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Biomedical subjects

J P Vaerman

Publications and source records attributed to J P Vaerman.

At least 91 records · Page 5Linked to original sources
PubMed1989

Ontogeny of secretory component in rat liver.

The ontogeny of the expression of secretory component (SC), the receptor for transepithelial transport of polymeric immunoglobulins, in the rat liver was assessed by measuring the SC concentration in liver homogenates of rats killed from birth to 60 days of age, and by quantifying the daily SC secretion of in vitro cultured hepatocytes isolated from rats similarly killed from 2 days before birth to 60 days of age. With both methodologies, only very small amounts of SC were produced by the rat liver up to 20 days of age, whereafter expression of SC markedly increased. The development of SC production in the rat liver was co-ordinate with that previously reported in the rat small intestine, preceding the appearance of large numbers of intestinal IgA plasmacytes. These data further emphasize the importance of the liver contribution, via the bile, to the intestinal secretory IgA system of the rat.

Aging↗
PubMed1989

Cholera toxin-induced fluid secretion in rat gut ligated loops: influence of bile from normal or cholera toxin-immunized rats.

Fresh normal rat bile premixed with cholera toxin (CT) did not significantly affect the CT-induced fluid accumulation in rat jejunal ligated loops. Bile from rats intrajejunally (i.j.) immunized three times with CT definitely inhibited CT-induced fluid secretion. Bile duct ligature (BDL) for 1-4 days in unimmunized rats, in contrast with mice, did not significantly affect subsequent CT-elicited fluid secretion in their ligated loops. BDL for 4 days in rats i.j. immunized with CT, only slightly decreased the CT-neutralizing ability of their gut loops. Passive transfer during 24 hr of bile from i.j.-immunized rats, but not from normal rats, into gut of normal recipient rats with BDL, significantly protected loops made in such recipients. The affinity-purified antibodies of immune bile, mixed with CT, neutralized its effect. Our data show that, unlike mice, rat bile acids are not required for expression of the CT effect in gut loops. In addition, bile from i.j.-immunized rats contains enough anti-CT antibodies to be protective on its own, but is not necessary for substantial gut protection against CT in i.j.-immunized BDL rats. Our results confirm a major and complementary role of both biliary and intestinal secretory IgA antibodies in protection of the rat gut mucosa against CT-induced fluid secretion.

Animals↗
PubMed1988

Activation of rat complement by soluble and insoluble rat IgA immune complexes.

The ability of rat monoclonal IgA, specific for 2,4-dinitrophenyl (DNA), to activate the complement (C) system of the rat was investigated using aggregated IgA or IgA immune complexes (IC). IgA was coated onto a solid phase, and tested for its capacity to bind C3 upon incubation at 37 degrees C in normal rat serum (NRS) in the presence of Mg-EGTA. Binding of C3 was observed dependent on the dose of dimeric (d-), polymeric (p-) and secretory IgA tested. In contrast, little C3 fixation was observed in this system with monomeric (m-) rat IgA or with mouse m- and d-IgA (MOPC315). Soluble and insoluble rat IgA IC were prepared using dinitrophenylated rat serum albumin (DNP8RSA) as antigen (Ag), and assessed for C activation. It was shown that insoluble IC (immune precipitates; IP) containing m-, d- or pIgA of rat origin activate the alternative pathway of rat C, as demonstrated by their capacity to induce C consumption in NRS in the presence of Mg-EGTA. When p- and m-IgA IP were compared for their capacity to activate C, it was found that p-IgA activated C four times as efficiently as m-IgA IP (at 2 mg/ml). Soluble rat IgA IC were prepared in an excess of DNP8RSA, fractionated by gel filtration on Sepharose 6B, and analyzed for C activation and antibody (Ab)/Ag ratio. In contrast to m-IgA IP, soluble m-IgA did not activate C. On the other hand soluble d-IgA IC activated C dependent on their concentration and size: at a concentration of 0.1 mg/ml high-molecular weight d-IgA IC with a high Ab/Ag ratio were four times as efficient as low-molecular weight IC with a low Ab/Ag ratio, and twice as efficient as IP prepared at equivalence. To demonstrate the induction by IgA of the assembly of the terminal membrane attack complex, trinitrophenyl (TNP)-conjugated rat red blood cells (TNP-RRBC) coated with d- or p-IgA were shown to be lysed in NRS in the presence of Mg-EGTA. No lysis of m-IgA-coated TNP-RRBC was observed. The results in this study demonstrate that both soluble and insoluble rat IgA IC activate the alternative pathway of homologous rat C. Alternative pathway activation by soluble rate IgA IC is dependent on the size of the IC. The degree of polymerization of the IgA Ab itself also influences C activation.

Animals↗
PubMed1988

Massive plasma cell infiltration of the digestive tract. Secretory component as the rate-limiting factor of immunoglobulin secretion in external fluids.

A 29-yr-old Tunisian man had a clinical immunoproliferative small intestinal disease, different from alpha-chain disease. Serum contained 52.5 mg/ml of polymeric immunoglobulin A (IgA). Immunohistochemistry revealed a massive diffuse polyclonal IgA (99%)-plasma cell infiltration in the small bowel mucosa, with a smaller increase of IgA-producing cells in gastric and colonic mucosae. Secretory IgA levels were normal in jejunal and bronchoalveolar secretions. However, both fluids contained polymeric IgA devoid of secretory component, and free secretory component was absent. This suggests that secretory component was the limiting factor in transport of IgA in the secretions. A relative deficiency in secretory component, as compared with the huge supply of polymeric IgA, may have limited the secretory component-mediated active transport of IgA into secretions. This resulted in the appearance of high levels of polymeric IgA, unlinked to secretory component, both in serum and in the jejunal and bronchoalveolar fluids.

Adult↗
PubMed1988

Jacalin: isolation, characterization, and influence of various factors on its interaction with human IgA1, as assessed by precipitation and latex agglutination.

An IgA1-specific lectin, Jacalin, was isolated from dried seeds of the jackfruit, Artocarpus integrifolia, by affinity binding to IgA1-Sepharose and elution with D-galactose. Jacalin is a glycoprotein with two non-covalently bound subunits (15 and 18 K). Interactions between Jacalin and human Igs were studied by precipitation in gel and in solution, and by agglutination of IgA1-coated latex by Jacalin. Jacalin precipitated only with IgA1-containing samples, including monomers, polymers, monoclonal, polyclonal and secretory IgA1, but not IgA2 of both A2m(1) and A2m(2) allotypes, nor with IgG1, 2, 3 and 4, IgM, IgD, and IgE; after neuraminidase treatment, only IgA1 and IgD were precipitated. Jacalin had a relatively broad pH range of activity in both precipitation and agglutination of IgA1-latex. Bivalent metal cations (Ca, Mg, Mn, Cu, Zn, Co, Cd), EDTA, Triton X-100, Tween-20, Na deoxycholate and ionic strength did not influence these reactions. Na dodecylsulphate, guanidine and urea inhibited the reactions whereas NP-40 rather enhanced them. Among 39 types of sugar tested, 10 displayed inhibitory activity, decreasing in the following order: p-nitrophenyl-alpha-D-galactopyranoside, 1-O-methyl-alpha-D-galactopyranoside, D-melibiose, p-nitrophenyl-beta-D-galactopyranoside, GalNAc, stachyose, 1-O-methyl-alpha-D-mannopyranoside, D-galactose, D-galactosamine and 1-O-methyl-alpha-D-glucopyranoside. IgA1, treated with neuraminidase or not, but not the other human Igs, was also an excellent inhibitor of agglutination, being more powerful than the best sugars studied. Only neuraminidase-treated IgD was also inhibitory, but less so than IgA1. Jacalin preferentially bound to alpha-linked non-reducing D-galactose. The configuration of OH-groups at C-2, C-4 and C-6 of D-galactose was important for the reaction. Jacalin recognizes terminal Gal beta 1-3GalNac-, as in the IgA1-hinge, and/or GalNAc-, but not Gal beta 1-4GlcNAc-, nor Gal beta 1-6GlcNAc-, nor their sialylayted extensions. Latex agglutination and its inhibition assay are particularly well suited for the study of these lectin-glycoprotein interactions.

Agglutination↗
PubMed1988

Cholera toxin neutralization: a comparison of purified serum IgG and biliary secretory IgA antibodies.

Rats were immunized three times with cholera toxin via the intraintestinal or intravenous route, and their respective biliary secretory IgA (sIgA) or serum IgG antibodies were affinity-purified on a cholera toxin immunoabsorbent. On a molar basis, the sIgA antibodies were roughly seven-fold more efficient than IgG antibodies in neutralizing cholera toxin in the ligated intestinal loop assay. Various explanations for this difference in neutralizing capacity are proposed.

Animals↗
PubMed1988

IgA immune response patterns to gliadin in serum.

The incidence, titer and molecular size of anti-gliadin (GL) IgA were analyzed in sera from children with celiac disease (CD, n = 66), hospitalized control children (n = 64) and children with other malabsorption disorders (n = 103). Anti-GL IgA was assessed by solid-phase radioimmunoassay, and its molecular size was analyzed by sucrose density gradient ultracentrifugation. The median anti-GL IgA titer was significantly higher in untreated CD than in the other groups, with some overlap. Whereas 57% of anti-GL IgA were polymeric IgA (pIgA) in acute CD, only 17% were pIgA in children with other malabsorption disorders. These anti-GL pIgA consisted mainly of dimers with in some children, a low proportion of anti-GL secretory IgA (SIgA). A large proportion of anti-GL pIgA was associated with high total serum IgA. After the onset of a gluten-free diet (GFD), anti-GL pIgA disappeared more quickly from serum than mIgA. During the gluten challenge test, anti-GL IgA comprised 20% pIgA when they reappeared in serum, but 59% pIgA at the end of the test. The presence of anti-GL pIgA in serum seems related to chronic exposure to gluten of CD patients with a flat intestinal mucosa. These serum pIgA antibodies could result from a spillover from the intestinal mucosal synthesis into the circulation.

Antibodies, Anti-Idiotypic↗
PubMed1988

Selectivity, specificity and kinetics of the androgen regulation of the ocular secretory immune system.

The purpose of the present investigation was to determine the selectivity, specificity and kinetics of the androgen regulation of the ocular secretory immune system. To examine the mucosal selectivity of hormone action, tears, saliva, respiratory and intestinal secretions, urine and serum were collected from orchiectomized rats following four days of treatment with saline or testosterone. Androgen administration significantly increased the tear levels of IgA and free SC. In contrast, this combined hormone response was not duplicated in other mucosal secretions or serum. Consequently, it appears that the androgen control of the ocular secretory immune system is unique to the eye. To evaluate androgenic specificity, orchiectomized rats were treated for four days with saline, testosterone, 5 alpha-androstan-17 beta-o1 ('5 alpha'), 4-estren-7 alpha-methyl-17 beta-o1-3-one ('4-E') or the synthetic analogue, danazol. Results demonstrated that testosterone and '4-E', a potent androgen, both stimulated the accumulation of tear IgA and free SC, compared to amounts in tears of saline-treated controls. The weak androgen '5 alpha' induced a slight rise in tear free SC, but not IgA, levels, whereas danazol had no effect on the ocular secretory immune system. These findings indicate that androgen structure is of critical importance in modulation of mucosal immunity in the eye. Lastly, to assess the kinetics of hormone action on tear IgA and free SC, orchiectomized rats were acutely (0, 1.5, 4, 7, 12, or 24 hours) or chronically (0, 4, 7, 11, 14, or 17 days) exposed to testosterone. Acute androgen exposure for less than 12 hours did not elicit any change in the tear content of IgA or free SC. In comparison, chronic androgen treatment induced a progressive and dramatic rise in the levels of both tear proteins. By 17 days of hormone exposure, the IgA and free SC concentrations in tears had increased by 14- and 18-fold amounts, respectively, relative to amounts in placebo-treated controls. Of interest, the temporal pattern of accumulation of tear IgA and free SC were different. Overall, these results show prolonged, but not abbreviated, exposure to androgens has a profound impact on the IgA and free SC profile in tears.

Androgens↗
PubMed1987

IgA-induced chemokinesis of human polymorphonuclear neutrophils: requirement of their Fc-alpha receptor.

The influence of purified human immunoglobulins on the migration of human neutrophils (PMN) was measured in a 48-well micro chemotaxis chamber, with results expressed as percentages of maximal formyl-methionyl-leucyl-phenylalanine (FMLP)-stimulated chemotaxis. Both monomeric and polymeric IgA, of both subclasses, in monoclonal and polyclonal form, as well as secretory IgA and Fc-alpha, but not Fab-alpha fragments, enhanced PMN migration when present either in the lower or in both compartments of the chamber (chemokinesis) at concns as low as 0.1 mg/ml. IgM and IgE had no such effect. In contrast, IgG was chemotactic at low concn (0.1 mg/ml). Both monomeric and polymeric IgA decreased the maximally induced FMLP-chemotaxis, but IgA increased chemotaxis induced by suboptimal levels of FMLP. Binding of 3[H]-FMLP to PMN was not affected. Cytofluorographic analysis revealed that, under the conditions of the assay, IgA did bind to 93% of PMN. Thus, the various forms of IgA have a dual effect on human PMN mobility: (1) increase PMN random migration (chemokinesis); and (2) decrease the maximal FMLP-induced chemotaxis. Our data support the requirement of binding of IgA to the Fc-alpha receptor of PMN for expression of these activities. This effect of IgA on PMN mobility may be relevant in IgA deficiency states.

Antibodies, Monoclonal↗
PubMed1987

Complement-mediated solubilization of rat IgA immune precipitates.

The complement-mediated solubilization (CMS) of immunoprecipitates (IP) consisting of DNP-rat serum albumin (RSA) and rat monoclonal anti-DNP antibodies of the IgA [both polymeric (p-) and monomeric (m-)] or IgG2b (sub)class was studied. In contrast to IgG2b IP, solubilization of IgA IP was only observed in an autologous system, with rat serum as the source of complement. IP prepared using m-IgA were solubilized faster than those prepared using p-IgA. Analysis of both affinity and avidity of the antibodies, indicated that this difference may be due to the lower avidity of the m-IgA antibodies as compared to p-IgA. Analysis of the solubilized IP revealed deposition of C3 and C4 on IgG2b, and only C3 on IgA IP. These results point toward a role of the alternative pathway in the solubilization of IgA IP. Size analysis of the solubilized IgA IP employing sucrose density gradient ultracentrifugation, indicated that these were heterogeneous, with a size generally larger than 19 S.

Animals↗