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

Jonard, P.; Rambaud, J C; Dive, Caroline; Vaerman, Jp.; Galian, A; Delacroix, Dominique L.

doi:10.1172/jci111450

Cited by 129 publications

(62 citation statements)

References 38 publications

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“…The dose was estimated to correspond to the daily amount of IgA synthesised and secreted throughout the bowel in man. 10 The placebo group received an equivalent volume of Haemaccel (Behringwerke AG, Marburg, Germany) three times daily during the same period. This substance was used because it was regarded as inert and had a colour, taste and consistency very similar to the immunoglobulin preparation.…”

Section: Methodsmentioning

confidence: 99%

Gut mucosa barrier preservation by orally administered IgA-IgG to patients undergoing bone marrow transplantation: a randomised pilot study

Johansson

Ekman

1999

Bone Marrow Transplant

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Summary:Intensive cytotoxic therapy with bone-marrow transplantation (BMT) allows a potential cure for haematological malignancies. Protective strategies to minimise haematological toxicities have been successful and currently toxicity to the gastro-intestinal tract is the major cause of treatment-related morbidity and the dose-limiting factor that prevents further dose escalation. In a randomised, placebo-controlled trial we investigated whether an oral immunoglobulin preparation (IgA-IgG) can diminish intestinal toxicity with autologous BMT. IgA-IgG (n = 6) and placebo (n = 7) were orally administered from 1 day prior to the start until 1 week after the termination of the cytotoxic treatment (a total of 14 days). Intestinal toxicity was assessed by a 51 Cr-EDTA absorption test for intestinal permeability and by the clinical criteria laid down by the WHO for the period before the start of the cytotoxic treatment, 1 day prior to stem-cell infusion and 4, 7, 10 and 14 days after stemcell infusion. In the placebo group there was a significant increase in intestinal permeability on day 4 (P Ͻ 0.005) and on day 7 (P Ͻ 0.05) after stem-cell infusion, compared with the baseline, which was not seen for IgA-IgG. In addition, patients receiving IgAIgG had significantly less intestinal permeability on day 4 (P Ͻ 0.05) and on day 7 (P Ͻ 0.05), compared with the placebo group. No significant, positive effect as regards clinical toxicity was observed. Oral administration of IgA-IgG to patients undergoing intensive cytotoxic therapy prior to BMT seems to have a protective effect on the gut mucosa barrier which is normally disrupted by this therapy.

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Section: Methodsmentioning

confidence: 99%

Gut mucosa barrier preservation by orally administered IgA-IgG to patients undergoing bone marrow transplantation: a randomised pilot study

Johansson

Ekman

1999

Bone Marrow Transplant

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“…However, the use of this quantity in the assessment of inflammatory bowel disease activity remains controversial (3,4). Owing to the absence of a specific mucosal transfer system, the monomeric IgA of intestinal secretions appears to be derived mainly from passive transport of plasma monomeric IgA (5,6). These monomeric IgA are relatively resistant to intestinal proteases and are found in the faeces in their native form or as fragments often bound to a r antiproteinase or pigments (7 -9).…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, their intestinal clearance appears to be markedly increased during diarrhoea (10). Jonard et al have demonstrated that IgG, present in the intestinal secretions of healthy subjects, are serum-derived (5). We therefore evaluated the value of determining monomeric IgA and IgG intestinal clearances, together with that of aiantiproteinase, for the purpose of exploring the degree of intestinal protein loss syndrome, which in turn is related to mucosal permeability.…”

Section: Introductionmentioning

confidence: 99%

“…the secretory component (17 -19). IgM, monomeric IgA and IgG play a less important role in this setting (5,17,18). The determination of the faecal output of polymeric IgA and IgM may provide a means of evaluating, in vivo, the repercussions of inflammatory bowel disease on local humoral immunity, which in turn represents an evaluation of the activity of the disease.…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of Intestinal Clearance and Faecal Excretion of α1-Antiproteinase and Immunoglobulins During Crohn’s Disease and Ulcerative Colitis

Kapel¹,

Meillet²,

Favennec³

et al. 1992

Clinical Chemistry and Laboratory Medicine

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Summary:The intestinal clearance of oc r antiproteinase, monomeric IgA and IgG, and the daily fecal output of polymeric IgA and IgM were investigated in patients with inflammatory bowel diseases (inactive and active Crohn's disease, ulcerative colitis) and in a control group. The intestinal clearance of a r antiproteinase was significantly increased in all patients with inflammatory bowel diseases (p < 0.01), irrespective of the grade of the disease. In contrast, increases in intestinal clearances of monomeric IgA and IgG were more closely related to the severity of the intestinal lesions. The associate determination of these three quantities should therefore be of interest for monitoring the degree of intestinal bowel inflammation. Faecal output of polymeric IgA was significantly increased in active intestinal disease (p < 0.01), whereas faecal IgM levels were not. The determination of the faecal output of polymeric IgA should contribute to the assessment of the activity of inflammatory bowel diseases, and may provide insight into the activation of the mucosal immune system.

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“…Consequently, it is also the target of specific receptors and proteases produced by a number of pathogenic bacteria (6). Blood also contains a large quantity [average, 2 mg/ml (7)] of predominantly monomeric IgA; this circulating pool is largely independent ofthe mucosal pool in humans (8).…”

mentioning

confidence: 99%

Recombinant human IgA expressed in insect cells.

Carayannopoulos

Max

Capra

1994

Proc. Natl. Acad. Sci. U.S.A.

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IgA serves as the fwst line of humoral defense at all mucosal surfaces and is present in large quantities in serum. To map the sites of interaction of immune effector molecules with the IgA constant region (C.), we have expressed soluble, chimeric human IgA in insect cells using recombinant baculoviruses. This antibody is correctly assembled into heavy chain/light chain heterodimers, N-glycosylated Consequently, it is also the target of specific receptors and proteases produced by a number of pathogenic bacteria (6). Blood also contains a large quantity [average, 2 mg/ml (7)] of predominantly monomeric IgA; this circulating pool is largely independent ofthe mucosal pool in humans (8).(ii) IgA binds to an Fca receptor [monocyte/macrophage (mFcaR) (9-11)] on the surface of eosinophils (12), neutrophils (13), and monocytes/macrophages (9), triggering effector responses in so doing. (iii) B lymphocytes and T lymphocytes possess surface receptors for Fca through which immunoregulatory signals are thought to be transmitted (14). (iv) IgA is thought to activate complement through the alternative pathway (15). Thus, IgA not only plays a role in host defense against extracellular viruses and bacteria but is also potentially critical for neutralization of intracellular viruses in tissues expressing pIgR (16) and for destruction of helminths, protozoans, and other eukaryotic parasites (17).Several immunologic disease processes are mediated by IgA, including IgA glomerulonephritis (18) and possibly the exacerbation of allergic asthma (19,20). Each of these properties of IgA depends on the ability of effector molecules such as complement component C3 and mFcaR to recognize specific sites on the surface of the IgA heavy-chain constant region (CJ; however, none of these sites has been well defined.To investigate the above-mentioned functions of IgA, we have established its production in insect cells utilizing recombinant baculoviruses (21). The baculovirus system allows production of mutant antibodies as well as combinatorial expression of immunoglobulin with other polypeptides (J chain, chaperoning, etc.) much more rapidly than with stably transfected mammalian lines. Here we describe production of immunologically and functionally authentic human IgA with hapten specificity and explore the utility of this expression system in addressing structure-function correlations in Ca. MATERIALS AND METHODSSynthesis of Ig Coding Regions. DNA fragments corresponding to the heavy-and light-chain variable (V) regions of monoclonal antibody (mAb) 93G7 were amplified by PCR from plasmids pHyl-360E and pHK-360E (22), respectively. The oligonucleotide primers for these amplifications included a 5' Nco I site at the initiation codon and a 12-nt antisense overlap with Cca at the 3' end. The coding regions of human Cal and CK were obtained from human peripheral-blood leukocyte RNA by reverse transcription-PCR (23); in this case, the primers included a 12-nt sense overlap with the appropriate V region at the 5' end and an Xba I site at the...

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

Cited by 129 publications

References 38 publications

Gut mucosa barrier preservation by orally administered IgA-IgG to patients undergoing bone marrow transplantation: a randomised pilot study

Gut mucosa barrier preservation by orally administered IgA-IgG to patients undergoing bone marrow transplantation: a randomised pilot study

Evaluation of Intestinal Clearance and Faecal Excretion of α1-Antiproteinase and Immunoglobulins During Crohn’s Disease and Ulcerative Colitis

Recombinant human IgA expressed in insect cells.

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