Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

C4A and C4B levels were measured in serum from 246 normal individuals. Complement-mediated solubilisation, assayed using alkaline phosphatase anti-alkaline phosphatase immune complexes (IC), correlated with both C4A and C4B levels. However, C4A and C4B levels showed no correlation with solubilisation of bovine serum albumin (BSA) ICs, or with the prevention of immune precipitation of BSA or alkaline phosphatase ICs, nor with immune adherence assayed using thyroglobulin and BSA ICs.
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PMID:The relative roles of C4A and C4B in prevention of immune precipitation, solubilisation and immune adherence. 129 20

Assays were developed to detect and measure autoantibodies (AA) to thyroglobulin (Tg) and to the thyroid hormones, thyroxine (T4) and triiodothyronine (T3). An ELISA to detect AA to Tg was developed, using purified canine Tg as the antigen and goat anti-canine IgG conjugated with alkaline phosphatase as the second antibody. A highly charged agarose electrophoresis assay was used for determination of AA to T4 and T3. Sera from dogs (n = 119) with clinical signs consistent with hypothyroidism were tested for AA to Tg, T4, and T3. Autoantibodies to at least 1 of the 3 thyroid antigens were detected in 58 of the 119 (48.7%) sera tested. Autoantibodies to Tg were detected more frequently in samples with low serum concentrations of thyroid hormones than in samples with normal concentrations. The presence of AA to T4, T3, or both was not significantly associated with low thyroid hormone concentrations, but this lack of association may have been attributable to binding of AA in the measurement of thyroid hormones by radioimmunoassay.
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PMID:Prevalence of autoantibodies to thyroglobulin, thyroxine, or triiodothyronine and relationship of autoantibodies and serum concentrations of iodothyronines in dogs. 158 11

We determined approximately 15,000 laboratory values in 236 individuals between the ages of 60 and 90 y, 22 individuals between 90 and 99 y, and 69 individuals greater than or equal to 100 y, and compared these with values in young adults. We tested 47 different analytes in the 60-90-y group and 93 analytes in the greater than or equal to 90-y group. Na, K, Cl, and CO2 values were either identical or showed minimal change with age; pH decreased slightly. Differences in Ca values were only minor, but ionized Ca increased slightly. Phosphate decreased in men, but changed only minimally in women; parathyroid hormone increased with age. Increases with age were also observed for glucose, insulin, and C-peptide. Among the enzymes, alkaline phosphatase increased in women, but in men only greater than 90 y; gamma-glutamyltransferase increased in both sexes. Creatine kinase (CK) decreased slightly in individuals greater than 70 y and markedly in those greater than 90 y of age, whereas CK-MB decreased markedly greater than 70 y, reaching the detection limit in individuals greater than 90 y. Lactate dehydrogenase isoenzyme 5 decreased slightly with age. Urea nitrogen increased gradually with age, but creatinine increased only in individuals greater than or equal to 90 y. The increase in urea is not paralleled by a loss of protein in urine, suggesting that the possible cause of azotemia may not always be renal pathology. Urate increased in women but not in men. Liver function, as measured by total bilirubin and liver enzymes, was exceedingly well maintained. Concentrations of most proteins show little change, except for slight decreases in prealbumin, albumin, and transferrin, proteins used as an index of nutritional status. IgA values increased, IgG ranges were wider, IgM and IgD decreased, and the range for IgE was narrower than in young adults. Cholesterol, high-density lipoprotein cholesterol, and triglyceride values increased with age, but decreased in individuals greater than or equal to 90 y. Among the trace elements, magnesium changed little, zinc and lead decreased, and copper values increased with age. Total triiodothyronine and thyroxine decreased, with concomitant increases in thyroid-stimulating hormone. More individuals had increased microsomal antibodies and thyroglobulin titers in the aging population than in the young. In men, the free, percent free, bioactive, and total testosterone values decreased, but luteinizing hormone (LH) and follicle-stimulating hormone (FSH) values increased. In women, estrone and estradiol values decreased, with concomitant increases in LH and FSH. Androstenedione and progesterone decreased in both sexes.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Laboratory values in fit aging individuals--sexagenarians through centenarians. 159 90

We showed previously that human thyroglobulin (hTG) contains anionic complex carbohydrate units with up to four sulfate groups, some containing both sulfate and sialic acid. Recent reports indicate that the carbohydrate units of hTG may also contain phosphate, but these reports are not all in accord. The purpose of this study was to confirm the presence of phosphate on the carbohydrate units of hTG and to determine whether phosphate coexists with other acidic moieties, such as sulfate and sialic acid, on the same carbohydrate units. Alkaline phosphatase and acid hydrolysis were used to detect phosphate on the sulfated carbohydrate units of hTG derived from normal and neoplastic tissues. Thyroid fragments from two patients were incubated for 16 h in [35S]sulfate-containing medium, and hTG was purified. Complex carbohydrates were released from hTG with endoglycosidase-F and analyzed at pH 2.2 on a HPLC ion exchange column. Sulfate-containing peaks were monitored by radioactivity, and sialic acid-containing ones were identified by their reduced charge after neuraminidase or acid treatment. None of the sulfate-labeled carbohydrate peaks shifted after alkaline phosphatase treatment alone, indicating that none of them contained phosphomonoesters. Several of the sulfate-labeled peaks shifted after acid hydrolysis, some to positions of decreased charge, due to removal of sialic acid, and some to positions of increased charge, suggesting the presence of phosphodiesters. The latter was confirmed by the observation that some of the newly formed peaks were susceptible to alkaline phosphatase digestion. Thus, acid hydrolysis converted phosphodiesters into alkaline phosphatase-susceptible phosphomonoesters, most likely mannose-6-phosphate. We conclude that some anionic complex carbohydrate units of hTG contain exclusively sulfate, while others contain combinations of sulfate, sialic acid, and phosphodiesters. Phosphodiesters are present in the sulfated carbohydrate units of hTG from normal as well as neoplastic thyroid tissue.
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PMID:Anionic carbohydrate groups of human thyroglobulin containing both phosphate and sulfate. 185 82

We have evaluated the epitope specificity of natural antihuman thyroglobulin (hTg) autoantibodies (aAb) in the plasma of healthy individuals. By an indirect ELISA technique, we selected 56 plasma samples with high anti-hTg antibody activity and used the IgG fraction isolated from these plasma to study the antigenic domains on the hTg molecule recognized by the natural anti-hTg aAb. A panel of 15 mAb, coupled to alkaline phosphatase and recognizing six regions (I to VI) on the hTg molecule, served to identify the domains recognized by the natural anti-hTg aAb using a competitive ELISA procedure. A total of 26 of the IgG fractions was found to interact with at least one of the regions defined by our battery of mAb. Region V was recognized by the majority of the IgG fractions. Interestingly, region II was rarely recognized by the same IgG fraction that reacted with region V. Inasmuch as we have previously shown that region II is mainly recognized by aAb in the serum of subjects with various thyroid disorders, we propose that recognition of region V reflects the normal physiologic state of the immune system with respect to the hTg molecule.
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PMID:Significance of the recognition of certain antigenic regions on the human thyroglobulin molecule by natural autoantibodies from healthy subjects. 247 18

The properties and distribution of an enzyme specifically hydrolyzing cytidine-5'-monophosphate and the possible relationship of the enzyme to the synthesis and secretion of thyroid hormone in man were investigated using cytochemical methods. Activity due to cytidine-5'-monophosphatase was separated from that due to acid or alkaline phosphatase, both of which are also capable of hydrolyzing cytidine-5'-monophosphate. This distinction was established on the basis of manganese ion stimulation and differences in localization, levels of activity, and pH optimums. The localization of the enzyme along the face of Golgi apparatus involved in the formation of thyroglobulin suggests an association of the enzyme with the glycosylation of thyroglobulin.
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PMID:The ultracytochemical localization of cytidine-5'-monophosphatase in normal human thyroid follicle cells. 624 90

A rapid and simple enzyme-linked immunosorbent assay (ELISA) for anti-thyroglobulin IgG antibodies is described. The method is based on a 'sandwich' using purified human thyroglobulin adsorbed to polystyrene microplates, human serum and anti-human IgG antiserum conjugated to alkaline phosphatase. The sensitivity of the method is about 8 ng/ml, as evaluated with a purified anti-thyroglobulin antibody preparation. High concentrations of antibodies were observed, as expected, in autoimmune thyroid disease; however, the majority of normal subjects have detectable, although very low, antibody levels. We conclude the method is suitable for current clinical use.
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PMID:Anti-human thyroglobulin autoantibodies assayed by an enzyme-linked immunosorbent assay. 635 37

Alternative splicing of primary transcripts from the calcitonin/alpha calcitonin gene-related peptide (alpha CGRP) gene result in mature mRNAs encoding either calcitonin or alpha CGRP. We have produced sequence-specific, synthetic, biotinylated oligodeoxynucleotide probes that recognize calcitonin (exon 4), and alpha CGRP (exon 6) sequences as well as sequences common to both splice variants (exon 3) of this gene. Probes to exons 4 and 3 revealed strong cytoplasmic signals in rat parafollicular cells. In addition, a punctate nuclear signal was obtained with these probes. The alpha CGRP-specific (exon 6) probe resulted in weak cytoplasmic labelling of parafollicular cells, but produced a punctate nuclear labelling similar to that seen with the exon 4 and 3 probes. RNase digestion removed all the cytoplasmic and nuclear signals obtained with all probes. Hybridization with a thyroglobulin-specific probe failed to label parafollicular cells. A control (human enterovirus) probe yielded negative results, while a probe to rat somatostatin produced cytoplasmic labelling of a small subpopulation of parafollicular cells. Finally, a probe specific for beta CGRP mRNA labelled most, if not all, parafollicular cells. Fluorescent alkaline phosphatase development of in situ hybridizations could be combined with indirect immunofluorescence for CGRP. Analysis by fluorescence and confocal microscopy revealed that CGRP immunoreactive cells contained calcitonin, alpha CGRP and beta CGRP hybridization signals. Our results demonstrate that all three genes may be simultaneously expressed by thyroid parafollicular cells and show that synthetic biotinylated oligonucleotide probes can be used for highly precise localizations of primary transcripts in the nuclei of these cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Detection of primary and mature transcripts of calcitonin-gene-related peptide genes in rat parafollicular cells by light, fluorescence and confocal microscopy. 773 76

We showed previously that supplementation for 30 d with 800 IU (727 mg) vitamin E/d did not adversely affect healthy elderly persons. We have now assessed the effects of 4 mo of supplementation with 60, 200, or 800 IU (55, 182, or 727 mg) all-rac-alpha-tocopherol/d on general health, nutrient status, liver enzyme function, thyroid hormone concentrations, creatinine concentrations, serum autoantibodies, killing of Candida albicans by neutrophils, and bleeding time in 88 healthy subjects aged >65 y participating in a double-blind, placebo-controlled trial. No side effects were reported by the subjects. Vitamin E supplementation had no effect on body weight, plasma total proteins, albumin, glucose, plasma lipids or the lipoprotein profile, total bilirubin, alkaline phosphatase, serum aspartate aminotransferase, serum alanine aminotransferase, lactate dehydrogenase, serum urea nitrogen, total red blood cells, white blood cells or white blood cell differential counts, platelet number, bleeding time, hemoglobin, hematocrit, thyroid hormones, or urinary or serum creatinine concentrations. Values from all supplemented groups were within normal ranges for older adults and were not significantly different from values in the placebo group. Vitamin E supplementation had no significant effects on plasma concentrations of other antioxidant vitamins and minerals, glutathione peroxidase, superoxide dismutase, or total homocysteine. There was no significant effect of vitamin E on serum nonspecific immunoglobulin concentrations or anti-DNA and anti-thyroglobulin antibodies. The cytotoxic ability of neutrophils against Candida albicans was not compromised. Thus, 4 mo of supplementation with 60-800 IU vitamin E/d had no adverse effects. These results are relevant for determining risk-to-benefit ratios for vitamin E supplementation.
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PMID:Assessment of the safety of supplementation with different amounts of vitamin E in healthy older adults. 970 Nov 88

The molecules of the B7 family play a major role in T-lymphocyte costimulation through interaction with their counterreceptors CD28 and CTLA4. In the present study, we analyzed the possible expression of B7 molecules on surgically removed thyroid tissue of patients with autoimmune [Hashimoto's thyroiditis (HT) or Graves' disease (GD)] or nonautoimmune [nontoxic goiter (NTG) or papillary cancer (PC)] thyroid diseases. We found clear positivity of thyroid follicular cells for B7.1 in HT but not in GD, nor in nonautoimmune specimens (NTG, PC) using in situ analysis by alkaline phosphatase anti-alkaline phosphatase (APAAP) technique. Double immunostaining experiments in combination with an anti-human thyroglobulin antibody confirmed follicular B7.1 localization. On the contrary, no follicular B7.2 expression was observed in any specimen analyzed. These findings were confirmed by immunofluorescence flow cytometry on isolated follicular cells. The cytokines IL1beta and LPS were able to induce de novo B7.1 expression on cultured thyroid follicular cells. Intrathyroid T cells proved responsive to stimulation via the B7 ligand CD28, even in the absence of IL2. Moreover preliminary evidence was obtained for an inhibitory effect of anti-B7.1 mAb on T-cell proliferation in coculture with isolated thyroid follicular cells. It is conceivable that in HT, expression of B7.1 on follicular cells, together with MHC class II antigens and ICAM1, could provide a local costimulatory signal for T-lymphocyte differentiation toward the type 1 cytokine secretion pattern and maintenance of the autoimmune process.
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PMID:B7.1 costimulatory molecule is expressed on thyroid follicular cells in Hashimoto's thyroiditis, but not in Graves' disease. 981 3


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