Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0265264 (HOS)
 1,119 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Estrogens play a central role in modulating bone turnover and in the postmenopausal female are formed almost exclusively by peripheral conversion of sex steroid precursors derived from the adrenals. In this study we have demonstrated that three human osteoblastic cell lines [HOS, U20S (HTB96) and MG63] possess the enzymes necessary for estrogen synthesis and metabolism. Aromatase, estradiol 17 beta-hydroxysteroid dehydrogenase (reductive and oxidative) and estrone sulfatase activities were measured in whole cell monolayers over a 20 h period by isotopic assay techniques. Significant aromatase activity was detected in all three cell lines ranging from 1.8 +/- 0.2 fmol/20 h/10(6) cells (mean +/- S.D., n = 3) for MG63 cells to 51 +/- 1.5 fmol/20 h/10(6) cells for HOS cells. The specific aromatase inhibitor, 4-hydroxyandrostenedione (1 mumol/L) completely inhibited aromatase activity in these cells. Two of the cell lines, HOS and MG63, had significant estradiol 17 beta-hydroxysteroid dehydrogenase activity with oxidative (32.7 +/- 1.9 and 1068.4 +/- 40.2 fmol/20 h/10(6) cells respectively) predominant over reductive activity (1.6 +/- 0.4 and 38.7 +/- 1.8 fmol/20 h/10(6) cells). All three cell lines were able to hydrolyse estrone sulfate to estrone with activities ranging from 13.3 +/- 1.5 fmol/20 h/10(6) cells for U20S cells to 482.2 +/- 3.7 fmol/20 h/10(6) cells for MG63 cells. Since estrogen has been implicated as a critical factor in the modulation of bone resorption and formation, the regulation of skeletal estrogen production, particularly at the time of the menopause, is likely to be an important mechanism by which bone volume is determined in physiological and pathological states.
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PMID:Estrogen synthesis by osteoblast cell lines. 139 46

The alteration of main disaccharide units in the skin of hairless mice (HOS:Hr 1) after chronic and repeated ultraviolet light (UV) radiation was investigated using high performance liquid chromatography after labeling with 1-phenyl-3-methyl-5-pyrazolone. The total amount of main disaccharide units increased by UVA irradiation at the 24th and 36th weeks in comparison with the control. At the 36th week UVA significantly increased hyaluronic acid-derived delta Di-HA (HA). Dermatan sulfate-derived delta Di 4S (DS) and chondroitin sulfate-derived delta Di-4S (CS) increased at the 36th week, although not statistically significant. The total amount of main disaccharide units was increased significantly by UVB irradiation at the 24th week as compared with the control. Concerning the compositional change in main disaccharide units after a 36-week repeated exposure, the decrease in delta Di-HA(HA) and the increase in delta Di-4S (DS) were found in the order of control, UVA- and UVB-irradiated groups. These results, for the first time, indicate the precise alterations of glycosaminoglycans, both in the total amount and in the composition, confirming the previous histochemical findings. This disaccharide analysis should provide a useful method to examine the biochemical changes of skin glycosaminoglycans in photoaging.
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PMID:Disaccharide analysis of the skin glycosaminoglycans in chronically ultraviolet light-irradiated hairless mice. 853 12

We have demonstrated steroid sulfatase activity in osteoblast cells and characteristics of the enzyme were also investigated. Cell free homogenate of rat osteoblast cell line, UMR106-01 and human osteoblast cell lines, MG-63, HOS were incubated with [3H] dehydroepiandrosterone-sulfate (DHEA-sulfate) or [3H] estrone-sulfate (E1-sulfate). The formation of DHEA or E1 from the corresponding substrate was identified by crystallization to constant specific activity. Michaelis constant (K(m)) for DHEA-sulfate was estimated as 2.1 x 10(-8)M in UMR106-01, 7.4 x 10(-7)M in MG-63, 5.8 x 10(-7)M in HOS and that for E1-sulfate was 4.1 x 10(-7)M, 3.0 x 10(-7)M, 9.8 x 10(-7)M, respectively. The expression of steroid sulfatase messenger ribonucleic acid in human osteoblast cells, HOS and MG-63 was first demonstrated by reverse transcription-polymerase chain reaction. The existence of steroid sulfatase in human and rat osteoblast cells suggests that osteoblast cells have the capacity to convert circulating sulfo-conjugated steroids to more active androgens and estrogens. This may indicate an important role of bone in facilitating hormonal action.
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PMID:Steroid sulfatase activity in osteoblast cells. 907 Feb 16

Sulfate conjugation is an important pathway in the metabolism of many drugs, xenobiotic compounds, and hormones. Sulfotransferases (SULTs) catalyze these reactions and have been detected and characterized in various human tissues including the liver and small intestine. Substrates for SULTs that include estrogen and thyroid hormones have well-established roles affecting skeletal integrity and disease processes. We performed the following studies to determine the presence of SULTs in human osteoblast-like cells, and to compare their characteristics to SULTs expressed in other human tissues. Four osteosarcoma cell lines (SaOS-2, U2-OS, PR, and HOS-TE85) were screened for the presence of four different SULT activities. Predominant activities were found for SULT1A1 in SaOS-2 cells, and SULT-1A3 in HOS-TE85 cells. Several biochemical properties of each enzyme that included apparent K(m) values, thermal stabilities, and responses to the inhibitors 2,6-dichloro-4-nitrophenol and NaCl were used to further characterize the SULT activities. High-performance liquid chromatography (HPLC) of the reaction products confirmed the known products of SULT1A1 and SULT1A3. When the mature human osteoblast HOB-03-CE6 cell line was tested for activity alone, the predominant activity was SULT1A3, with minimal SULT1A1. The results indicate that SULT1A1 and SULT1A3 are present in human osteosarcoma and mature osteoblast cell lines, and that the characteristics of the osteosarcoma cell SULTs are similar to those expressed in other human tissues. SULTs may have regulatory roles in the deactivation of thyroid hormones or estrogenic compounds in bone, and thus may affect hormone action and bone responses in the human skeleton.
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PMID:Thermostable (SULT1A1) and thermolabile (SULT1A3) phenol sulfotransferases in human osteosarcoma and osteoblast cells. 1142 50

The aim was to test whether sulfatase activity is differently regulated by tibolone in human bone, endometrium and breast cells since selective inhibition of sulfatases in various tissues may contribute to the tissue-specificity of tibolone. Tibolone, its 3 alpha- and 3 beta-hydroxy metabolites and their 3-sulfated forms, and its Delta(4)-isomer strongly (70-90%) inhibited the sulfatase activity in human breast cell lines (two T-47D clones) and intermediately (8-43%) in human endometrial cells (HEC-1A). In contrast, they did not inhibit sulfatase in two human osteoblast-like cell lines (MG 63, HOS TE-85). The specific sulfatase inhibitor, EMATE, showed inhibition in all cell lines. Just as estrone sulfate, 3 alpha-sulfated tibolone was also converted by sulfatase to the unconjugated 3 alpha-hydroxy-tibolone intracellularly in all cell lines. The tissue specific inhibition pattern of sulfatase activity by tibolone and its metabolites suggest that tibolone could be protective against development of mammary carcinomas, whereas it retains favorable estrogenic effects on bone.
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PMID:Tibolone: a compound with tissue specific inhibitory effects on sulfatase. 1160 25

The radical HSO is an oxidation product of pollutants such as H(2)S and CH(3)SH in Earth's atmosphere. For the first time, the interaction of HSO and its tautomer HOS with single water molecules to yield the hydrates HSO.nH(2)O and HOS.nH(2)O was studied for n = 1-3, applying the high-level G3X(MP2) theory. A large number of structures corresponding to local minima on the potential energy surfaces has been identified. While gaseous HSO is more stable than HOS, the enthalpy diffference between HSO.nH(2)O and HOS.nH(2)O decreases with increasing degree of hydration and becomes practically zero for n = 3. Thus, in aqueous solution as well as in fog and rain droplets, HOS is expected to compete with HSO. The barrier for the tautomerization of HSO to HOS is dramatically lowered by the presence of water molecules since a cyclic transition state allows a concerted proton shift within the system of neighboring hydrogen bonds. The corresponding activation enthalpy of only 73.5 kJ mol(-1) predicted for the transformation of HSO.2H(2)O into HOS.2H(2)O may be compared to the 202 kJ mol(-1) reported for the tautomerization of the unhydrated gaseous HSO/HOS molecules. The impact of water of hydration on the fundamental vibrational modes of HSO and HOS has also been studied. Furthermore, HOS is predicted to dimerize at low temperatures to give two van der Waals molecules with singlet (symmetry C(2)) or triplet configuration (symmetry C(2h)), the latter being more stable than the singlet isomer. The disproportionation of 2HSO to H(2)S and SO(2) is predicted to be exothermic by -263.5 kJ mol(-1). The reaction of HSO with ozone to HSO(2) and O(2) is also strongly exothermic by -274.0 kJ mol(-1) and seems to proceed without any barrier. HOS forms a 1:1 van der Waals complex with O(3); the redox reaction of its two components is calculated as exothermic by -410.9 kJ mol(-1) and results in a rather stable adduct between HOSO and O(2) with the structure of a peroxo isomer of HOSO(3). This unprecedented hydrogen peroxosulfite radical might open a novel route to atmospheric sulfate without the intermediate formation of SO(2) and SO(3).
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PMID:Reversal of the relative stability of the isomeric radicals HSO and HOS upon hydration and their reactions with ozone. 2021 92

We have carried out species determination and kinetic analysis in the hydrogen peroxide-thiosulfate reaction by means of capillary electrophoresis and high performance liquid chromatography. In addition to thiosulfate, dithionate, trithionate, and tetrathionate, other polythionates such as pentathionate and hexathionate were detected during the oxidation process. The polythionates found are sensitive to the pH, with the average length of the sulfur chain decreasing with increasing pH. By varying the pH and the concentrations of the reactants, we find that the reaction is first order with respect to each of the reactants with rate constant k = 0.025 M(-1) s(-1). With HOS(2)O(3)(-), HSO(3)(-)/SO(3)(2-), S(3)O(6)(2-), S(4)O(6)(2-), and S(5)O(6)(2-) as key intermediates that are eventually oxidized to sulfate, a proposed 14-step kinetic model simulates the reaction process, including the evolution of the thiosulfate and tetrathionate concentrations at various pHs.
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PMID:Oxygen-sulfur species distribution and kinetic analysis in the hydrogen peroxide-thiosulfate system. 2051 27