Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Secretory Component”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 73 records · Page 4Linked to original sources

Localization of free secretory component in pleomorphic adenomas of minor salivary gland origin.

Secretory component (a glycoprotein) is an antigenically distinct portion of the secretory immunoglobulin A, which has been identified in a number of normal and neoplastic epithelial cells. Localization of secretory component was determined in pleomorphic adenomas of minor salivary gland origin using the four-step peroxidase-antiperoxidase technique. Antiserum that detected only free secretory component (FSC) was used. Staining for secretory component was noted in the epithelium that lined duct-like spaces; but was absent in myoepithelial cells and mucous acini. These findings suggest a role for FSC in evaluating the histogenesis of various salivary gland neoplasms.

Adenoma↗

A comparison of the binding of secretory component to immunoglobulin A (IgA) in human colostral S-IgA1 and S-IgA2.

A detailed investigation of the binding of secretory component to immunoglobulin A (IgA) in human secretory IgA2 (S-IgA2) was made possible by the development of a new method of purifying S-IgA1, S-IgA2 and free secretory component from human colostrum using thiophilic gel chromatography and chromatography on Jacalin-agarose. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis of unreduced pure S-IgA2 revealed that, unlike in S-IgA1, a significant proportion of the secretory component was bound non-covalently in S-IgA2. When S-IgA1 was incubated with a protease purified from Proteus mirabilis the secretory component, but not the alpha-chain, was cleaved. This is in contrast to serum IgA1, in which the alpha-chain was cleaved under the same conditions - direct evidence that secretory component does protect the alpha-chain from proteolytic cleavage in S-IgA. Comparisons between the products of cleavage with P. mirabilis protease of free secretory component and bound secretory component in S-IgA1 and S-IgA2 also indicated that, contrary to the general assumption, the binding of secretory component to IgA is different in S-IgA2 from that in S-IgA1.

Blotting, Western↗

Circulating secretory component in relation to early diagnosis and treatment of liver metastasis from colorectal carcinomas.

AIMS: To evaluate serum secretory component in relation to early detection and clinical management of liver metastasis in patients with colorectal cancer. METHODS: Secretory component and carcinoembryonic antigen (CEA) were analysed in serial serum samples from 23 patients who had liver metastases as the only apparent recurrence, and in sera from 54 matched controls. Results of surgical treatment of recurrences were classified peroperatively as radical when no residual tumour was apparent and resection margins were free of disease. RESULTS: In total, 18 (78%) patients had increased secretory component during the whole follow up period (median 16 months); 12 (52%) had raised secretory component concentrations before clinical recurrence (median lead time 5.2 months). There was no difference before recurrence between circulating secretory component and CEA in sensitivity and lead times. Seventeen patients underwent surgery for hepatic metastasis; seven had radical hepatic resection of which only two (29%) showed increased secretory component concentrations before clinical recurrence; both had concurrent raised CEA values. By contrast, secretory component was raised in 83% of those cases considered inoperable. CONCLUSIONS: Although serum secretory component clearly increases in most patients with liver metastases, its clinical value seems questionable because secretory component apparently indicates mainly inoperable hepatic metastases.

Adult↗

[Receptors for the secretory component on human thymic lymphocytes. Stimulation of their expression as affected by adenosine, theophylline and a thymic lymphocyte supernatant].

It has been established by indirect immunofluorescence that thymic lymphocytes bear receptors for secretory component (Rsc). The bound secretory component, i. e., in the molecule of secretory IgA, was found to react with a greater number of thymocytes than free secretory component. Such difference may indicate that T-Rsc have higher affinity to the bound secretory component than to free secretory component. However, this needs detailed investigation. The ability of thymocytes to express Rsc depends on the cellular cAMP level, as the treatment with adenosine and theophylline increases the number of cells with Rsc. Supernatant of a 3-hour thymocyte culture was also capable of stimulating the expression of Rsc. It is assumed that secretory component contained in great amounts in the thymus membrane system takes part in the differentiation of T alpha and Tsc cells of the thymus, which repopulate lymphoid organs and regulate their immune reactions. Rsc may also be useful in assessing the state of Tsc subpopulation in different pathological conditions.

Adenosine↗

Secretory component: a potential regulator of endometrial-decidual prostaglandin production in early human pregnancy.

OBJECTIVE: We sought to investigate the production of secretory component, an inhibitor of phospholipase A(2), and prostaglandins by human endometrium-decidua. STUDY DESIGN: The production of secretory component and prostaglandins by explants and dispersed glandular and stromal cells of secretory endometrium and first-trimester and term decidua were measured by enzyme-linked immunosorbent assay and radioimmunoassay, respectively. RESULTS: Explants of first-trimester decidua produced significantly more secretory component and less prostaglandins than secretory endometrium. Immunohistochemical studies localized secretory component to epithelial glandular cells. At term, when fewer glandular cells are present, both secretory component and prostaglandin production were low. Exposure of first-trimester decidua to progesterone significantly increased secretory component production. CONCLUSION: Secretory component and prostaglandins localize primarily to epithelial glandular cells in endometrium-decidua, and their production appears to be inversely correlated. The increase in secretory component by first-trimester decidua after progesterone stimulation may account for the down-regulation of endometrial prostaglandin synthesis after implantation, a process thought to be necessary for pregnancy success.

Adolescent↗

Disulfide bonding of secretory component to a single monomer subunit in human secretory IgA.

The arrangement of disulfide bonds joining secretory component (SC) to the alpha chains in secretory IgA was studied by determining the molecular size of the principal fragments resulting from CNBr digestion of secretory dimeric Fc fragments from IgA (Fc)2alpha fragments). In vitro complexes formed by incubating 125I-free SC and myeloma 131I-(Fc)2alpha fragments were isolated by gel filtration and subsequently digested with cyanogen bromide. The CNBr digests of SC-(Fc)2alpha fragments were analyzed by gel filtration in 5 M guanidine. Two principal fragments were obtained, one containing a monomeric Fc fragment from IgA (Fcalpha) associated with SC (m.w. congruent to 110,000) and a second containing the second Fcalpha monomer (m.w. congruent to 50,000) from the dimeric SC-(Fc)2alpha. Similar results were obtained when secretory (Fc)2alpha fragments isolated from native secretory IgA dimer were subjected to CNBr digestion. The data indicate that SC is disulfide bonded to a single monomer subunit in secretory IgA dimer.

Chemical Phenomena↗

Secretory component in pulmonary adenocarcinoma and mesothelioma.

The distribution of secretory component was examined by an immunoperoxidase method in 40 pulmonary adenocarcinomas, 11 malignant pleural mesotheliomas and areas of normal lung adjacent to the tumours. Secretory component was demonstrated in tumour cells in 25 (67%) adenocarcinomas. Its presence correlated with the degree of differentiation but was not related to tumour pattern. In the normal lung secretory component can be demonstrated in bronchial ciliated cells, bronchial gland serous cells, bronchiolar epithelium and hyperplastic alveolar epithelium. Although not usually detectable in normal mucous cells it was frequently present in mucin-producing tumours. None of the mesotheliomas examined contained secretory component and this may be an additional useful feature in the differential diagnosis between mesothelioma and adenocarcinoma.

Adenocarcinoma↗

Distribution of secretory component in hepatocytes and its mode of transfer into bile.

Immunoglobin A in bile and other external secretions is mostly bound to a glycoprotein known as secretory component. This glycoprotein is not synthesized by the same cells as immunoglobulin A and is not found in blood. We now report the mechanism by which secretory component reaches the bile and describe its function in immunoglobulin A transport across the hepatocyte. Fractionation of rat liver homogenates by zonal centrifugation was followed by measurement of the amounts of secretory component in the various fractions by rocket immunoelectrophoresis. Secretory component was found in two fractions. One of these was identified as containing Golgi vesicles from its isopycnic density and appearance in the electron microscope; the other contained principally fragments of the plasma membrane of the sinusoidal face of the hepatocyte, as shown by its particle size and content of marker enzymes. Only the latter fraction bound (125)I-labelled immunoglobulin A added in vitro. At 5min after intravenous injection of [(14)C]fucose, the secretory component in the Golgi fraction was labelled, but not that in the plasma membrane. The secretory component in the sinusoidal plasma membrane did, however, become labelled before the first labelled secretory component appeared in bile, about 30min after injection. We suggest that fucose is added to the newly synthesized secretory component in the Golgi apparatus. The secretory component then passes, with the other newly secreted glycoproteins, to the sinusoidal plasma membrane. There it remains bound but exposed to the blood and able to bind any polymeric immunoglobulin A present in serum. The secretory component then moves across the hepatocyte to the bile-canalicular face in association with the endocytic-shuttle vesicles which carry immunoglobulin A. Hence there is a lag before newly synthesized secretory component appears in bile.

Animals↗

Effect of age, malnutrition and renutrition on free secretory component and IgA in secretions.

The development of free secretory component (FSC) was studied in the tears of normal infants, children and adults. The level of FSC in tears was higher in older adults than in children. Free secretory component was also measured in the tears of normal, moderately and severely malnourished Colombian children. Children suffering from kwashiorkor, combined protein-calorie malnutrition or marasmus were studied before and after renutrition. No change was detected in the concentration of FSC in tears of moderately malnourished (Grade I and II) children. There was a significant difference between normal and severely malnourished children which improved with renutrition. The levels of tear IgA were decreased in the moderately malnourished children. These results indicate that reduction in secretory IgA levels in moderate malnutrition may not be explained by a lack of available free secretory component in tears, but that severe malnutrition may impair the S-IgA system by significantly reducing the availability of free secretory component.

Adolescent↗

Immunohistological localization of IgG1, IgA and secretory component in the bovine mammary gland during involution.

Immunoperoxidase methods were used to localize secretory component, immunoglobulin A and immunoglobulin G1 in mammary tissue from dairy cows. In lactating tissue, immunostaining for immunoglobulin A and secretory component was observed primarily in the luminal contents of alveoli. By day 2 of involution, alveolar epithelial cells stained for both immunoglobulin A and secretory component. Staining of alveolar epithelial cells for immunoglobulin A and secretory component continued throughout the period of mammary involution. No staining for secretory component was observed in the interalveolar stromal area. Immunoglobulin G1 immunostaining was localized primarily in the interalveolar areas in lactating tissue, but was localized at the apical and basolateral surface of alveolar cells on day 2 of involution. In contrast to immunoglobulin A, immunoglobulin G1 staining of epithelial cells did not persist and was primarily in the interalveolar areas by day 4. These results suggest that an increased localization of immunoglobulin G1 in bovine mammary epithelial cells may occur transiently in early involution, while an increase in immunoglobulin A and secretory component localization in epithelial cells persists throughout involution.

Animals↗

Gravidin, an endogenous inhibitor of phospholipase A2 activity, is a secretory component of IgA.

Gravidin, a phospholipase inhibitor characterised previously from amniotic fluid, was partially sequenced at the N-terminal and found to be identical to secretory component of human IgA. Inhibition of antiphospholipase activity was observed after incubation of gravidin with monoclonal antibody to human secretory component. Secretory component isolated from human saliva and breast milk was found to inhibit arachidonic acid release from human lymphocytes. It was concluded that gravidin is secretory component of IgA.

Amino Acid Sequence↗

Glandular distribution of immunoglobulins, J chain, secretory component, and HLA-DR in the human endometrium throughout the menstrual cycle.

Two-colour immunofluorescence was used to study components of the secretory immune system in the endometrium. Tissue sampling was performed in the follicular, ovulatory and luteal menstrual phase from women admitted for laparoscopic sterilization. The specimens were prepared for immunohistochemistry by a method that removes most extracellular immunoglobulin (Ig). The stroma contained only a few Ig-producing immunocytes, but was rich in HLA-DR positive cells. Most of the IgA- and IgM-producing immunocytes also expressed J chain, which is necessary for the generation of polymeric Ig (poly-Ig) with affinity for epithelial secretory component (SC or poly-Ig receptor). Throughout the menstrual cycle there was increasing accumulation of Ig within the endometrial glands, with preferential apical and intraluminal occurrence of IgA and IgM, usually along with J chain and SC. It is likely that some monomeric IgA (without J chain) and IgG enter the endometrial glands by passive diffusion from the stroma, but there is clearly an additional active external poly-Ig transport. Some of the glands stained for HLA-DR irrespective of the menstrual phase or degree of SC expression. Our findings suggest that active SC-mediated external transport of serum-derived (and to some extent locally produced) poly-Ig is enhanced in the luteal phase, and that SC and HLA class II molecules are differently regulated in the endometrial glands.

Adult↗

Distribution of secretory component and immunoglobulins in the developing lung.

The distribution of secretory component and immunoglobulins, IgA, IgG, and IgM in developing human lungs, ranging in age from 12 gestational weeks to 8 yr, was studied using the indirect peroxidase-labeled antibody method. Secretory component appeared first in the serous bronchial epithelium near the duct openings at the sixteenth gestational week, in goblet cells at the twentieth gestational week, and in bronchiolar epithelium at the twenty-second gestational week. The number of secretory component-positive cells (Y) in bronchial epithelium increased with age in weeks (X) according to the formula Y = 15.328 + 0.094 log X (p less than 0.001). Secretory component was almost absent in bronchiolar epithelium in atelectatic lungs with or without hyaline membrane. Secretory component-positive cells were never observed below the levels of respiratory bronchioles. Immunocompetent cells appeared in the bronchial walls after birth in normal lungs, but they appeared at the thirty-ninth gestational week in cases of pulmonary infection. The IgA- and IgM-containing cells were present around the bronchial glands in normal lungs, whereas IgG-containing cells were not associated with the glands. In normal lungs, IgA-containing cells were most prominent, followed by IgM-containing cells and IgG-containing cells. The apical portions of serous epithelial cells of bronchi and bronchial glands were positive for IgA and IgM. In bacterial and viral pulmonary infections, IgA-containing cells increased in number in the bronchial glands. The appearance of secretory component-positive cells long before immunoglobulin-containing cells in fetal lungs suggests that secretory component may play some role in the formation of the mucociliary blanket, instead of selective transport of IgA or IgM.

Bacterial Infections↗

Secretory component production by polarized epithelial cells from the human female reproductive tract.

At mucosal surfaces, the polymeric Ig receptor (pIgR) is responsible for transporting polymeric IgA across epithelial cells. The purpose of this study was to determine whether normal epithelial cells from the female reproductive tract form tight junctions and produce secretory component, the external domain of the pIgR. Uterine, cervical and vaginal tissues from women at different stages of the menstrual cycle and following menopause were used to prepare purified epithelial cell sheets, which were cultured in cell chambers. Transepithelial resistance was measured and the media from apical and basolateral compartments assayed for secretory component. Secretory component produced by uterine epithelial cells accumulated preferentially in apical compartment and correlated with increased transepithelial resistance. Seeding as epithelial sheets at 1 x 10(6) cells/cm2 of matrix coated cell chambers was required for growth. Epithelial cells from endo-cervix and ecto-cervix, but not the vagina, also showed preferential production and release of secretory component into the apical chamber. In conclusion, normal epithelial cells from the human female reproductive tract grow to confluence, become polarized and produce secretory component. Our results suggest that uterine and cervical epithelial cells play a key regulatory role in the control of IgA transcytosis from tissue into secretions.

Cell Polarity↗

Distribution of immunoglobulins and secretory component in gastric cancer of the aged.

The secretory immune system plays an important role in the local humoral immunity of the gastrointestinal tract. In order to evaluate humoral immunity in gastric cancer, distribution of immunoglobulins (Ig) and secretory component was immunohistochemically studied in 74 early and 15 advanced primary gastric cancers. In non-cancerous gastric mucosa, IgA and IgM, and secretory component were mainly identified in the cytoplasm of the intestinal metaplasia. In early gastric cancer of well-differentiated type, the localization of IgA and IgM, and secretory component was similar to that of intestinal metaplasia. In advanced gastric cancer, they were faintly observed and showed low positivity. The number of Ig-containing cells infiltrating cancerous stroma was enumerated. Immunoglobulin A-containing cells were dominant in the stroma of early gastric cancer. On the other hand, there were few Ig-containing cells in the stroma of advanced gastric cancer, and the number of IgA-containing and IgM-containing cells was also decreased. These results suggest that local humoral immunity is suppressed in gastric cancer, especially in advanced gastric cancer.

Aged↗

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↗

IgG antibodies to secretory component in normal human serum.

While isolating free secretory component (FSC) by monoclonal antibody affinity chromatography, we demonstrated FSC-IgG complexes in human milk. We hypothesized that IgG antibody to secretory component (SC) might be transported into the milk from the serum. We therefore examined sera from 10 normal adults and 10 infants for IgG capable of binding to FSC in an enzyme-linked immunosorbent assay. Eight of 10 normal adult sera and nine of 10 infant sera demonstrated IgG binding to FSC with titers ranging from 1:54 to 1:4096. Quantitation of the IgG bound to FSC was hampered in adult sera by the binding of IgM and polymeric IgA to the FSC. Quantitation in five infant sera ranged from 0.5 to 6.4 micrograms/ml. A pepsin digest of an IgG fraction of serum demonstrated binding of the F(ab')2 fragments to the FSC. The specificity of the antibodies in human serum was evaluated by examining the binding to secretory IgA (sIgA) and FSC isolated from pooled human milk and polymeric IgA isolated from the ascitic fluid of a patient with an IgA myeloma. Eight of the 10 adults had antibody specific for FSC. Three of the eight, all female, also had antibody specific for sIgA. Two of the eight had antibody either to FSC and sIgA or to FSC plus an antibody that could bind to an epitope shared by sIgA and FSC. Competition experiments with monoclonal antibodies to human secretory component and sIgA were used to confirm and further define these specificities. The results of this study indicate that antibody to SC is common in normal adult and infant sera. The majority of antibodies seem to be directed against epitopes present on FSC but not on sIgA, which suggests sensitization to circulating or membrane-bound SC. The significance of these antibodies in normal human sera remains to be elucidated.

Adult↗

Serum secretory IgA and secretory component in patients with non-cirrhotic alcoholic liver diseases.

Elevated levels of secretory IgA in serum have been demonstrated in several liver dysfunctions such as hepatic cytolysis and cholestasis. However, these possible alterations at an early stage of liver diseases have not yet been investigated. We studied a cohort of chronic alcoholic patients without cirrhosis in order to assess the changes in serum secretory IgA and other forms of secretory component, the split product of the polymeric Ig-receptor of epithelial cells. The possible diagnostic value of these measurements in the assessment of alcoholic disease was compared to that of serum gamma-glutamyl transpeptidase activity. Serum levels of secretory IgA and IgM and free secretory component, were quantified by an enzyme-linked immunosorbent assay in 71 patients with chronic alcoholic liver disease without cirrhosis and in 45 healthy controls. Patients were divided into two groups according to the severity of the liver abnormalities. In addition, the reversibility of serum secretory IgA, IgM and free secretory component abnormalities after alcohol withdrawal was evaluated in 15 patients. Serum levels of the three molecular forms of secretory component were significantly higher than those measured in control subjects, both in the whole population of patients and in the two groups of alcoholic patients without cirrhosis. In all groups, serum secretory IgA levels were correlated to free secretory component but not to total IgA levels. Serum secretory IgA levels were as discriminative as gammaglutamyl transferase activity in distinguishing between chronic alcoholic patients without cirrhosis and non-alcoholic subjects. The abnormalities of serum secretory IgA concentrations were reversible after alcohol withdrawal.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗