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At least 559 records · Page 31Linked to original sources
PubMed1983

Primary cultures of rat hepatocytes as a model system of canalicular development, biliary secretion, and intrahepatic cholestasis. III. Properties of the biliary transport of immunoglobulin A revealed by immunofluorescence.

The present study was designed to investigate whether or not the vesicle-mediated, biliary transport of polymeric immunoglobulin A operates in primary cultures of rat hepatocytes. Using immunofluorescence techniques, immunoglobulin A of human or rat origin added to a time-dependent process around and within presumptive bile canaliculi. As a transitory event preceding this accumulation, an intensive particulate fluorescence was detected within the cytoplasm of the hepatocytes. Secretory component could be localized by a faint fluorescence in the cytoplasm and at the margin of bile canaliculi, where the fluorescence was accentuated concomitantly to the accumulation of immunoglobulin A. Translocation of immunoglobulin A could be blocked by an antiserum against secretory component, whereas colostral immunoglobulin A already containing secretory component was not transported. These findings suggest that the pathway for the biliary secretion of immunoglobulin A is active in cultured hepatocytes and provide evidence for the reconstruction of a functionally intact biliary polarity by these cells.

Animals↗
PubMed1998

Excretory-secretory antigenic components of adult Fasciola gigantica recognized by infected human sera.

The immunogenic components of Fasciola gigantica excretory-secretory (ES) products were revealed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting technic using sera from patients with F. gigantica infection, from patients with clinical suspected fascioliasis, from patients with other illness and from healthy adults. By SDS-PAGE, it was found that the ES products comprised more than 6 polypeptides. Immunoblotting analysis revealed 12 components which were strongly recognized by fascioliasis antisera. These antigenic components had a molecular mass ranging from less than 14.4 to 38 kDa. One antigenic band of 27 kDa was found to give a consistent reaction with fascioliasis antisera (100% sensitivity and 98% specificity). The present findings suggest that the 27 kDa components are sensitive and specific for the diagnosis of human F. gigantica infection.

Adult↗
PubMed1982

Autoantibody activities of human IgM M-components.

By means of indirect immunofluorescence microscopy we have shown that 11 out of 18 (61%) IgM M-components from patient sera had affinity for various tissue structures. The great variation in affinity patterns, and the high titres support the antigen-antibody mode of interaction. The high incidence of activity against smooth muscle (4/18) shown in this study, and against IgG, and red blood cell antigens shown by others indicates that the onset of IgM M-component production is initiated in situations where a polyclonal IgM-antibody response is the rule. Beside specific antibody activities, the M-components tested showed affinity for gastric epithelium and hepatocytes. The titres correlated roughly to the serum concentrations of IgM, and the patterns corresponded to the localization of secretory component as shown by others indicating a non-antigen--antibody reaction between the IgM M-components and secretory component.

Animals↗
PubMed1992

Cytoskeleton and molecular mechanisms in neurotransmitter release by neurosecretory cells.

The process of exocytosis is a fascinating interplay between secretory vesicles and cellular components. Secretory vesicles are true organelles which not only store and protect neurotransmitters from inactivation but also provide the cell with efficient carriers of material for export. Different types of secretory vesicles are described and their membrane components compared. Associations of several cytoplasmic proteins and cytoskeletal components with secretory vesicles and the importance of such associations in the mechanism of secretion are discussed. A description of possible sites of action for Ca2+ as well as possible roles for calmodulin, G-proteins and protein kinase C in secretion are also presented. Important aspects of the cytoskeleton of neurosecretory cells are discussed. The cytoskeleton undergoes dynamic changes as a result of cell stimulation. These changes (i.e. actin filament disassembly) which are a prelude to exocytosis, play a central role in secretion. Moreover, advanced electrophysiological techniques which allow the study of secretory vesicle-plasma membrane fusion in real-time resolution and at the level of the single secretory vesicle, have also provided a better understanding of the secretory process.

Calmodulin↗
PubMed1976

The presence of secretory component-free human colostral IgA in early colostrum.

Human secretory IgA was prepared from colostrum. Different elution diagrams from CM-cellulose were obtained depending on the time of collection of colostrum. In case of early colostrum, collected within 6 hours post partum, two IgA fractions were obtained after chromatography on CM-cellulose. Both fractions have different molecular weights and different amino acid compositions. The results obtained suggest that the first fraction is a dimer of IgA monomers containing J chain with a molecular weight of 330,000 whereas the second fraction having the molecular weight 395,000 daltons is composed of IgA dimer, J chain and SC. When colostrum collected 48 or more hours was used as a source of IgA, only the second IgA fraction was obtained. The problem of SC-free IgA immunoglobulins is discussed.

Amino Acids↗
PubMed1992

Redistribution of secretory granule components precedes that of synaptic vesicle proteins during differentiation of a neuronal cell line in serum-free medium.

Incubation of the rat sensory neuron-derived cell line ND7 in serum-free medium results in the arrest of mitosis and the appearance of numerous neuronal processes. During this differentiation event, secretory granule components such as chromogranins, neuropeptide Y and the C-flanking peptide of pro-neuropeptide Y move to the tips of the majority of the neuronal processes regardless of process length. In contrast, the synaptic vesicle component, synaptophysin, is found only at the tips of the very long processes which appear following prolonged periods of culture in serum-free medium. A similar restriction of synaptophysin to long processes is also observed following differentiation and process formation induced by other treatments such as incubation in reduced serum or treatment with cyclic AMP or phorbol myristate acetate. Hence the regulated secretory pathway associated with the chromogranins and neuropeptides appears to be segregated into the processes at an earlier stage of ND7 differentiation than the synaptophysin-associated synaptic vesicle pathway. ND7 cells therefore provide a model system for studying the processes regulating these pathways and the redistribution of their components during neuronal differentiation.

Animals↗
PubMed1982

Receptors for IgA on rabbit lymphocytes. II. Characterization of their binding parameters for IgA.

The specificity of rabbit receptors for IgA (RFc alpha) was investigated on lymphocytes isolated from the Peyer's patches and spleen. Specifically was determined by the inhibition of IgA rosette formation with intact and proteolytic fragments of rabbit and human secretory IgA (SIgA), human myeloma proteins, and secretory component. RFc alpha bound human SIgA as efficiently as rabbit SIgA. Of the human IgA tested, RFc alpha preferentially bound to the IgA2 subclass and most avidity to a multimeric IgA molecule. In addition., the site of the RFc alpha-IgA interactions was localized to the C alpha 2 domain in the Fc portion of IgA. RFc alpha on spleen lymphocytes showed the same pattern of binding specificity toward the human IgA subclasses as the RFc alpha on lymphocytes from Peyer's patches. However, differences between the spleen and Peyer's patches were observed in the interaction of RFc alpha and the rabbit IgA subclasses. RFc alpha on lymphocytes from the Peyer's patches bound the rabbit IgA-g subclass more efficiently than the rabbit IgA-f subclass, whereas the converse was true for the spleen RFc alpha. Human secretory component inhibited IgA but not IgG or IgM rosette formation as a result of its interaction with lymphocytes. These studies suggest: 1) that there may be two types of RFc alpha expressed by lymphocytes in certain tissues, and 2) that there are two closely associated receptors on the lymphocyte--one specific for secretory component and the other for structures within the C alpha 2 domain of IgA.

Animals↗
PubMed1994

Disulfide bond formation between dimeric immunoglobulin A and the polymeric immunoglobulin receptor during hepatic transcytosis.

The polymeric immunoglobulin receptor on rat hepatocytes binds dimeric IgA on the sinusoidal surface and mediates its transport to the canaliculus, where the complex of dimeric IgA and secretory component, the cleaved extracellular domain of polymeric immunoglobulin receptor, is secreted into bile. This process is unique in that disulfide bonds are formed between dimeric IgA and polymeric immunoglobulin receptor during transcytosis, permanently preventing their dissociation. Here we present three lines of evidence that disulfide bonding between dimeric IgA and polymeric immunoglobulin receptor occurs predominantly in a late transcytotic compartment and that hepatic transcytosis can proceed in the absence of disulfide bond formation. First, throughout the course of transcytosis the percentage of intracellular dimeric IgA disulfide bonded to polymeric immunoglobulin receptor is less than half that in bile, suggesting that disulfide bond formation is a late event in transcytosis. Second, dimeric IgA that recycles from early endocytotic compartments into the circulation is mostly noncovalently bound to secretory component. Finally, the rate of transcytosis of dimeric IgA and its appearance in bile are not affected when disulfide bond formation with polymeric immunoglobulin receptor is inhibited by blocking of free thiol groups on dimeric IgA with iodoacetamide. These results are consistent with other findings in the literature and indicate that the main physiological role of disulfide bond formation between dimeric IgA and polymeric immunoglobulin receptor is not to facilitate transcytosis but, rather, to stabilize the dimeric IgA-secretory component complex after its release into external secretions such as bile and intestinal secretions.

Animals↗
PubMedDate not supplied

Immunopathological study of the larynx. IgA distribution and secretory activity.

Using immunofluorescent and histopathological techniques, we studied the distribution and secretory activity of the glands of the larynx from 55 humans. The cavity of the larynx was covered with secretory glandular cells with the exception of the true vocal cords, aryepiglottic folds and upper part of the laryngeal surface of the epiglottis. Immunofluorescent study revealed the presence of IgG and other immunoglobulins throughout the connective tissue ground in each laryngeal mucosa. The most striking was seen in the staining pattern of IgA. Diffuse fluorescence for IgA was observed not only in the submucosal or periglandular connective tissue area but also in the intraeptithelial or submucosa glands. Secretory component synthesis was found mainly in each serous-type glandular epithelium or acinus. In the submucosa or periglandular area, IgA producing plasma cells were numerous. Our observations suggest that IgA, produced locally, is secreted via the glandular cells as secretory component--SIgA. Secretory activity of SIgA in these glandular tissues indicates that the larynx is possibly an immunologically active organ in the upper respiratory tract.

Adolescent↗
PubMed1987

Transport defect of IgM into luminal space in selective IgA deficiency.

This study explored the pathogenesis of a transport defect of IgM into the lumen in a patient with selective IgA deficiency. In addition to the absence of IgM in the saliva, no IgM was localized on the luminal surface of colonic mucosa from the patient despite the presence of J chain-positive IgM cells. On tissue sections, IgM cells did not bind secretory component. The serum IgM also showed a negligible capacity to bind secretory component in vitro. Such abnormalities of IgM molecules as stated above seem to be clinicopathologically linked with IgA deficiency or its associated Sjögren's syndrome.

Biological Transport↗
PubMed1977

A sensitive method for specific quantitation of secretory IgA.

A method to quantitate specifically secretory IgA (SIgA) has been developed using the enzyme-linked immunosorbent assay. The IgA in the test sample was adsorbed to anti-alpha antibodies attached to plastic tubes via a cost of IgA myeloma protein. The reacted SIgA was determined using anti-secretory component antiserum conjugated with alkaline phosphatase. The technique permitted quantitation of secretory IgA in biological fluids like milk, urine, and saliva with a reproducibility of +/-7%, down to 0.03 mg/l. In contrast to earlier techniques, the presence of up to 157% of serum IgA without secretory component (SC) and free SC did not disturb the measurements of SIgA. Furthermore, variations in pH and osmolarity, within biological ranges in secretions, did not influence the estimations.

Animals↗
PubMedDate not supplied

Secretory IgA epitopes in basal tears of extended-wear soft contact lens wearers and in non-lens wearers.

PURPOSE: To determine secretory IgA epitopes in tears of extended-wear soft contact lens wearers and non-wearing controls. METHODS: We developed enzyme-linked immunosorbent assays (ELISA) to determine the tear concentrations of two epitopes of secretory IgA, the IgA alpha-chain and the secretory component. These epitopes were measured in basal tears of 20 individuals in 6 nights of extended wear of etafilcon A soft contact lenses and in 19 non-lens-wearing individuals. RESULTS: Levels of IgA alpha-chain immunoreactivity were significantly decreased in the lens-wearing group compared to non-lens wearers. However, the level of secretory component immunoreactivity was not significantly different between groups. IgA alpha-chain and secretory component immunoreactvity were highly correlated; however, some samples showed a marked variation between these two values. CONCLUSION: Tear concentrations of sIgA epitopes are significantly reduced in extended-wear contact lens wearers, and may contribute to the increased susceptibility to ocular infection seen in this group.

Adult↗
PubMed1990

A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact.

In addition to the induction of tumor regression, tumor necrosis factor (TNF) has been implicated as the causative agent in a number of pathologies, including cachexia, septic shock, rheumatoid arthritis, autoimmunity, and induction of HIV expression. We propose that this complex physiology might be manifest by different forms of TNF: the 17 kd secretory component, the 26 kd transmembrane form, or both. To determine whether the 26 kd form of TNF was biologically active and whether its biology differed from that of the secretory component, we generated uncleavable and solely secretable mutants of TNF and studied their biological activities. We found that an uncleavable mutant of the 26 kd cell surface transmembrane form of TNF kills tumor cells and virus-infected cells by cell-to-cell contact, and that TNF need not be internalized by its target to kill. Thus, the 26 kd integral transmembrane form of TNF may function in vivo to kill tumor cells and other targets locally in contrast to the systemic bioactivity of the secretory component.

Amino Acid Sequence↗
PubMed1976

Immunoglobulins in fluid from non-keratinizing jaw cysts.

Thirty-six fluids from non-keratinizing jaw cysts have been examined together with autologous sera by immunoelectrophoresis and double diffusion in agar or agrose gels. Except for one cyst fluid which contained electrophoretically homogeneous ("monoclonal") IgG of the kappa type together with free kappa chains, IgG of cyst fluid was electrophoretically heterogeneous. For the most, IgA of cyst fluid migrated more slowly than IgA of serum, whereas the IgM migrated similarly. The three immunoglobulins showed reactions of antigenic identity with the corresponding Ig classes of serum when examined with rabbit antisera against human IgG, IgA, and IgM. Fluid from the median palatine cyst contained secretory component, which showed a reaction of identity with free secretory component isolated from human saliva, and probably also IgA of the secretory type. Two cyst fluids also precipitated a component in rabbit serum.

Cysts↗
PubMed1988

Quantitation of human serum polymeric IgA, IgA1 and IgA2 immunoglobulin by enzyme immunoassay.

This report concerns the relative quantitation of serum polymeric IgA and polymeric IgA subclass concentrations by enzyme immunoassay (EIA). The assay relies on the specific binding of polymeric IgA to secretory component. Competition between pentameric IgM and polymeric IgA for binding to secretory component was observed. Thus, samples were adsorbed for IgM by affinity chromatography before the EIA was performed. The assay was used to determine an age-related range of serum polymeric IgA concentrations and to compare the polymeric IgA concentrations in patients with IgA nephropathy (n = 50) to those of controls (n = 50). The serum concentrations of both polymeric IgA and polymeric IgA1 increased with age reaching adult values of around 12 years of age. Polymeric IgA2 concentrations did not reach adult levels until 18 years of age. The ratio of the polymeric IgA concentration to the total serum IgA concentration was found to be significantly increased in children under 2 years of age compared with those over 4 years of age (Mann-Whitney U-test, P less than 0.01). Patients with IgA nephropathy had significantly increased concentrations of polymeric IgA (P = 0.001) and polymeric IgA1 (P = 0.001) but similar polymeric IgA2 concentrations to controls.

Adolescent↗
PubMedDate not supplied

Characteristics of serum IgA and liver IgA deposits in alcoholic liver disease.

Patients with alcoholic liver disease frequently reveal an increase in IgA serum concentration and IgA deposits in a continuous pattern along hepatic sinusoids. We investigated whether the hepatic IgA deposits are a passive reflection of changes in concentration or composition of IgA in the circulation, or represent a distinct effect of alcohol on the liver. Forty-one patients with alcoholic liver disease (daily alcohol intake at least 50 gm for more than five consecutive years) were compared with 41 patients with nonalcoholic liver disease. Patients in both groups were matched for serum IgA and histopathological changes in the liver biopsy. IgA deposits in the liver were found in 78% of the alcoholic patients and in 12% of the nonalcoholic patients. The presence of deposits was not related to histopathological changes in the liver or to the serum IgA concentration. In serum IgA subclass distribution, alcoholic patients differed from nonalcoholic patients by a slight but significant shift to IgA2; in contrast, the hepatic IgA deposits in alcoholic patients were almost of the IgA1 subclass. Serum secretory component (which is an equivalent of serum secretory IgA) was elevated in both alcoholic and nonalcoholic patients; patients with a liver biopsy revealing hepatitis showed the highest level. In contrast, the hepatic deposits did not contain secretory component. We conclude that the continuous deposits of IgA along liver sinusoids are not a passive reflection of changes in concentration or composition of circulating IgA, but may represent a distinct effect of alcohol on the liver related to the role of this organ in IgA metabolism.

Biopsy, Needle↗