examination of mucosal and non-mucosal (lymph nodes, spleen, and bone marrow) tissues by immunohistochemical techniques, and analyses of the molecular forms of IgA produced by cells obtained from such tissues have yielded information relevant to the interpretation of the above-described results. Cells capable of producing plgA (as determined by the presence of intraccllular J chain and ability to bind SC)are found in high proportions in mucosal tissues and secretory glands while the bone marrow, spleen, and lymph nodes display these markers of pigA synthesis with LI much lower frequency [64,65]. Determination of the molecular projxirties of IgA secreted into culture supernatants by explants or cell suspensions from such tissues has confirmed these findings [27.28.58.66].…”

Section: Cellular Originsmentioning

confidence: 93%

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1992

Clinical &Amp; Experimental Immunology

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SUMMARYHuman IgA occurs in multiple molecular forms (polymeric and monomcric) and iwo subclasses which show ditferential distribution between the niucosai and circulatory comparimenis of the immune system. However, the molecular form and subclass of specific IgA antibodies are influenced, especially during an immune response, by Ihe type of antigen and duration of the response as well as by the route ofexposure. These considerations quesUon previously held notions thai polymeric IgA and an increased representation of the lgA2 subclass among circulating antibodies or antibodysecreting cells signify their mucosal origin. Although the functional properties of different molecular forms and subclasses of IgA antibodies are incompletely understood, it appears that there is physiological benefit in the diversity of the IgA immune system.

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The Origin of Monomeric and Polymeric Forms of IgA in Man

Cited by 35 publications

References 10 publications

Changes in size, subclass, and metabolic properties of serum immunoglobulin A in liver diseases and in other diseases with high serum immunoglobulin A.

Changes in size, subclass, and metabolic properties of serum immunoglobulin A in liver diseases and in other diseases with high serum immunoglobulin A.

Secretion of immunoglobulins and plasma proteins from the jejunal mucosa. Transport rate and origin of polymeric immunoglobulin A.

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