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Biomedical subjects

Y C Tseng

Publications and source records attributed to Y C Tseng.

At least 19 recordsLinked to original sources
PubMed1992

Synthesis of photoreactive poly(ethylene glycol) and its application to the prevention of surface-induced platelet activation.

Photoreactive poly(ethylene glycol) (PEG) was synthesized by reacting 4-fluoro-3-nitrophenyl azide (FNPA) with sodium salt of PEG. The synthesized 4-azido-2-nitrophenyl PEG (ANP-PEG) was characterized by 1H-NMR, IR, and UV spectroscopy. ANP-PEG was grafted to dimethyldichlorosilane-coated glass (DDS-glass) by photolysis without any premodification of the surface. The effects of various grafting factors, such as the polymer adsorption time, concentration of ANP-PEG, and UV irradiation time, on the PEG grafting efficiency were examined. The PEG-grafted DDS-glass was characterized by measuring surface free energies, surface-induced platelet activation, and the relative amount of PEG grafted on the surface using electron spectroscopy for chemical analysis (ESCA). Platelet adhesion and activation was analyzed by measuring the number and spread area of adherent platelets. The results showed that ANP-PEG had to be adsorbed onto DDS-glass for at least 12 h before photolysis for the maximum grafting efficiency. No platelets could adhere to the PEG-grafted DDS-glass, if the bulk concentration of ANP-PEG in the adsorption solution was between 1 mg/mL and 10 mg/mL. Above 10 mg/mL, platelet activation gradually increased and reached the maximum at 30 mg/mL. Our data indicate that the grafting of ANP-PEG requires careful control of the grafting conditions and that the grafted PEG can prevent surface-induced platelet activation.

Biocompatible Materials↗
PubMed1992

Thyrotropin modulation of epidermal growth factor (EGF) binding to receptors on cultured thyroid cells.

Previous studies had shown that epidermal growth factor (EGF) will stimulate growth of cultured thyroid cells in vitro, and TSH will stimulate total assayable EGF receptor in cultured porcine thyroid cells. In this study, we report the effect of TSH on EGF binding to human thyroid cells. Addition of bTSH (1 mU/mL) in binding buffer during receptor assay stimulated specific EGF binding to cells, with an increase of 44% observed over the control after 1 h incubation at 37 degrees C. Affinity crosslinking of the [125I]EGF-receptor complex showed a single labeled band with molecular size of 170 kD. No additional band was detected in the presence of TSH. Preincubation of cells with chloroquine, which inhibits lysosomal degradative enzyme activity, caused a continuous accumulation of bound EGF over a 4 h study period at 37 degrees C, and TSH stimulated an increase in internalized EGF. In the presence of chloroquine, total specific bound EGF was linearly correlated to incubation time up to 4 h and can be expressed as Bound = slope*time+intercept (time0) Addition of TSH during the binding assay significantly increased the value of the slope when compared to control (p < 0.002). The rate at which prebound [125I]EGF was released into medium was not affected by the presence of TSH, indicating that TSH-enhanced binding may not be attributed to a reduction in EGF degradation. Coincubation of thyroid cells with EGF at 0 and 1 ng/mL and increasing concentrations of TSH (0-10 mU/mL) indicated that EGF stimulated thymidine incorporation, although TSH failed to synergistically enhance EGF-stimulated cell growth.(ABSTRACT TRUNCATED AT 250 WORDS)

Cell Membrane↗
PubMed1992

Receptors for endothelin in cultured human thyroid cells and inhibition by endothelin of thyroglobulin secretion.

Specific receptors for endothelin-1 (ET), a newly described vasoconstrictor peptide isolated from endothelium, have been identified in endocrine tissues such as hypothalamus, adrenal and pituitary. ET binding or action, not previously described in thyroid, were explored in this study. ET binding in cultured human thyrocytes was assayed at 4 C, 25 C, and 37 C, for 0.5-6 h with [125I]ET (0.1 nmol/L), and nonspecific binding estimated by coincubation with unlabeled ET (100 nmol/L). At 4 C, maximum specific binding was reached after 4 h; at 25 C and 37 C, specific binding increased in a time-dependent manner over 6 h with increased binding obtained at higher temperature. At 37 C after 2 h, 11% specific bound ET localized to surface membranes with 89% internalized. Scatchard analysis of surface membrane binding at 4 C for 4 h showed high affinity single class ET receptor (Kd = 0.20 nmol/L) and binding capacity of 4045 sites per cell. ET binding to thyroid cells had no effect on production of cAMP or cGMP. ET (0.1 nmol/L) significantly (P less than 0.001) inhibited thyroglobulin release from thyroid cells after 6 days with no effect on thymidine incorporation. Thus, we have identified specific receptors for endothelin in human thyrocytes, and an inhibitory action of the peptide on thyroglobulin release which is mediated by a noncyclic nucleotide mechanism.

Cells, Cultured↗
PubMed1992

Atrial natriuretic peptide receptors in human endometrial stromal cells.

Atrial natriuretic peptide (ANP) has been shown to affect water and ion transport and specific ANP binding has been identified in several secretory tissues. ANP commonly acts via stimulation of membrane-bound particulate guanylate cyclase with the production of cyclic guanosine monophosphate (cGMP). We questioned whether ANP played a role in the complex cyclic transformation of the endometrium into a secretory tissue, and whether its action was cGMP mediated. Endometrium was obtained by biopsy in regularly menstruating women and stromal cells were isolated and cultured for use in this study. ANP competitive binding assays were performed using 125I-labeled ANP (0.1 nmol/L) and increasing concentrations of unlabeled ANP (0-1000 nmol/L). Optimal binding was obtained after 3-h incubation at 4 C and binding characteristics, including dissociation constant and binding site quantity, were estimated by Scatchard analysis. Specific, high affinity (dissociation constant, 0.078 +/- 0.004 nmol/L) and low capacity (4,877 +/- 1,951 binding sites/cell) ANP binding was identified, with nonspecific binding representing less than or equal to 16% of total binding. Evaluation of ANP-stimulated cyclic nucleotide production revealed an increase in cGMP production, with a 7-fold increase at 1000 nmol/L ANP, and no effect on cAMP production. In conclusion, we have identified specific high affinity receptors for ANP in human endometrial cells, suggesting a role for ANP in endometrial cell function and/or development mediated via cGMP production. We propose that ANP may affect local salt and water metabolism, may be involved in the secretory evolution of glandular and stromal cells, and may further facilitate endometrial development via modulation of local vascular tone and endothelial permeability.

Atrial Natriuretic Factor↗
PubMed1991

Inhibition of TSH activation of human cultured thyroid cells by tumor necrosis factor: an explanation for decreased thyroid function in systemic illness?

Thyroidal economy in systemic nonthyroidal illness (the sick euthyroid syndrome) is marked by reductions in both thyroid function and peripheral T4 to T3 conversion, presumed to reflect a homeostatic mechanism to conserve energy. TSH levels tend to be normal in these patients, and the mechanism underlying reduced thyroidal secretion is unknown. Since increased blood levels of tumor necrosis factor (TNF) are found in many of the conditions associated with the sick euthyroid syndrome, we hypothesized that TNF might affect the function of the thyroid gland. We, therefore, explored the effects of TNF on TSH stimulation of the thyroid, employing a human thyrocyte cell culture model. Cells were incubated with various concentrations (0-1000 pg/mL) of recombinant human TNF-alpha and bTSH (1 mU/mL), with measurement of secreted thyroglobulin (Tg) and cyclic AMP (cAMP) as the end points of stimulation. TNF had no effect on either basal or TSH-stimulated cAMP generation, but significantly blunted TSH-stimulated Tg secretion. No loss of cell viability and growth was observed based on trypan blue exclusion and thymidine incorporation by cells. These studies demonstrated an inhibitory effect on TNF on human thyrocytes in concentrations comparable to blood levels seen in humans during systemic illness. We conclude that increases in serum TNF may be responsible for reduced thyroid function in patients with the sick euthyroid syndrome.

Cyclic AMP↗
PubMed1990

Modified ethoxyethyl cyanoacrylate for therapeutic embolization of arteriovenous malformation.

Aiming at alleviating the problems of using 2-cyanoacrylates as a material for therapeutic embolization, this experiment made some physical modifications by mixing contrast media. It was found that the physicochemical properties of 2-cyanoacrylates can be altered by changing the concentration and the composition of the contrast media added. A 50 wt% cyanoacrylate-50 wt% contrast medium mixture has enough radiopacity for the practical requirement for embolization. A mixture of 50 wt% (ethoxyethyl cyanoacrylate-5 wt% lactide/epsilon-caprolactone copolymer), 25 wt% lipiodol and 25 wt% tetrafluorodibromoethane provides a viscosity of 13.8 cP, a bonding strength of 14.9 kg/cm2, a set time of 6 s, and a spreading in canine blood of 33 mm. It was concluded that the mixture is much more satisfactory than the conventional cyanoacrylates as an embolus material in vitro. The results obtained by in vivo experiments and clinical trials so far suggest that the mixture is very promising as a material for embolization.

Animals↗
PubMed1990

In vitro toxicity test of 2-cyanoacrylate polymers by cell culture method.

The inhibition of Swiss 3T3 cell growth by the microspheres prepared from various 2-cyanoacrylate polymers was investigated to assess their cell toxicity. Poly(ethoxy-ethyl 2-cyanoacrylate) and poly(methyl 2-cyanoacrylate) microspheres inhibited cell growth in a smaller amount than poly-(isobutyl 2-cyanoacrylate) and poly (ethyl 2-cyanoacrylate) microspheres. The extent of cell growth inhibition by the microspheres decreased with the increasing molecular weight, regardless of the kind of polymers used. Every kind of the microspheres was degraded releasing formaldehyde in the culture medium. The cell growth inhibition by the medium containing the microspheres was observed within 24 h for poly(ethoxyethyl 2-cyanoacrylate) and poly(methyl 2-cyanoacrylate). The extent of inhibition was in a linear proportion with the amount of formaldehyde released. It is concluded that the cell toxicity of 2-cyanoacrylate polymers is attributed to formaldehyde released upon polymer degradation.

Animals↗
PubMed1990

Characterization by affinity cross-linking of a receptor for atrial natriuretic peptide in cultured human thyroid cells associated with reductions in both adenosine 3',5'-monophosphate production and thyroglobulin secretion.

We have previously identified specific atriopeptin (ANP) receptors in cultured human thyroid cells and demonstrated that ANP reduced thyroglobulin (Tg) secretion. In this report the relationship of Tg inhibition to cyclic nucleotide intermediate pathways was explored, and the thyroidal ANP receptor was characterized by affinity cross-linking. Concentrations of Tg, cGMP, and cAMP were measured in medium from thyroid cells cocultured with ANP. ANP significantly inhibited cAMP production at the lower concentration of 0.1 nmol/L and stimulated cGMP levels at a higher concentration of 10 nmol/L. The percentage of inhibition of Tg release over the ANP range of 0.01-10 nmol/L appeared to parallel cAMP, but not cGMP, levels, suggesting that ANP acts via a cAMP pathway in the thyroid. Affinity cross-linking studies characterizing the ANP receptor in thyrocytes and a bovine endothelial cell line known to be cGMP responsive to ANP indicated a single unit ANP receptor of 140 kD coupled to guanylate cyclase in endothelial cells, while a 70-kD receptor was found in thyroid cells which specifically binds to ANP, atriopeptin-I, and atriopeptin-III. These studies in thyrocytes suggest that reduced Tg release may be mediated by a specific single 70-kD ANP receptor associated with an inhibitor cAMP pathway and provide additional insight into the nature of a newly described thyroid-ANP interaction.

Atrial Natriuretic Factor↗
PubMed1990

Modification of synthesis and investigation of properties for 2-cyanoacrylates.

The conventional method for synthesis of 2-cyanoacrylate monomers was modified and the adhesive properties were studied for the cyanoacrylate monomers and the resultant polymers. Toluene was found to be better as reaction solvent than methyl alcohol or xylene. The higher the molecular weight of the condensation oligomer before pyrolysis and the narrower the molecular weight distribution, the higher the yield of cyanoacrylate monomer. Ethoxyethyl cyanoacrylate with an ether side chain was shown to be a soft and biodegradable adhesive. The softening and glass transition temperatures of ethoxyethyl cyanoacrylate polymer were much lower than those of cyanoacrylate polymers with methyl, ethyl or isobutyl side chains. Hydrolysis of poly(ethoxyethyl cyanoacrylate), evaluated from formaldehyde generation and mass loss, was faster than that of ethyl cyanoacrylate and isobutyl cyanoacrylate polymer. Hydrolysis of the ethoxyethyl cyanoacrylate polymers was greatly affected by the molecular weight of the polymers. The morphological change of the cyanoacrylate polymer films was studied by scanning electron microscopy.

Adhesiveness↗
PubMed1989

Receptors for atrial natriuretic peptide (ANP) and regulation of thyroglobulin secretion by ANP in human thyroid cells.

Specific binding sites for atrial natriuretic peptide (ANP) were identified and characterized in primary cultures of human thyroid cells. Saturation analysis using [125I] alpha rat ANP as the ligand showed a single class of high affinity binding (Kd = 0.2 nM) which was inhibited by atriopeptin I and the alpha -human form of ANP, but not by a C-terminal fragment of the peptide. The number of ANP binding sites in these cultures was not altered by the thyroid hormone concentration of the medium. In a dose-response experiment, thyro-globulin secretion was significantly reduced in the presence of 0.01 nM ANP and was maximally reduced (to 25% of control value) with 10 nM ANP. Cyclic GMP production was increased threefold in the presence of 100 nM ANP, but was unchanged with lower doses (0.01 and 0.1 nM) of the peptide. The finding of receptors in thyroid follicular cells suggests a hitherto unrecognized role of ANP in the thyroid gland.

Atrial Natriuretic Factor↗
PubMed1989

Thyrotropin modulates receptors for atrial natriuretic peptide on intact human thyroid cells.

Interest in the mechanism of impaired salt and water metabolism in hypothyroidism has led to growing evidence of an interaction between atrial natriuretic peptide (ANP) and the thyroid, which includes reports of direct effects of thyroid hormone on ANP synthesis and circulating ANP levels, and of the presence of specific ANP receptors in human thyroid tissue, which may act to inhibit thyroglobulin (Tg) secretion. The authors questioned whether or not thyrotropin (TSH) has a role in this interaction. They used 125I-ANP to study the effect of TSH on ANP binding to human thyroid cells in primary culture. Binding competition by increasing concentrations of unlabeled ANP in the presence or absence of TSH was assessed by Scatchard analysis. At lower temperatures of 4 degrees C or 23 degrees C, TSH had no effect either on the ANP receptor equilibrium dissociation constant (Kd) or number of binding sites. However, at 37 degrees C, bovine TSH at 1 mU/ml reduced measurable binding sites by about 50% without affecting receptor affinity (Kd = 0.2 nM). Prolonged (6 days) coincubation of TSH with thyroid cells decreased the assayable ANP receptor. The effects of TSH appear to be specific because human luteinizing hormone, follicle-stimulatory hormone, growth hormone, human chorionic gonadotropin and iodide had no effect on ANP binding. Thus, human thyroid cells possess a single class of high-affinity, specific receptors for ANP with binding activity that is temperature dependent and modulated by TSH at physiologic temperature. TSH-mediated reduction of binding at 37 degrees C but not at 4 degrees C suggests an energy-dependent process that acts possibly by activating an ANP degradative enzyme or by changing the rate of receptor internalization and subsequent degradation.

Atrial Natriuretic Factor↗
PubMed1989

Effects of epidermal growth factor on thyroglobulin and adenosine 3',5'-monophosphate production by cultured human thyrocytes.

While several workers have identified epidermal growth factor (EGF) receptors on human thyroid membranes, very few reports have described EGF effects on intact human thyroid cells in primary culture, and these were short term studies indicating that EGF effects were primarily inhibitory [reduced iodide uptake and thyroglobulin (Tg), T4, and T3 release]. Paradoxically, in vivo EGF stimulates thyroid growth and increases colloid stores. In this study we examined the effects of EGF on cultured thyroid cells in regard to thymidine incorporation, Tg secretion, and cAMP production during a 12-day period. Addition of EGF (0-30 ng/mL) to medium for 6 or 12 days stimulated thymidine incorporation and enhanced Tg synthesis by thyroid cells. However, the profile of Tg release into medium was biphasic. Tg release was inhibited by EGF (0.1-10 ng/mL) during the first 3 days of culture, but the inhibitory effect disappeared by the sixth day, and EGF stimulated Tg release by day 12 and thereafter. EGF enhanced endogenous cAMP levels in thyroid cells, but did not augment TSH-stimulated increases in cAMP production. Our observations of EGF-stimulated growth and inhibited Tg secretion during short term culture are consistent with the findings of earlier studies with nonhuman thyrocytes. However, the later phase of enhanced cAMP levels with stimulation of Tg secretion indicates that EGF may have trophic effects on thyrocytes previously unrecognized because of the short term nature of the studies. These observations suggest an important role for EGF in maintenance of normal thyroid physiology.

Cells, Cultured↗
PubMed1988

Seronegative Hashimoto thyroiditis with thyroid autoantibody production localized to the thyroid.

A patient without serologic evidence of an autoimmune disorder had a thyroidectomy for neck compression caused by her goiter. Histologic examination of the gland revealed pathologic changes compatible with Hashimoto disease, and lymphocytes isolated from her thyroid gland were transformed into lymphoblastoid cells in vitro by Epstein-Barr virus in the presence of cyclosporine. These cells produced antibodies against thyroglobulin, thyroid microsome, thyrocyte membrane, and thyrotropin, whereas lymphoblastoid cells produced from the patient's peripheral blood lymphocytes showed no antithyroid activity. Several human monoclonal antibodies were produced from the intrathyroidal lymphocytes by fusion with the SHM-D33 heteromyeloma, and the resulting cell lines produced antibodies with high-affinity binding specific for thyroid antigens. These studies show that lymphocytes capable of producing antithyroid antibodies can be present in the thyroid glands of patients with Hashimoto disease without evidence of a peripheral immune response, thus indicating that Hashimoto disease can exist as an organ-restricted autoimmune disorder.

Adipose Tissue↗
PubMed1988

Eponyms.

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Eponyms↗
PubMed1987

Intrinsic abnormality of thyroid cells from a patient with a Brobdingnagian goiter.

Thyrocytes from normal and goitrous portions of the thyroid gland from a patient with an enormous (635 gm) goiter were cultured in media, and their relative abilities to uptake thymidine, synthesize DNA, and secrete Tg and T4 were assessed. Tg, T4 and the ratio Tg/T4 in media at 72 h were 120 micrograms/dl, 1.6 micrograms/dl and 75 for normal cells, and 410 micrograms/dl and 273 for goitrous cells. DNA synthesis was 30-100% greater in goitrous than normal cells over a period of 72 h indicating abnormally high rates of cell division and growth, but their thymidine uptake was only 20% of that in normal cells. TSH elicited stimulation of thymidine uptake and DNA synthesis both in goitrous and in normal cells, but to a lesser extent in goitrous cells. No evidence of growth stimulating autoantibody activity was detected in the patient's serum. These data indicate that although the ability of goitrous cells to uptake thymidine was impaired, their DNA synthesis was more active than normal thyroid, which may have led to disordered cell growth as evidenced by the enormous goiter size in this patient. Although goitrous cells secreted more than three times as much Tg into media compared to normal, media T4 levels were similar, indicating an increased synthesis yet low iodination of Tg in goitrous cells. There does not appear to be any support for TGSI mediation of the goiter in this patient, but rather, the goiter may have been due to an intrinsic alteration in DNA synthesis resulting in vigorous cell growth.

Cells, Cultured↗
PubMed1986

L-thyroxine dosage: a reevaluation of therapy with contemporary preparations.

Traditional L-thyroxine dosing formulas may overestimate the thyroid hormone requirement in patients treated with contemporary L-thyroxine preparations. We did clinical and laboratory assessments of 41 patients treated in successive periods with Levothroid (Armour Pharmaceuticals, Kankakee, Illinois) and Synthroid (Flint Division, Travenol Laboratories, Morton Grove, Illinois), obtaining 87 sets of data. Clinical subgroups were defined on the basis of the thyrotrophin response to thyrotrophin-releasing hormone. Normal responses were seen in 9 of 14 (64%) patients taking 100 micrograms/d and were associated with an average replacement dosage of 127 micrograms/d (1.7 micrograms/kg body weight). Nine of twenty-eight (32%) serum thyroxine values in the "physiologically replaced" group were elevated. Forty-three of fifty-four (80%) patients ingesting 125 micrograms or more had blunted responses (thyroxine "overreplaced"), averaging a daily dosage of 154 micrograms (2.14 micrograms/kg X d). No significant difference was found between Levothroid and Synthroid in predicting clinical group assignment. Guidelines for currently available L-thyroxine preparations should be revised and the recommended dosage reduced.

Adult↗
PubMed1985

A rapid, sensitive enzyme-linked immunoassay for human thyrotropin.

In this enzyme-linked immunoassay for human thyrotropin (TSH) in unextracted serum we use 96-well immunoenzymometric assay plates, first coated with polyclonal antibody to TSH, then incubated with the serum samples and reacted with mouse monoclonal antibody to human TSH. After incubation with alkaline phosphatase-labeled antibody against mouse IgG, disodium p-nitrophenyl phosphate is added and the color change is measured spectrophotometrically. Assay sensitivity is 0.1 milli-int. unit/L. Cross reactivity with lutropin, follitropin, or choriogonadotropin was negligible. TSH concentrations ranged from 0.4 to 4.1 milli-int. units/L in 43 normal subjects (mean 2.0, SD 1.0), and were uniformly less than 0.3 milli-int. unit/L in 23 patients with hyperthyroidism. Features which make this assay advantageous to the clinical laboratory include ease of set-up, ability to assay many samples at a time, high sensitivity, rapid turnaround time (8 h), and absence of requirements for radioactive materials.

Animals↗