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

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

syn-HOSO is the most stable form of hydrogenated sulfur dioxide, a possible intermediate in the creation of sulfuric acid. Recent work has characterized the structure and rotational constants, but the present work provides new insights into the vibrational spectra of this molecule. The central S-O bond is weaker than the terminal S-O bond, which allows for near-free rotation of the hydrogen atom. The stretches and the torsional modes are relatively bright infrared emitters/absorbers. The torsional mode is very low in frequency making it a potential target for terahertz observation. The other vibrational frequencies for HOSO are reduced relative to the corresponding frequencies in SO2, H2SO4, and the HOS radical making the infrared features of syn-HOSO likely red-shifted in mixed spectral observation, where oxygen, hydrogen, and sulfur are all found.
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PMID:Quantum Chemical Rovibrational Analysis of the HOSO Radical. 2897 56