Cerebrospinal fluid lactoferrin in bacterial and viral meningitis.
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Humans↗
Biomedical subjects
P Tuohimaa
Publications and source records attributed to P Tuohimaa.
Immunocytochemical localization of progesterone receptor in the chick ovary.
The distribution of progesterone receptor (PR) in the chick ovary was studied using light- and electron-microscopic immunocytochemical methods. With the light microscopic technique, PR was observed in the germinal epithelium cells of estrogen-treated and estrogen-untreated immature chicks. With the preembedding immunocytochemical technique, which proved to be more sensitive than immunohistochemistry using paraffin sections, the germinal epithelium and also part of the thecal and stromal cells were stained when immature chicks were not treated with estrogen. After estrogen treatment, the number of PR-positive stromal and thecal cells increased, as did the immunostaining intensity in their nuclei. The granulosa cells were PR-positive only after estrogen treatment. In the ovary of laying hens, the most intense staining for PR was localized in the germinal epithelium. PR was also present in the thecal, stromal, and granulosa cells. At the subcellular level, PR was detected only in the cell nuclei, indicating that ovarian PR is intranuclear independent of the presence of progesterone. In conclusion, immunocytochemical methods proved to be suitable for studying steroid hormone receptors in steroid-producing tissues (e.g. the ovary), because excess endogenous hormones do not affect detection of the receptor with the antibody as they do detection with labeled ligands. Immunocytochemically, the germinal epithelium, stromal, thecal, and granulosa cells of the laying hen ovary were shown to be target cells for progesterone. The inducibility of PR by estrogen in the thecal, stromal, and granulosa cells suggests that these cell types are also sensitive to estrogen.
Animals↗
Ontogeny of oestrogen-sensitive mesenchymal cells in the bursa of Fabricius of the chick embryo. An immunohistochemical study on progesterone receptor.
The expression of progesterone receptor (PR) and its induction by oestradiol during the embryogenesis of the chick bursa of Fabricius (BF) were studied by immunohistochemistry using three different polyclonal antibodies to the chicken oviduct PR. Mesenchymal cells of the cloacal area surrounding the bursa primordium in controls (without exogenous oestrogen) express the PR between 9 and 11 days of incubation. In the same cells, PR was induced experimentally by oestradiol at 9 days. Mesenchymal cells in the bursa did not express PR after oestradiol treatment before the age of 11 days. The PR was not inducible in the bursal epithelium or in haemopoietic cells. None of the bursal cells expressed the PR to a detectable level during embryonic life without exogenous treatment. Some haemopoietic cells showed strong artefactual staining in their nuclei. It is concluded that (1) the embryonic bursa of Fabricius is a sex-steroid-sensitive organ, (2) exogenous oestradiol is able to induce progesterone receptor in the mesenchymal cells, but (3) the PR is not expressed without exogenous oestrogen. This indicates that the PR becomes oestrogen inducible well before it is naturally expressed during sexual maturation and that the level of endogenous oestrogen during embryonic life is not high enough to affect the bursa significantly.
Animals↗
[Pediatric sleep apnea syndrome].
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Airway Obstruction↗
Nuclear origin of progesterone receptor of the chick oviduct cytosol. An immunoelectron microscopic study.
Progesterone receptor (PR) was studied immunoelectron microscopically from fixed vibratome sections of the chick oviduct and biochemically from the fractionated oviduct homogenate. Immunoelectron microscopically both unoccupied and occupied PR were localized inside the nuclei. Only a few cells showed PR immunoreactivity in the endoplasmic reticulum which probably represents newly synthetized PR. Biochemically unoccupied PR was in the cytosol fraction. The cytosol and nuclear PR as well as the non-transformed 8S-form and the transformed 4S-forms of cytosol PR were recognized by the anti-PR antibody (IgG-RB). The lack of PR immunostaining in the cytoplasm is therefore not due to lack of recognition by IgG-RB. We propose that in the chick oviduct progesterone receptor is a nuclear protein but synthetized in the endoplasmic reticulum.
Animals↗
Antimicrobial factors in whole saliva of human infants.
Antimicrobial factors were analyzed in samples of whole saliva from 31 children, aged 0.8 to 3.8 years. When compared with the adult reference group, the children displayed similar levels of lysozyme, salivary peroxidase, and hypothiocyanite (OSCN-), whereas the amounts of immunoglobulins (isotypes A, G, and M), lactoferrin, myeloperoxidase, thiocyanate (SCN-), amylase, and protein were significantly lower than the adult values. The child's behavior during the collection period noticeably influenced the composition of the saliva. Children who were restless and crying during the collection had significantly more immunoglobulins, lysozyme, lactoferrin, salivary peroxidase, myeloperoxidase, and protein in their saliva samples, obviously due to the contamination of saliva mixed with nasal or lacrimal secretions. Therefore, the normal values for saliva could be determined for the noncrying children only. These salivary defense systems did not show any relation to the length of breast-feeding or to the previous history of antibiotic treatment. Thus, with the exception of lactoferrin and myeloperoxidase, the nonimmunoglobulin antimicrobial saliva systems studied here seem to be already at the adult level during early childhood, when the protective antibody systems are still immature.
Adult↗
Immunoglobulins and innate antimicrobial factors in whole saliva of patients with insulin-dependent diabetes mellitus.
We analyzed the flow rate and composition of paraffin-stimulated whole saliva samples from 35 adult diabetic patients and their age- and sex-matched, non-diabetic, clinically healthy controls. All patients had insulin-dependent diabetes (IDDM) with a mean (+/- S.D.) duration of 14.0 +/- 9.1 years. The saliva analysis included the quantitation of total protein, amylase, immunoglobulins (isotypes A, G, and M), and the non-antibody, innate antimicrobial factors (lysozyme, lactoferrin, salivary peroxidase, myeloperoxidase, thiocyanate, and hypothiocyanite). The whole saliva samples from diabetic patients had significantly higher amounts of IgA (p less than 0.001) and IgG (p less than 0.05) than did the controls. No differences between the study groups were observed in flow rate, protein content, amylase activity, or IgM. The levels of innate defense factors were similar in both study groups except for salivary peroxidase, which was higher (p less than 0.02) among diabetics than among controls. Our results indicate that the antimicrobial defense capacity of whole saliva is not impaired in diabetic patients.
Adolescent↗
Steroid hormone receptors in laryngeal carcinoma.
The larynx has long been shown to be a target organ for androgenic steroids in both women and men, and specific androgen receptors have been determined in normal laryngeal mucosa and in laryngeal carcinoma tissue. In this study, samples from 21 primary laryngeal carcinomas, from 4 recurrent laryngeal carcinomas and from 1 cervical metastasis of laryngeal carcinoma were obtained at the time of surgery to assay specific androgen, estrogen, and progesterone receptors. Specific androgen receptors were found in 8 samples (31%). The level of receptors varied from 1.7 femtomoles (fmol) per milligram to 7.3 fmol/mg cytosol protein. Detectable levels of specific estrogen receptors were found in 18 samples (69%) and progesterone receptors in 8 of the 15 samples studied (53%). There was no apparent correspondence with donors' sex, since samples from both females and males contained all kinds of receptors. We know that antiestrogen inhibits the growth of squamous carcinoma cells lines positive for estrogen receptors in vitro and that this effect is reversible with the appropriate hormone. Thus, the relatively high percentage of estrogen and progesterone receptors found in laryngeal carcinoma tissue may open new aspects in the treatment of laryngeal carcinoma with antihormones.
Aged↗
A rapid and sensitive non-competitive avidin-biotin assay for lactoferrin.
We have developed an avidin-biotin assay for the detection of lactoferrin in human seminal plasma. We compared 5 modifications of this assay, and found the non-competitive avidin-biotin assay (NABA) to be the most sensitive. The detection limit of 3-step NABA was 0.2 or 0.1 ng lactoferrin/ml, depending whether avidin-biotin-peroxidase complex (ABC) or avidin-peroxidase was used. The intra-assay and inter-assay coefficients of variation for 3-step NABA were 6.2 and 8.5%, respectively. The lactoferrin levels of human seminal plasma samples measured by 3-step NABA and radioimmunoassay (RIA) showed good correlation (r = 0.96). The total performance time of 3-step NABA is flexible and the method can be modified for rapid (less than 1 h) or overnight assay according to need.
Avidin↗
Production of monoclonal antibodies against avidin.
Monoclonal antibodies of the IgG1 subclass were generated against chicken avidin. These antibodies were shown to be as sensitive as polyclonal antiserum in detecting avidin by radioimmunoassay (RIA) and enzyme linked immunosorbent assay (ELISA) methods. Furthermore, the monoclonal antibodies were considerably more specific. Our results with a monoclonal anti-avidin RIA support previous findings that in inflammatory conditions avidin is synthesized also in other organs than the oviduct, although in the liver a major part of the activity detected by polyclonal anti-avidin RIA or biotin-bentonite assay was not due to avidin.
Animals↗
Pneumococcal immune complexes and clinical course of secretory otitis media.
One-hundred-and-six children (182 ears) with secretory otitis media (SOM) were included in a follow-up study to determine whether presence of immune complexes to pneumococcal capsular polysaccharides in the middle ear fluid or adenoid suspension was related to the clinical course of SOM. The patients with immune complexes did not differ significantly from those without demonstrable immune complexes as to length of healing period or chronicity. The presence of immune complexes must be seen as evidence of the infectious etiology of SOM (pneumococcal in at least 25%), the immune complexes forming part of the immunological defense system. Poor immune response to serotype 6 can explain why this serotype plays a dominant role in the pneumococcal immune complexes in SOM fluid and adenoid suspension.
Adenoids↗
Peroral prednisolone in the treatment of middle-ear effusion in children: a double-blind study.
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Administration, Oral↗
Progesterone receptor in the chick bursa of fabricius: characterization and immunohistochemical localization.
A high affinity progesterone-binding site was studied in the chick bursa of Fabricius. The dissociation constant for progesterone was 1.4 nM, and the concentration of progesterone-binding sites increased with estradiol treatment. In estradiol-treated bursas, the receptor concentration was about 240 fmol/mg protein. The binding site was specific for progestins, with the following order of affinities: ORG 2058 greater than progesterone greater than promegestone. Androgens, dexamethasone, and estradiol were weak competitors for progesterone binding in the bursa cytosols from estradiol-treated chicks. Immunoglobulin G fraction of antiserum (immunoglobulin G-RB) raised in rabbit against the B-subunit of chick oviduct progesterone receptor (PR) was used for an immunohistochemical study. The PR was found only in the interfollicular cells, which were most probably nonlymphoid cells. Staining was localized exclusively in the elongated nuclei of these cells. No staining was seen in the bursal epithelium or inside the lymphoid follicles. The results indicate that the interfollicular cells of the bursa contain specific PRs which are under estrogen regulation as in the oviduct. Thus, these cells might be under direct progesterone regulation.
Animals↗
Antibodies against highly purified B-subunit of the chick oviduct progesterone receptor.
A rabbit was immunized with the highly purified B-subunit (110kDa) (20 to 50 micrograms per injection) of the chick oviduct progesterone receptor (PR). Specific antibodies (IgG-RB) were observed 2 weeks after the first booster injection and high antibody titers in the serum were found after the second and third booster injections (with Kdeq of interaction integral of 2 nM). IgG-RB were tested by immunoprecipitation, immunoblotting, density gradient ultracentrifugation and protein A-sepharose assay methods. They recognized not only the B-subunit but also the A-subunit (79K), the nuclear PR, the mero-receptor (proteolytic cleavage product) and the "non-activated" molybdate-stabilized "8S" PR. However, IgG-RB did not interact with the 90K non hormone-binding component of this 8S-PR. IgG-RB did not affect the binding of the hormone to PR, whether incubated with the receptor before or after labelling with tritiated progesterone. They did not cross-react with glucocorticosteroid receptor of the chick oviduct. Weak interaction was observed with estrogen receptor of the chick oviduct and with KC1 activated "4S" forms of the rabbit and human uterus PR.
Animals↗
Purification by affinity chromatography and immunological characterization of a 110kDa component of the chick oviduct progesterone receptor.
A 110kDa component of the chick oviduct progesterone receptor (PR) has been purified to homogeneity according to electrophoretic criteria and specific activity (assuming one progestagen-binding site/110kDa). The procedure involved affinity chromatography of 0.3 M-KCl-prepared cytosol, followed by DEAE-Sephacel chromatography (elution at 0.2 M-KCl). The final yield was about 12% in terms of binding activity. Properties of the 110kDa component indicate that it is identical with the 'B' subunit described previously [Stokes radius approximately 6.1 nm; sedimentation coefficient, (S20, w) approximately 4S; frictional ratio approximately 1.77]. It reacted with the IgG-G3 polyclonal antibody, but not with BF4 monoclonal antibody raised against the 8S molybdate-stabilized chick oviduct PR and reacting with its 90kDa component. Another progesterone-binding component, corresponding to the 'A' subunit, also previously described, was eluted from the DEAE-Sephacel column at approximately 0.08 M-KCl, and contained a peptide of molecular mass approx. 75-80kDa, which had S20, w approximately 4S in a sucrose gradient. This component was also recognized by IgG-G3, but not by BF4; it was very unstable in terms of hormone-binding activity.
Animals↗
Effects of calcium on the chick oviduct progesterone receptor.
The chick oviduct cytosol progesterone receptor can be transformed to a small form (Rs = 21A, S20,w:2.9) denoted "mero-receptor" by incubation in the presence of Ca2+ [8]. In the molybdate-free cytosol all the progestin binding components could be completely transformed to mero-form by 1 h treatment with 100 mM Ca2+ at 0 degrees C. If EDTA was secondarily added, the ligand was rapidly released. If molybdate (20 mM) containing cytosol was incubated with Ca2+, no radioactivity was found in the meroposition on the Agarose A 0.5 m column, but the bound steroid sedimented at 2.9 S in sucrose gradients containing Ca2+ (and no molybdate). When 20 nM molybdate was added to cytosol containing receptor activated by 0.3 M KCl, complete mero-transformation by Ca2+ was obtained also by the gel filtration criterion, indicating that molybdate does not inhibit the mero-transforming factor. Ligand-free progesterone receptor could also be completely converted to mero-form by endogenous cytosolic transforming factor and calcium. The transforming factor was completely inactivated, when cytosol was run through Agarose A 0.5 m gel. Mero-transformation was found to be irreversible. The purified progesterone receptor subunit 110 K (B) was partially converted to smaller forms by calcium alone (100 mM, 0 degrees C, 1 h) whereas addition of a small amount of cytosol allowed complete conversion to mero-form.
Animals↗
Augmentation of progesterone receptor concentration by progesterone and estrogen treatments in the chick oviduct.
Cytosol receptors for progesterone in the chick oviduct were measured by charcoal-adsorption assay by using ORG 2058 as a ligand after long-term administration of progesterone and diethylstilbestrol (DES). Steroid administration was carried out by using daily injections or silastic capsules. DES treatment increased the progesterone receptor concentration (from 11500 to 21500 sites per cell, day 14). Progesterone also augmented the concentration of its own receptors (from 11500 to 29000 sites per cell, day 14). In the experiments with capsule administration the same trend was seen. This indicates that both diethylstilbestrol and progesterone are able to increase the concentration of progesterone specific cytosol receptors in the non-differentiated chick oviduct.
Animals↗
Progesterone receptor in the chick oviduct: an immunohistochemical study with antibodies to distinct receptor components.
We performed immunohistochemical studies of chicken oviduct after different fixation procedures, by using antibodies against the progesterone receptor: polyclonal antibodies IgG-G3 against the "8S" form (an oligomere containing progesterone-binding and nonprogesterone-binding units), polyclonal antibodies IgG-RB against the progesterone-binding B subunit, and monoclonal BF4 against the non-progesterone-binding 90,000-mol-wt protein component. Chickens were immature animals with or without estrogen priming, and with or without progesterone treatment. The antibodies were revealed by means of an immunoperoxidase technique that used the avidin-biotin-peroxidase complex, and controls were performed by presaturation of antibodies with the purified 8S-progesterone receptor, the B subunit, and 90,000-mol-wt protein. The progesterone receptor was detected not only in well-characterized target tissues, i.e., in glands and luminal epithelium, but also in stromal cells (some displayed the strongest reaction), in mesothelium, and in fibers of smooth muscles. Only in cell nuclei, whether or not the animals received an injection of progesterone was an antigen revealed corresponding to the B subunit (and/or to the A subunit, because there is immunoreactivity of IgG-RB with both hormone-binding subunits A and B). The 90,000-mol-wt protein was revealed in both cytoplasm and nuclei. These immunohistological data suggest that the concept of steroid action that necessarily involves the original formation of the hormone-receptor complexes in the cytoplasm before translocation to the nucleus, may have to be revised.
Animals↗