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PubMed1989

Secretory immunoglobulin A in urinary tract infection, chronic glomerulonephritis, and renal transplantation.

An enzyme-linked immunoassay (ELISA) for the quantitation of secretory IgA (S-IgA) in the urine is described. The assay is sensitive (linear down to 0.02 microgram/ml), specific, and reproducible (intraassay variation 7.8%, interassay variation 18.9%). The assay was used to determine the urinary excretion rates of S-IgA in patients with bladder catheter (n = 12), cystotomy and urinary tract infection (n = 13), urosepsis (n = 5), chronic glomerulonephritis, including IgA-nephritis (n = 31), in renal allograft recipients (n = 30), and in healthy controls (n = 46). An elevated S-IgA urinary excretion (P less than 0.01) was found in all patient groups studied. The highest values were observed in urosepsis. No significant differences between S-IgA levels in IgA-nephritis and other forms of chronic glomerulonephritis were detected. The elevated S-IgA excretion in renal allograft recipients indicates that immunosuppressive therapy does not influence the local S-IgA production in the urinary tract. The susceptibility of these patients to urinary tract infections is therefore not due to a S-IgA deficiency.

Diuresis↗
PubMed1989

Regulation of the production of secretory and membrane immunoglobulin during lymphocyte development.

An area of great controversy in molecular immunology is the mechanism by which the differential expression of secretory and membrane immunoglobulin heavy chain is regulated during B cell development. Since the changes in expression of the two proteins are determined largely by the steady state levels of the mRNAs that encode them, recent work has focused on the regulation of the expression of the two messages. This problem is central to understanding humoral immunity, with the specific antigen driven switch from antibody as receptor to antibody as secreted product and may be of direct relevance to some forms of the common variable immunodeficiency syndrome. In addition, numerous other genes have been shown to be regulated by alternative RNA processing. Since its beginnings, research in immunology has brought about profound changes in our view of biology. Jenner's landmark experiment, inducing a minor illness to prevent a major one, showed that the body's future susceptibility to a particular disease could be manipulated. More recently the demonstration that immunoglobulin V, D, and J gene segments, originally spread over many kilobases (kbs) in the genome, must be assembled to form a functional heavy chain gene has shattered both the concept of a genome fixed at fertilization and the "one gene, one protein" rule. The alternative processing of heavy chain transcripts to produce secretory and membrane forms of immunoglobulin has demonstrated how the same gene can give rise to proteins with alternative structures. Since the discovery of the role of alternative RNA processing in heavy chain mRNA synthesis, numerous other cellular genes have been shown to be regulated by modulation of RNA processing pathways.

Animals↗
PubMed1991

Immunoglobulin concentrations in nasal secretions differ between patients with an IgE-mediated rhinopathy and a non-IgE-mediated rhinopathy.

Nasal secretions from patients with an IgE-mediated rhinopathy, patients with a non-IgE-mediated rhinopathy, and healthy control subjects were collected with a newly developed direct aspiration system. Total protein, albumin, secretory IgA (sIgA), IgE, IgG, and IgM concentrations were measured in the nasal secretions to detect whether the nasal pathology is reflected in nasal secretion protein concentrations. It was found that protein and immunoglobulin concentrations in nasal secretions were inversely related to amount of secretion in the nasal cavity. Both patients' groups had a significantly higher sIgA to protein ratio than the healthy control subjects. Furthermore, patients with an IgE-mediated rhinopathy had significantly higher sIgA and IgM to total protein ratios in their nasal secretions than patients with a non-IgE-mediated rhinopathy. Probably these differences are due to changes in immunoregulation.

Adolescent↗
PubMed1985

Transcytosis.

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Animals↗
PubMed1991

Selective inhibition of transcytosis by brefeldin A in MDCK cells.

Treatment of most cells with brefeldin A (BFA) leads to the retrieval of the Golgi complex to the endoplasmic reticulum, presumably reflecting an inhibition of cytoplasmic coat protein binding to Golgi membranes. Although BFA has been thought to act only on biosynthetic organelles, we now show that this drug also reversibly blocks polymeric immunoglobulin receptor-mediated transcytosis in MDCK cells. The action of BFA on transcytosis was selective, since internalization, recycling, and intracellular degradation were unaffected. The block occurred early on the transcytotic pathway, probably before the translocation of IgA-containing vesicles from the basal to the apical cytoplasm. Although BFA caused MDCK cell endosomes to become more tubular, the organization of the Golgi and binding of the 110 kd Golgi coat protein beta-COP was surprisingly unaffected. These results suggest that in MDCK cells, endocytic organelles contain a BFA-sensitive coat that regulates their organization and function even though the Golgi coat is BFA resistant.

Animals↗
PubMed1993

Interferon-gamma induces polymeric immunoglobulin receptor mRNA in human intestinal epithelial cells by a protein synthesis dependent mechanism.

Transport of secretory IgA into external fluids is mediated by the polymeric immunoglobulin receptor (pIgR) on the surface of mucosal epithelial cells. We studied the mechanism by which interferon-gamma (IFN-gamma) induces pIgR expression in HT-29.74 cells, a subclone of the HT-29 cell line selected for high concns of pIgR. Here we report the isolation of genomic DNA and cDNA clones encoding human pIgR and development of a sensitive ribonuclease protection assay for pIgR mRNA. This assay was used to determine if induction of pIgR by IFN-gamma is mediated by accumulation of pIgR mRNA. After an initial lag of 12 hr, pIgR mRNA increased seven-fold in response to IFN-gamma, reaching a plateau at 24 hr. Concentrations of pIgR protein also increased seven-fold, but the increase was delayed until 48 hr following stimulation with IFN-gamma. Cycloheximide treatment abolished the IFN-gamma induced increase in pIgR mRNA, indicating that induction of pIgR mRNA by IFN-gamma requires de novo protein synthesis. These results suggest that induction of pIgR expression by IFN-gamma involves an increase in steady-state concns of pIgR mRNA via a protein synthesis dependent mechanism.

Amino Acid Sequence↗
PubMed1994

Expression and purification of biologically active domain I of the human polymeric immunoglobulin receptor.

Previous studies using proteolytic fragments and synthetic peptides have indicated that domain I of human polymeric immunoglobulin receptor (PIgR) is necessary for ligand binding. The expression in E. coli, and subsequent IgM-affinity purification of domain I of human PIgR is described. The recombinant domain I protein (rDI) was similar in structure to native SC domain I in that it bound specifically to MAb 6G11, an antibody which recognizes a critical portion of the PIg binding site in domain I. The biological activity of rDI was indicated by high affinity binding to PIgA (Kd = 1.6 x 10(-7) M) and IgM (Kd = 5.1 x 10(-7) M). Domain I of human SC is therefore sufficient for binding to PIg.

Amino Acid Sequence↗
PubMed1986

Monoclonal antibodies to distinct epitopes on human IgA and their use to IgA determination.

Several monoclonal antibodies (MAbs) against human IgA have been obtained which specifically bind to human myeloma and polyclonal IgA. Three of these MAbs have been purified and studied further. They recognize both IgA subclasses and define three distinct epitopes on the IgA molecule. These MAbs were used to develop a solid-phase radioimmunoassay (RIA) in which one MAb was immobilized and the other two were labeled with 125I. The assay has a sensitivity in the nanogram range. A good correlation was found (r = 0.97, P less than 0.001) when the solid-phase RIA was compared with a commercially available immunodiffusion technique for the determination of IgA levels in serum samples.

Antibodies, Monoclonal↗
PubMed1990

Proteolytic processing of chromogranin A in cultured chromaffin cells.

The prohormone chromogranin A is the major soluble component of secretory granules in chromaffin cells of adrenal medulla and in many other different endocrine cell types. The proteolytic processing of chromogranin A was studied in cultured bovine chromaffin cells using [35S]methionine to label proteins and a specific antibody to immunoprecipitate the native protein and its breakdown products. In resting cells, it was found that the degradation of chromogranin A is a slow process, since no degradation was observed after a 40 h incubation with radiolabelled methionine. Stimulation of cells with a single pulse or with successive pulses of nicotine did not significantly enhance the degree of proteolytic processing of chromogranin A. As it has recently been shown (Simon, J.P., Bader, M.F. and Aunis, D. Biochem. J. (1989) 260, 915-922) that protein kinase C may be involved in the regulation of chromogranin A synthesis, the possibility that prohormone processing may also be controlled by protein kinase C was examined using the activator of protein kinase C, 12-O-tetradecanoylphorbol 13-acetate (TPA). However, incubation of cells with TPA did not significantly modify chromogranin A processing, indicating that biosynthesis and proteolytic processing of chromogranin A are two distinctly regulated mechanisms. Glucocorticoids are known to exert regulatory control of chromaffin cell metabolism; however, incubation of cells with dexamethasone did not alter slow chromogranin A processing. Stimulation of labelled cells rapidly released newly synthesized chromogranin A into external medium. In addition, released chromogranin A was found to be actively processed into its 60 kDa and 43 kDa breakdown products. This extracellular proteolytic degradation mechanism may be of importance with regard to the function of chromogranin A as a prohormone.

Animals↗
PubMed1993

Calcium-induced secretion from permeabilized rat mast cells: requirements for guanine nucleotides.

Cells used in this work were permeabilized by streptolysin-O and then washed to remove freely soluble components. The secretory responsiveness of these cells to various combinations of calcium, MgATP and guanine nucleotide was characterized and in most respects was found to be similar to that of the metabolically inhibited (unwashed) cells. The content of adenosine and guanine nucleotides, which remain within the permeabilized cells after washing, was estimated as 0.83 and 0.12 mM (extrapolated to intact cells), which constitutes 18 and 25%, respectively, of the total nucleotide content of mast cells. High (> mM) concentrations of MgATP, required for the calcium-induced secretion, were reduced to microM levels by suboptimal concentrations of GTP, which also markedly increased both the rate and extent of the response. Similarly, microM concentrations of MgATP reduced the requirements of the calcium-dependent secretion for GTP. The synergy of the GTP and ATP effects suggests that, together, the two nucleotides can maintain a pool of free GTP, presumably as a result of transphosphorylation from ATP to GDP. Thus, MgATP may work by transphosphorylating the endogenous GDP. However, neither GTP nor GTP-gamma-S were effective as substitutes for MgATP in the calcium-induced secretion, particularly that from metabolically inhibited cells. This indicates that MgATP does not act simply by providing GTP but is needed to maintain a phosphorylated state of the system. The synergistic effects of ATP and GTP were observed only in the presence of calcium. To test whether calcium/MgATP-induced secretion requires an activated G protein, the effects of G-protein inactivators were studied. GDP, deoxy GDP and GDP-beta-S exerted differing degrees of inhibition on secretory responses induced by various combinations of effectors. The response to calcium/MgATP was less sensitive to these inhibitors than that to GTP-gamma-S (with or without calcium). However, all three 'inhibitors' were also capable of stimulating calcium/MgATP-dependent secretion, indicating a transphosphorylation, producing GTP, dGTP and GTP-beta-S. Thus, in the absence of any specific inhibitors for either G proteins or the transphosphorylation reaction, the degree of dependence of the calcium-induced secretion on a G protein remains unclear.

Adenine Nucleotides↗
PubMed1991

Detergent enhances binding of a secreted HLA-A2 molecule to solid phase peptides.

We have constructed a secreted analogue (sA2) of the human class I molecule HLA-A2. sA2 was affinity purified both in the presence and absence of detergent and the effects of detergent on the magnitude and specificity of A2 binding to solid phase peptides tested. sA2 purified in the presence of detergent and detergent-solubilized A2 are shown to function comparably in the binding of the synthetic peptide M.Y + 57-68, a known T-cell epitope derived from the influenza A matrix protein. The molecules binding to M.Y + 57-68 typically represent 8% to 10% of the added protein. In contrast, less than 1% of sA2 protein purified in the absence of detergent binds M.Y + 57-68. This reduced binding is not due to a change in the affinity of sA2 for M.Y + 57-68. Addition of detergent at various stages of the purification and iodination procedures indicates that the longer the sA2 molecules are exposed to detergent the better they bind. However, the concentration of detergent during the actual binding assay does not appear to be critical. We also find that while the sA2-detergent and the sA2-no detergent molecules differ in the extent to which they bind various peptides, they do not differ in their patterns of binding. We conclude that detergent probably does not influence the specificity of class I/peptide binding but does increase the number of sA2 molecules that can participate in the binding of peptide either by generating and stabilizing "empty" sA2 molecules or by stabilizing a structure that is more amenable to binding peptide.

Amino Acid Sequence↗
PubMed1995

Polymeric-Ig receptor gene expression in rabbit mammary gland during pregnancy and lactation: evolution and hormonal regulation.

The polymeric immunoglobulin receptor (poly Ig-R) mediates transcytosis of IgA and IgM antibodies produced by local plasma cells across epithelial cells of mucosal and glandular tissues. Gene expression of the poly-Ig R was analyzed in rabbit mammary gland during pregnancy and lactation. The poly Ig-R was expressed as early as day 8 (G8) of gestation and mRNA accumulation remained low until about G18. From G21, the mRNA abundance increased and reached steady state levels approximately 5-fold higher at day 15 of lactation (L15) when compared to basal levels at G8. The hormonal regulation of poly-Ig receptor gene expression was assessed in mammary organ cultures. Poly-Ig R mRNA accumulation in mammary explants cultured for 24 or 48 h in the presence of ovine prolactin (oPRL) was significantly increased to a maximal 4-fold level at 1 microgram ml-1 of oPRL. Estradiol (100 pg ml-1) or progesterone (1 microgram ml-1) did not further stimulate poly-Ig R expression. In contrast, their combination resulted in a significant 30-50% decrease of poly-Ig-R mRNA levels. The addition of 1 microgram ml-1 of cortisol to medium in the absence or presence of estradiol or progesterone decreased the amount of poly-Ig-R mRNA. The results suggest that until mid-pregnancy, poly-Ig-R expression is inhibited by elevated progesterone-estradiol concentrations and that the subsequent increase is due to the concomitant decrease of the two circulating steroids and the increase of serum prolactin levels.

Animals↗
PubMed1992

Proteolytic enzymes from Trichinella spiralis larvae.

Trichinella spiralis larvae infect their hosts by the penetration of small intestine enterocytes. The exact mechanism of penetration is unknown, but the presence of proteolytic enzymes is suspected. In this study, whole worm extracts and excretory-secretory (ES) components were obtained and their proteolytic enzymes examined. Enzymes from worm extracts were capable of hydrolysing azocoll, a general protease substrate in a wide range of pH (2-8), with maximal activity at pH 5. Trichinella spiralis larval enzymes were sensitive to metalloprotease and serine protease inhibitors. Three proteases were identified in worm extracts at molecular weight (MW) 48, 54 and 62 kDa by incorporating a gelatine substrate into a standard or a modified sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) set-up, in which we used low SDS concentration in gel and electrophoresis buffer (0.01%). Intact larvae incubated in a medium containing azocoll showed azocollytic activity. Subsequent analysis of ES products by modified SDS-PAGE in gels containing gelatine demonstrated the presence of three protease of apparent MW 33, 62 and 230 kDa.

Animals↗
PubMed1983

Relationship between the secretor status and the expression of ABH blood group antigenic determinants in human intestinal brush-border membrane hydrolases.

At least six hydrolases of the human intestinal brush-border membrane bear ABH blood group antigenic determinants related to the erythrocyte phenotype: the intestinal glycoproteins of blood group A and B subjects express A or B determinants, respectively, while blood group O subjects express the H determinant identified with Ulex europaeus lectin I. These expressions are under the control of the secretor gene: ABH antigens were not detected in the hydrolases of non-secretor subjects.

ABO Blood-Group System↗