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1.
Osteoporos Int ; 25(7): 1917-29, 2014 Jul.
Article in English | MEDLINE | ID: mdl-24682357

ABSTRACT

UNLABELLED: We studied 472 elders to assess joint association of vitamin D receptor (VDR) variability and physical activity on low handgrip strength (LHS) and osteoporosis (OST). Our findings showed that higher risks of OST were associated with physically inactive elders with some specific VDR variations, highlighting the importance of promotion program for physical activity. INTRODUCTION: The aim of this study was to determine the joint association between VDR variability and physical activity on LHS and OST in community-dwelling elders. METHODS: Bone mineral density of the lumbar spine (LS), the femoral neck (FN), and the total hip were measured by dual-energy X-ray absorptiometry. Four single-nucleotide polymorphisms (SNPs) (rs7975232, rs1544410, rs2239185, and rs3782905) of the VDR gene were examined in 472 participants. RESULTS: Physical inactivity and each of the four SNPs were jointly associated with a significantly greater risk of LHS in people than that associated with each of the VDR SNPs or low physical activity alone. Physically inactive men with the AG or AA genotype of rs2239185 had a significantly greater risk of overall, LS, and FN OST than those of physically active men with the GG genotype [odds ratio (OR) 3.57, 95 % confidence interval (CI) 1.10-11.65; OR 4.74, 95 % CI 1.43-15.70; and OR 5.06, 95 % CI 1.08-23.71, respectively]. Similarly, physically inactive women with the CG or CC genotype of rs3782905 and the AG or AA genotype of rs1544410 had a significantly greater risk of FN OST than physically active women with the GG genotype (OR 5.33, 95 % CI 1.23-23.06 and OR 5.36, 95 % CI 1.11-25.94, respectively). CONCLUSIONS: VDR polymorphisms and physical activity are jointly associated with LHS and OST in elders. Health care programs should promote physical activity among elders as a cost-effective way to prevent LHS and OST, especially in those who may be genetically predisposed.


Subject(s)
Hand Strength/physiology , Motor Activity/physiology , Osteoporosis/genetics , Receptors, Calcitriol/genetics , Absorptiometry, Photon , Aged , Aged, 80 and over , Bone Density/physiology , Female , Femur Neck/physiopathology , Gene Frequency , Genetic Predisposition to Disease , Genotype , Hip Joint/physiopathology , Humans , Lumbar Vertebrae/physiopathology , Male , Osteoporosis/physiopathology , Polymorphism, Single Nucleotide
2.
Am J Clin Pathol ; 105(3): 360-3, 1996 Mar.
Article in English | MEDLINE | ID: mdl-8602618

ABSTRACT

A new herpesvirus-like DNA sequence (KSHV) has been recently identified in Kaposi's sarcoma (KS) from patients with AIDS and non-AIDS patients. To verify the specificity of the association of this new viral DNA with KS, a total of 155 cases of benign and malignant vascular neoplasms sharing similar histogenesis of endothelial derivation were analyzed for the presence of this KSHV sequence using the published 330-233 primers by polymerase chain reaction (PCR). The results revealed that all 17 cases of KS, both AIDS and non-AIDS, were positive for this KSHV, whereas the remaining 138 cases of vascular lesions other than KS, including 15 cases of angiosarcoma, showed negative reaction. These results confirm and extend the previous observation that this KSHV sequence is specifically associated with KS and is a reliable diagnostic marker to distinguish KS, particularly at its early stage, from other vascular lesions.


Subject(s)
DNA, Viral/analysis , Herpesviridae/isolation & purification , Sarcoma, Kaposi/virology , Vascular Neoplasms/virology , Acquired Immunodeficiency Syndrome/complications , Base Sequence , Biomarkers/analysis , Herpesviridae/genetics , Herpesviridae Infections/complications , Herpesviridae Infections/diagnosis , Herpesviridae Infections/pathology , Humans , Molecular Sequence Data , Polymerase Chain Reaction , Sarcoma, Kaposi/complications , Sarcoma, Kaposi/diagnosis , Sarcoma, Kaposi/pathology , Sequence Analysis, DNA , Vascular Neoplasms/diagnosis , Vascular Neoplasms/pathology
3.
J Pharm Sci ; 64(6): 1052-4, 1975 Jun.
Article in English | MEDLINE | ID: mdl-1133731

ABSTRACT

Binding of trichloromonofluoromethane, dichlorodifluoromethane, and dichlorotetrafluoroethane was studied in aqueous 5% human albumin solution, using the partition coefficient method in sealed serum bottles. The partition coefficient and the fraction of fluorocarbons bound were highly dependent on fluorocarbon concentrations. The average binding sites per molecule of albumin were 2.17, 0.30, and 0.42 and the binding association constants were 1.11 X10-3, 1.73 X10-3, and 5.06X10-3 M-minus 1, respectively. At the lowest concentration studied, 62.3, 25.5, and 65.6% were found bound to albumin, respectively. This appears to represent the first extensive study on any gas-albumin interaction.


Subject(s)
Aerosol Propellants/pharmacology , Aerosols/pharmacology , Fluorocarbon Polymers/pharmacology , Fluorocarbons/pharmacology , Serum Albumin/metabolism , Binding Sites , Binding, Competitive , Dose-Response Relationship, Drug , Drug Interactions , Humans , In Vitro Techniques
4.
Pharmacology ; 13(2): 128-36, 1975.
Article in English | MEDLINE | ID: mdl-1144513

ABSTRACT

Binding of dichlorotetrafluoroethane (F 114) with bovine albumin was studied at 37, 20.5 and 5 C. It was found that at the total concentration of 0.4 x 10-3 M of F 114 in the 5-percent protein solution, 50, 51 and 55% of them, respectively, were in bound form at the temperatures indicated above. The termodynamic data found for the F 114-bovine albumin interaction in the temperature range studied were: deltaG = -3.44 to -4.11 Kcal/mol. deltaS =20.40 to 20.45 e.u., and deltaH =2.23 Kcal/mol. It is postulated that the large positive entropic change associated with a sizable positive enthalpy change indicates that the breaking of iceberg water stucture and slight unfolding of albumin molecule are involved in the interaction.


Subject(s)
Albumins/metabolism , Fluorocarbon Polymers/metabolism , Fluorocarbons/metabolism , Aerosol Propellants , Animals , Cattle , Protein Binding , Solubility , Temperature
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