Bovine Thyroid Research Articles

Partial Characterization of Guanylyl Cyclase Activity in Calf Thyroid

The aim of the present study was to perform the partial characterization of the enzyme guanylyl cyclase (GC) in bovine thyroid. The results obtained showed the presence of two types of GC: one is soluble and comprises around 79% of total activity, while the other is particuiate. Treatment with 1% Triton X-100 increased both activities.When the kinetics of the enzyme was analyzed, using the complex MnGTP as a substrate, the results showed a Michaelis type kinetics for the soluble enzyme, with a Km of 0.037 mM, whereas the particulate GC showed a positive allosteric behavior with a S0.5 of 0.214 mM and a Hill coefficient of 1.9, indicating that the enzyme has at least two binding sites for the substrate. When the influence of different Mn2+ concentrations was studied, a positive allosteric behavior for the soluble GC was found, with a S0.5 of 1.2 mM and a Hill coefficient of 2.2. The kinetics of the particulate enzyme under similar conditions was of Michaelis type, with a Km of 0.752 mM.Although the enzyme is highly dependent on Mn2+ it was of interest to investigate the possible effects of other divalent cations, such as Ca2+ and Mg2+ The replacement of Mn2+ for Mg2+ caused a complete disappearance of the particulate enzyme activity, while the soluble activity decreased by 85%. Addition of Ca2+ had no effect on either GC. However, with suboptimum. concentrations of Mn2+, high Ca2+ concentration caused an increase in soluble activity, but it comprised only 20% of maximum activity with optimum Mn2+ concentrations. With the particulate enzyme a slight but significant inhibition was observed.

Novel dolichyl derivatives in rat spleen.

Novel dolichyl derivatives were found in rat spleen. The compounds were eluted from reverse phase HPLC after eluting dolichyl fatty acid ester. The elution profiles of the unsaponified forms of the unknown compounds were coincident with that of dolichol from spleen on reverse phase HPLC. The compounds were not dolichyl dolichoate, which are present in bovine thyroid. The compounds were not found in young rats (4 months of age) but were found in old rats (above 12 months of age), and they were not detected in other tissues under our conditions.

Nitric oxide donors inhibit iodide transport and organification and induce morphological changes in cultured bovine thyroid cells.

Nitric oxide (NO) has been proposed as an intracellular signal in the thyroid. The NO effect on function and morphology of bovine thyroid follicles in culture was analyzed by using the NO donors sodium nitroprusside (SNP) and S-nitrosoglutathione (GSNO). Both NO donors induced a concentration-dependent NO release measured by the nitrite accumulation in the culture medium. The SNP (10 to 500 micromol/L) treatment for 24 hours significantly inhibited the uptake, organification and transport of iodide in a concentration-dependent manner. When SNP (50 micromol/L) was withdrawn from the culture medium after 24 hours' incubation, iodide uptake and organification were partially recovered at 24 hours and reached the control value at 48 hours, indicating a reversible effect of SNP. A possible involvement of cyanide in the SNP inhibitory effect was excluded because incubation of follicles with potassium cyanide (KCN) at concentrations estimated to be present in the medium (40 and 80 micromol/L) for 24 hours did not modify iodide uptake and organification. The GSNO (10 to 500 micromol/L) treatment for 24 hours also reduced the iodide uptake, organification and transport in a concentration-dependent manner. A significant inhibition of iodide organification was induced after incubation with 1000 micromol/L of N2, 2'-O-dibutyrylguanosine 3':5'-cyclic monophosphate ([Bu]2cGMP). Morphological evaluation by light microscopy revealed that the incubation with NPS or GSNO (500 micromol/L) produced cellular dispersion with loss of follicular cell aggregates that was evident at 96 hours exposure. Cell viability was not altered by 10-500 micromol/L SNP or GSNO (80% to 85%). We concluded that long-term NO exposure induces functional and morphological modifications compatible with a loss of differentiation in thyroid follicles. These observations further support a role of NO in the regulation of the thyroid function.

The Application of anin VitroPerfused Liver Preparation to Examine the Effects of Epinephrine and Bovine Thyroid-Stimulating Hormone on Triiodo-l-thyronine Release from the Liver of Rainbow Trout (Oncorhynchus mykiss)

An isolated, perfused rainbow trout liver preparation was developed to investigate the action of nonthyroidal hormones on hepatic thyroid hormone metabolism. Several assessments were made of the stability and viability of the preparations under a range of conditions, including measures of lactate dehydrogenase flux and tissue ATP and glycogen content, all of which indicated that the perfused liver was stable for the 60-min perfusion period. Moreover, the liver preparations were responsive to an epinephrine challenge and, throughout the series of experiments, sustained hepatic glucose release. Triiodo-l-thyronine (T3) flux from the liver preparation was significantly increased by the provision of thyroxine (T4) substrate. Epinephrine and bovine thyroid stimulating hormone (TSH) were perfused alone and in combination with T4to evaluate the effect of these hormones on T3flux from the liver. Both epinephrine and TSH significantly enhanced hepatic T3flux in the absence of T3substrate, but neither had an additional effect on T3flux when perfused in combination with T4. The results of the study suggest that a relationship exists between the circulating levels of nonthyroid hormones and peripheral thyroid hormone metabolism that may be receptor-mediated.

Biochemical and functional changes during the bovine fetal thyroid development.

To establish biochemical and functional relations during thyroid development, the activity of thyroid peroxidase (TPO), nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome c reductase and monoamine oxidase (MAO) in a particulate fraction and the iodide transport and organification in slices of bovine fetal thyroid were examined throughout gestation. The cytochemical localization of TPO, H2O2 generating sites and MAO was also studied. Fetal glands were grouped in stages I to V according to increasing developmental features; adult tissues were also analyzed. TPO activity in each of the fetal stages was higher than in the adult; a marked increase was observed in stages IV and V. Iodide transport (T/M) was similar in stages I to V and the adult. Iodide organification in fetal thyroids showed a similar pattern to that of TPO activity. When compared with the adult, at midgestation (stages II to III), a lower iodination coexisted with a higher TPO activity. The activity of NADPH-cytochrome c reductase and MAO, two enzymes previously proposed to participate in thyroid H2O2 generation, did not parallel the level of iodide organification. Cells from stages II to V exhibited a positive cytochemical reaction for TPO in the rough endoplasmic reticulum (RER) and the perinuclear cisternae (PC). In stages IV, V, and adult, TPO was occasionally found in apical vesicles and microvilli, whereas H2O2 was detected within the RER and the PC. MAO reaction was positive in adult, but not in fetal thyroid. These results indicate that a high TPO activity accompanied the onset of the organification process during fetal thyroid development. The level of iodination was associated with the presence of TPO at a proper site rather than to the level of TPO activity. Evidence against a role of NADPH-cytochrome c reductase and MAO in the iodide organification was obtained.

Calmodulin purified from human and porcine thyroids inhibits thyrotropin binding to porcine thyroid cells.

A thyrotropin (TSH) binding inhibiting protein (TBIP) that inhibits TSH binding to the TSH receptor, as determined by the TSH receptor assay, was purified from human and porcine thyroid. The soluble fraction (100,000 x g supernatant of Graves' thyroid homogenate) was precipitated with ammonium sulfate between 1.75 to 2.5 mol/L. TBIP was eluted by 0.5 mol/L sodium chloride (NaCl) containing 20 mmol/L Tris buffer, pH 7.5 from a Q-sepharose column. The unbound fraction from concanavalin A (Con A) and blue-sepharose was gel-filtered using sephadex G-100, and finally purified by Resource Q column chromatography. Purified TBIP was confirmed as a single protein band of 17 kDa. The TBI activity in the purified TBIP was significantly decreased by either etnylene glycol tetraacetate (EGTA) (1 mmol/L) or antibody to calmodulin (CaM) in the TSH receptor assay. The TBIP was confirmed immunologically as CaM by the Ouchterlony method using antibody for CaM. These findings demonstrated that the TBIP purified from human and porcine thyroids was, in fact, CaM. We examined the effects of TBIP purified from human thyroid on bovine TSH (bTSH) or thyroid stimulating antibody (TSAb)-stimulated cyclic adenosine monophosphate (cAMP) production in porcine thyroid cells (PTC). TBIP itself did not increase basal levels of cAMP production, but inhibited bTSH (100 mU/L)-stimulated cAMP production. However, TBIP did not inhibit cAMP production stimulated by TSAb-IgG and various thyroid stimulators (GTPgammaS, forskolin and pituitary adenylate cyclase-activating polypeptide [PACAP, 27 and 38 amino acids]). Authentic CaM purified from bovine brain behaved in a manner similar to that of TBIP. These data showed that CaM differentially affects thyroid stimulation by TSH and TSAb in intact thyroid cell experiments.

The Na+-I- cotransporter of the thyroid: characterisation of new inhibitors.

New inhibitors of the Na+-I- cotransporter of the thyroid in bovine thyroid slices and in bovine plasma membrane vesicles have been investigated. They include: (1) econazole; (2) 5-(N,N-hexamethylene)amiloride (HMA); and (3) dysidenin. In both systems, the kinetics of iodide transport yielded apparent Km values of 39 and 14 microM respectively. The possible interaction of each of these inhibitors with the iodide site of the Na+-I- cotransporter was tested by performing detailed transport kinetics analysis at varying iodide concentrations and at 150 mM NaCl. Econazole induced a non-competitive inhibition while dysidenin and HMA gave a mixed type of inhibition. The Ki values for dysidenin and econazole, computed from Dixon plots, were 5 and 2 microM respectively while the Ki value for HMA could not be determined. Each inhibition was reversible, indicating the absence of covalent binding of the inhibitor to the Na+-I- cotransporter.

Expression of CFTR in human and bovine thyroid epithelium.

The expression of cystic fibrosis transmembrane conductance regulator (CFTR) in the thyroid has not been documented to date, although a role for CFTR in the thyroid follicular epithelium is suggested both clinically, by the occurrence of subclinical hypothyroidism in patients with cystic fibrosis (CF), and physiologically, by the presence of low-conductance, adenosine 3',5'-cyclic monophosphate-activated Cl channels in the follicular cells. Using reverse transcriptase-polymerase chain reaction with nested primers derived from exons 13 and 14 of the human CF gene, we have now documented the presence of CFTR mRNA in the human thyroid. Western blot analyses using six antibodies directed against different domains of human CFTR showed that a 165-kDa band was present in membrane extracts from bovine and human thyroid. This protein has the predicted size of mature CFTR and was not detected with preimmune serum or preadsorbed antiserum. By immunofluorescence and immunoperoxidase, CFTR was located in the follicular cells, with a diffuse, intracellular labeling pattern. Quantitative analysis revealed that 64% of the follicles were CFTR positive, but only 16% of the follicular cells were stained per follicle. The number of CFTR-positive cells was inversely proportional to the size of the follicle. These results 1) demonstrate the expression of CFTR at the mRNA and protein levels in human and bovine thyroid follicular cells and 2) suggest that CFTR expression could be instrumental in follicular enlargement.

Bovine thyrotropin receptor cDNA is characterized by full-length and truncated transcripts.

The complete coding sequence for the bovine thyrotropin (TSH) receptor was derived using a modified PCR cloning strategy. The bovine thyrotropin receptor conforms to the pattern of receptor interacting with membrane-bound G-protein already established in other species for TSH and gonadotropins receptors. The cDNA for the bovine TSH receptor consists of an open reading frame 2289 nucleotides in length, corresponding to a protein of 763 amino acids (estimated molecular mass of 86.4 kDa) which includes a 20 amino acid putative leading signal peptide. The receptor consists of a large NH2-terminal extracellular membrane domain of 417 amino acids with 5 potential N-linked glycosylation sites, a transmembrane domain (265 amino acids) consisting of 7 putative membrane alpha-helix spanning segments, and an intracytoplasmic COOH-terminal domain (82 amino acids). The bovine TSH receptor is one amino acid less than the corresponding sequence in dog, human, rat and mouse. Cysteine residues (n = 22) were conserved when compared with other TSH receptors. Three potential phosphorylation sites were found in the transmembrane domain and the COOH-terminal domain. As with other members of this receptor family, alternative splicing was observed. A transcribed but truncated TSH receptor of 1769 nucleotides was demonstrated, lacking half of the V segment of the transmembrane domain up to the COOH-terminal domain of the full length TSH receptor. Additionally, alternative transcriptional start sites were observed. Northern blot analysis using a probe (1170 bp) spanning part of the extracellular domain up to the first loop of the transmembrane domain showed specific expression in the bovine thyroid gland with major transcripts of 9.3 and 4.3 kb, and a minor transcript of 3.8 kb being detected.

Determination of total iodine and sample preparation for AMS measurement of 129I in environmental matrices

A method is described for the measurement of total iodine and sample preparation for accelerator mass spectrometry (AMS) measurement of 129I. Samples were combusted in a stream of oxygen and the iodine liberated was collected in a trapping solution. Aliquots of the trapping solution were used to measure total iodine by gas chromatography and 129I by AMS. The method was tested using standard reference materials 2709 San Joaquin Soil, 2711 Montana Soil and 2704 Buffalo River Sediment from the National Institute of Standards and Technology, IAEA-375 soil from the International Atomic Energy Agency, a bovine thyroid sample from Gomel, KI and KIO3. The recoveries with respect to the reference values were between 89 and 100%. No tracers were used and no efficiency corrections were applied to these results.

A guide to the literature on aggressive behavior

A guide to the literature on aggressive behavior

Detection of Sheep-Associated Malignant Catarrhal Fever Virus Antibodies by Complement Fixation Tests.

Some serological diagnosis methods and examinations for detection of antibodies to sheep-associated malignant catarrhal fever (MCF) infection were investigated. The wildebeest-associated MCF virus strain WC11 propagated on fetal bovine thyroid cell cultures was used as an antigen. Antibodies were detected by complement fixation (CF) tests in cattle pathologically diagnosed as having sheep-associated MCF, as well as in cattle experimentally infected with MCF virus strain WC11. However, immunodiffusion precipitation was only detected in cattle infected with MCF virus strain WC11. The results of serological investigation by CF tests indicated that 64.3% of sheep possessed antibodies to MCF virus in the Hokkaido district of Japan and all serum samples which contained CF antibody titers greater than 1:4 had antibody titers larger than 1:8 in indirect immunofluorescence tests. The CF test we demonstrated here is available to quantitatively detect MCF virus antibody titers in epidemiological surveys.

Evidence that thyroglobulin has an associated protein kinase activity correlated with the presence of an adenosine triphosphate binding site

19S Thyroglobulin (Tg), a dimeric glycoprotein with an M(r) of 660,000, was extracted from rat, bovine, and human (goitrous) thyroid tissues, as well as from culture medium of FRTL5 rat thyroid cells. Subjected to rigorous purification procedures, all Tg preparations showed a protein kinase activity that is able to phosphorylate serine residues in vitro. Further characterization of this enzymatic activity revealed that Tg has the specificities of a protein kinase A when Kemptide was used as specific substrate and after analysis of cAMP-stimulated phosphotransferase activity in all Tg preparations tested. Furthermore, Tg contains a specific and saturable ATP binding site, as evidenced by specific binding with the ATP affinity analog p-fluorosulfonylbenzoyl 5'-p-adenosine (FSO2BzAdo). Limited proteolysis of FSO2[14C]BzAdo-labeled human goiter Tg with clostripain gave rise to a M(r) 64,000 amino terminal polypeptide carrying almost all of the label. The analysis of this fragment revealed two sequences that may play an analogous phosphate-loop (P-loop) function, even though their primary sequences differ slightly from the classical A consensus sequence or P-loop. The ATP binding site of Tg may be functionally associated with the presence of a protein kinase A phosphorylating activity linked to the Tg itself, because the addition of the analog is able to inhibit the enzymatic activity in a dose-dependent fashion. Contamination with non-Tg phosphorylase cannot be ruled out at present, even though the amount of ATP that Tg was able to bind did not significantly change during the various purification steps. Together these findings favor the hypothesis that the Tg molecule contains a protein kinase activity that is capable of autophosphorylation.

Evidence that thyroglobulin has an associated protein kinase activity correlated with the presence of an adenosine triphosphate binding site.

19S Thyroglobulin (Tg), a dimeric glycoprotein with an M(r) of 660,000, was extracted from rat, bovine, and human (goitrous) thyroid tissues, as well as from culture medium of FRTL5 rat thyroid cells. Subjected to rigorous purification procedures, all Tg preparations showed a protein kinase activity that is able to phosphorylate serine residues in vitro. Further characterization of this enzymatic activity revealed that Tg has the specificities of a protein kinase A when Kemptide was used as specific substrate and after analysis of cAMP-stimulated phosphotransferase activity in all Tg preparations tested. Furthermore, Tg contains a specific and saturable ATP binding site, as evidenced by specific binding with the ATP affinity analog p-fluorosulfonylbenzoyl 5'-p-adenosine (FSO2BzAdo). Limited proteolysis of FSO2[14C]BzAdo-labeled human goiter Tg with clostripain gave rise to a M(r) 64,000 amino terminal polypeptide carrying almost all of the label. The analysis of this fragment revealed two sequences that may play an analogous phosphate-loop (P-loop) function, even though their primary sequences differ slightly from the classical A consensus sequence or P-loop. The ATP binding site of Tg may be functionally associated with the presence of a protein kinase A phosphorylating activity linked to the Tg itself, because the addition of the analog is able to inhibit the enzymatic activity in a dose-dependent fashion. Contamination with non-Tg phosphorylase cannot be ruled out at present, even though the amount of ATP that Tg was able to bind did not significantly change during the various purification steps. Together these findings favor the hypothesis that the Tg molecule contains a protein kinase activity that is capable of autophosphorylation.

Molecular Cloning and Characterization of Bovine β-Mannosidase

Deficiency of lysosomal beta-mannosidase activity results in a severe neurodegenerative disease in goats and cattle and a relatively milder phenotype in humans. A cDNA coding for the entire beta-mannosidase protein is described. Mixed oligonucleotides derived from bovine beta-mannosidase peptide sequences were used to screen a bovine thyroid cDNA library. Clones covering about 80% of the C-terminal region were recovered. The missing 5'-region was obtained using the technique of 5'-rapid amplification of cDNA ends. The composite cDNA contains 3852 nucleotides, encoding 879 amino acids. The N-terminal methionine is followed by 16 amino acids displaying the characteristics of a typical signal peptide sequence. The deduced amino acid sequence is colinear with all peptide sequences determined by protein microsequencing. Northern blot analysis demonstrates a single 4.2-kilobase transcript in various tissues from both normal and affected goats and calves. The mRNA level is decreased in tissues of affected beta-mannosidosis animals. The gene encoding beta-mannosidase is localized to human chromosome 4 as shown by Southern analysis of rodent/human somatic cell hybrids. This is the first report of cloning of lysosomal beta-mannosidase.

Aggressive Behavior and Fire-Setting in a 4-Year-Old Boy Associated with Ingestion of Ground Beef Contaminated with Bovine Thyroid Tissue: A Case Report and Review of Neuropsychiatrie Findings in Pediatric Thyrotoxicosis

An epidemic of thyrotoxicosis in 1984—1985 was traced to the ingestion of ground beef that was contaminated by bovine thyroid tissue in the tri-state area of Minnesota, South Dakota, and Iowa. This article describes a case of possible thyrotoxicosis-induced violent aggressiveness and firesetting in a 4-year-old boy affected by this epidemic. Although psychosocial factors were initially considered primary, dietary factors eventually proven to be etiologic. This child showed spontaneous decreases in violent behavior during two admissions to a hospital (where thyroid-laced beef was not available) and recurrences with returning home (where he ate contaminated ground beef). A literature review on neuropsychiatrie manifestations of pediatric thyrotoxicosis revealed that thyrotoxicosis in children may present with subtle symptoms (new onset of ADHD, drop in school grades) or overt neuropsychiatric disorders (anxiety, mood, cognitive or psychotic disorders). However, the literature did not appear to have revealed previous reports of violent aggressiveness or firesetting in children. Our case suggests that thyrotoxicosis is able to induce or exacerbate behavioral deterioration, including marked aggressivity, in susceptible children. Clinicians should watch for thyrotoxicosis, which may occur without thyroid disease for a variety of reasons. Delayed treatment can result in enduring physical, cognitive, and emotional disturbances.

Hypothalamic and Thyroidal Regulation of Growth Hormone in Tilapia

A radioimmunoassay (RIA) for recombinant tilapia growth hormone (GH) was established and validated. The ability of various hypothalamic factors to regulate GH secretion in the tilapia hybrid ( Oreochromis niloticus × Oreochromis aureus) was studied. Somatostatin 1-14 (SRIF 1-14; 10-100 μg/kg) was found to reduce circulating GH levels in a dose-dependent manner. SRIF 1-14 (0.1-1000 n M) inhibited GH release from perifused pituitary fragments (ED 50 0.83 n M). Human growth hormone-releasing hormone fragment 1-29 (hGHRH 1-29; 100 μg/kg) doubled circulating GH levels and modestly stimulated GH secretion in vitro. Carp growth hormone-releasing hormone (cGHRH) stimulated GH secretion in vitro to a similar degree at the same dose (1 μ M). Injection of salmon gonadotropin-releasing hormone (sGnRH) superactive analog (10-100 μg/kg) increased plasma GH levels sixfold. sGnRH also stimulated GH release in vitro (ED 50 142.56 n M). Dopamine (0.1-10 μ M) and the D 1 DA receptor agonist SKF 38393 increased GH secretion from perifused pituitary fragments dose-relatedly. Thyrotropin-releasing hormone (TRH) had no effect on GH secretion from perifused pituitary fragments, but increased plasma GH levels, as did bovine thyroid stimulating hormone (bTSH). The increased plasma GH in the bTSH-treated fish coincided with a dramatic increase in T 4; however, TRH increased GH without changing T 4 levels. T 3 increased the synthesis of GH by isolated pituitaries (incorporation of [ 3H]leucine). SRIF 1-14 seems to be a most potent hypothalamic regulator of GH secretion in tilapia; sGnRH and DA both increased GH secretion, although sGnRH elicited considerably greater responses at lower doses. Two forms of GHRH increased GH levels, although the unavailability of the homologous peptide prevented an accurate evaluation of its importance in regulating GH secretion. The thyroid axis (TRH, TSH, and T 3) stimulates both synthesis and release of GH, although TRH did not appear to have a direct effect on the level of the pituitary.

Thyroid iodide transport is reduced by administration of monoamine oxidase A inhibitors to rats.

The present work was addressed to study a possible relationship between monoamine oxidase (MAO) and the thyroid iodide transport mechanism. Normal rats treated with clorgyline (a selective MAO-A inhibitor) or tranylcypromine (a non-selective MAO inhibitor) showed a significantly diminished thyroid MAO activity, while deprenyl and pargyline (MAO-B inhibitors) did not modify the thyroidal enzyme activity with respect to the control group. Under these conditions, in vivo iodide transport was reduced both by clorgyline and tranylcypromine administration whereas it remained unchanged after treatment with MAO-B inhibitors. The effect of MAO inhibitors on thyroid MAO activity and in vivo iodide transport was also evaluated in rats treated with exogenous thyrotrophin (TSH) after endogenous TSH secretion blockade produced by T4 administration. In this condition, thyroid MAO activity was significantly lowered by clorgyline and was not modified by deprenyl. In contrast to the results observed in normal rats, in vivo iodide transport in TSH-treated rats remained unaltered after treatment either with clorgyline or deprenyl. MAO activity evaluated in bovine thyroid follicles in primary culture was highly sensitive to low concentrations of clorgyline (< 10 nmol/l) and relatively insensitive to deprenyl, a finding that indicates a predominance of the MAO-A isoform in the follicular cells in culture. When clorgyline (0.1 and 1 mumol/l) or deprenyl (1 mumol/l) were added to the culture medium, no modifications in the active transport of iodide were observed. These results indicate the absence of a direct linkage between thyroid MAO activity and the active iodide transport.(ABSTRACT TRUNCATED AT 250 WORDS)

Fetal Thyroid Metabolism: A Pluralistic System

ThyroidVol. 4, No. 3 Fetal Thyroid Metabolism: A Pluralistic SystemD.A. FISHER, D.H. POLK, and S.Y. WUD.A. FISHERSearch for more papers by this author, D.H. POLKSearch for more papers by this author, and S.Y. WUSearch for more papers by this authorPublished Online:4 Feb 2009https://doi.org/10.1089/thy.1994.4.367AboutSectionsPDF/EPUB ToolsPermissionsDownload CitationsTrack CitationsAdd to favorites Back To Publication ShareShare onFacebookTwitterLinked InRedditEmail FiguresReferencesRelatedDetailsCited byBisphenols as Environmental Triggers of Thyroid Dysfunction: Clues and Evidence13 April 2020 | International Journal of Environmental Research and Public Health, Vol. 17, No. 8Disorders of the Thyroid GlandMaternal hypothyroidism: An overview of current experimental modelsLife Sciences, Vol. 187Evidence for bisphenol A-induced disruption of maternal thyroid homeostasis in the pregnant ewe at low level representative of human exposureChemosphere, Vol. 182Perinatal Factors Associated with the Preterm Thyroid Screening TestKorean Journal of Perinatology, Vol. 27, No. 1Thyroid Hormone Metabolism and TransportRôle de l’hormone thyroïdienne T3 dans la régénération axonale chez les vertébrés supérieurs27 March 2013 | médecine/sciences, Vol. 29, No. 3Thyroid hormone triggers the developmental loss of axonal regenerative capacity via thyroid hormone receptor α1 and krüppel-like factor 9 in Purkinje cells13 August 2012 | Proceedings of the National Academy of Sciences, Vol. 109, No. 35Disorders of the Thyroid GlandOxidative stress elevated DNA damage and homocysteine level in normal pregnant women in a segment of Pakistani population24 November 2010 | Molecular Biology Reports, Vol. 38, No. 4Fetal and Neonatal Thyroid PhysiologyThyroid Hormone MetabolismThyroid System Immaturities in Very Low Birth Weight Premature InfantsSeminars in Perinatology, Vol. 32, No. 6Disorders of the Thyroid in the Newborn and InfantHigh Risk of Congenital Hypothyroidism in Multiple PregnanciesThe Journal of Clinical Endocrinology & Metabolism, Vol. 92, No. 8Thyroid Medications During PregnancyTherapeutic Drug Monitoring, Vol. 28, No. 3Hypothyroxinaemia and thyroid function after preterm birthSeminars in Neonatology, Vol. 9, No. 1Fetal and Neonatal Thyroid PhysiologyThyroid Disease During PregnancyPregnancy and Hyperthyroidism28 March 2013Fetal-Perinatal Thyroid PhysiologyPostnatal thyroid hormone replacement in very preterm infantsSeminars in Perinatology, Vol. 25, No. 6Effects of Thyroid Hormone Deficiency on Electrocardiogram Findings of Congenitally Hypothyroid Neonates9 July 2004 | Thyroid, Vol. 11, No. 8Thyroid hormones and their effects: a new perspective11 January 2007 | Biological Reviews, Vol. 75, No. 4The Potential Repercussions of Maternal, Fetal, and Neonatal Hypothyroxinemia on the Progeny30 January 2009 | Thyroid, Vol. 10, No. 10Thyroid Function and Thyroid Hormone Requirements of Very Preterm Infants1 June 2000 | NeoReviews, Vol. 1, No. 6Thyroid Function during Pregnancy1 December 1999 | Clinical Chemistry, Vol. 45, No. 12Hypothyroxinemia in Premature Infants: Is Thyroxine Treatment Necessary?30 January 2009 | Thyroid, Vol. 9, No. 7Thyroid Function in Very Preterm Newborns: Possible Implications30 January 2009 | Thyroid, Vol. 9, No. 1Thyroid Function Tests in the Newborn Infants of Preeclamptic WomenJournal of Pediatric Endocrinology and Metabolism, Vol. 12, No. 1Thyroid Function in Premature Infants: The Hypothyroxinemia of PrematurityClinics in Perinatology, Vol. 25, No. 4Somatosensory Evoked Potentials in Very Preterm Infants in Relation to l -Thyroxine Supplementation1 May 1998 | Pediatrics, Vol. 101, No. 5Biochemical and Functional Changes During the Bovine Fetal Thyroid Development3 February 2009 | Thyroid, Vol. 8, No. 1Thyroid Function in Very Preterm Infants: Influences of Gestational Age and DiseasePediatric Research, Vol. 42, No. 5The Hypothroxinemia of PrematurityThe Journal of Clinical Endocrinology & Metabolism, Vol. 82, No. 6The Regulation of Thyroid Function in Pregnancy: Pathways of Endocrine Adaptation from Physiology to PathologyEndocrine Reviews, Vol. 18, No. 3Fetal Thyroid Function: Diagnosis and Management of Fetal Thyroid DisordersClinical Obstetrics and Gynecology, Vol. 40, No. 1 Volume 4Issue 3Jan 1994 To cite this article:D.A. FISHER, D.H. POLK, and S.Y. WU.Fetal Thyroid Metabolism: A Pluralistic System.Thyroid.Jan 1994.367-371.http://doi.org/10.1089/thy.1994.4.367Published in Volume: 4 Issue 3: February 4, 2009PDF download

Establishment and Characteristics of a Cell Line from Fetal Bovine Thyroid (FBTY)

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