249 research outputs found

    Left Ventricular Mass in Physically Active Adults with a Family History of Hypertension

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    Influence of Anthropometric Variables on Three Different Maximal Oxygen Consumption Units: NHANES 2003-2004

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    Does Weight Status Influence Cardiovascular Response to Sitting Versus Standing While Performing Computer Work?

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    Sex Hormone-Binding Globulin and Resting Testosterone Levels in Relation to Weight Status: NHANES 2003-2004

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    PARENT/CAREGIVER INVOLVEMENT IN 2018: PAST CHALLENGES AND FUTURE POSSIBILITIES IN A TECHNOLOGY-RICH SOCIETY

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    The purpose of the study was to explore how the use of technology can support parent/caregiver-teacher communications, thus allowing for parent/caregiver-teacher involvement through contemporary approaches. The study looked at how parent/caregivers and teachers define parent/caregiver involvement, what they see as barriers to parent/caregiver involvement, and how they believe technology can support the involvement experience. The review of literature examines varying factors that influence parent/caregivers’ level of involvement in their children’s schooling, as well as three major influences that have the greatest impact on student achievement: family, school, and community. It also identifies barriers to parent/caregiver involvement. Although challenges exist at the family, school, and community levels, the review of literature shows that the child receives maximum benefit when all parties collaborate. Interviews and surveys reveal how parent/caregivers and teachers of third-graders feel about parent/caregiver involvement and how technology affects communications between parent/caregivers and teachers. Findings indicate that parent/caregivers and teachers believe the use of technology supports parent/caregiver-teacher communications, therefore fostering parent/caregiver involvement. They believe it eases communication processes and allows parent/caregivers to be involved despite busy schedules. Parent/caregivers and teachers communicated that they still desire personal conversations with one another to address topics of concern, but, overall, they feel technology cultivates and supports parent/caregiver involvement

    Incorporation of a Product of Mevalonic Acid Metabolism Into Proteins of Chinese Hamster Ovary Nuclei

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    We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14C]mevalonate. Nuclear proteins of 68, 70, and 74 kD, posttranslationally modified by an isoprenoid, are also components of a nuclear matrix-intermediate filament preparation from CHO cells. Furthermore, the 68-, 70-, and 74-kD isoprenylated polypeptides are immunoprecipitated from cell extracts with two different anti-lamin antisera. Based on exact two-dimensional comigration with lamin B, both from rat liver lamin and CHO nuclear matrix-intermediate filament preparations, and its immunoprecipitation with anti-lamin antisera, we conclude that the 68-kD isoprenylated protein found in nuclei from [14C]mevalonate-labeled CHO cells is lamin B. The more basic 74-kD isoprenylated nuclear protein is similar in molecular mass and isoelectric pH variants to the lamin A precursor polypeptide reported by others. Starving cells for mevalonate results in a dramatic accumulation of a polypeptide that comigrates on two-dimensional, non-equilibrium pH gradient electrophoresis (NEPHGE) gels with the 74-kD isoprenylated protein. The 70-kD isoprenylated protein, which is resolved on NEPHGE gels as being higher in molecular mass and slightly more basic than lamin B, has not yet been identified

    Changes in Plasma Potassium During Graded Aerobic Exercise and Two Hours of Recovery

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    Plasma potassium increases with exercise intensity. Subjects (n=8) were monitored for changes in plasma potas-sium while exercising at progressively increasing steady-state intensities and for two hours of recovery. Plasma po-tassium was significantly increased at 100% of VO2peak compared to 20% and 40% (p<0.01). Plasma potassium at 60 and 120 minutes of recovery from exercise was significantly higher than 6 minutes post exercise (p<0.015). These results support the supposition that high-intensity exercise may lead to hyperkalemia, and also indicates that in-creases in [K + ] occur up to two hours after the cessation of exercise, a newly reported phenomenon. Although, high levels of plasma potassium are known to cause cardiac abnormalities and related events, exercise induced changes in normal healthy adults are not currently believed to have clinical implications

    Isoprenylation is Required for the Processing of the Lamin A Precursor

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    The nuclear lamina proteins, prelamin A, lamin B, and a 70-kD lamina-associated protein, are posttranslationally modified by a metabolite derived from mevalonate. This modification can be inhibited by treatment with (3-R,S)-3-fluoromevalonate, demonstrating that it is isoprenoid in nature. We have examined the association between isoprenoid metabolism and processing of the lamin A precursor in human and hamster cells. Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevinolin (lovastatin) specifically depletes endogenous isoprenoid pools and inhibits the conversion of prelamin A to lamin A. Prelamin A processing is also blocked by mevalonate starvation of Mev-1, a CHO cell line auxotrophic for mevalonate. Moreover, inhibition of prelamin A processing by mevinolin treatment is rapidly reversed by the addition of exogenous mevalonate. Processing of prelamin A is, therefore, dependent on isoprenoid metabolism. Analysis of the conversion of prelamin A to lamin A by two independent methods, immunoprecipitation and two-dimensional nonequilibrium pH gel electrophoresis, demonstrates that a precursor-product relationship exists between prelamin A and lamin A. Analysis of R,S-[5-3H(N)]mevalonate-labeled cells shows that the rate of turnover of the isoprenoid group from prelamin A is comparable to the rate of conversion of prelamin A to lamin A. These results suggest that during the proteolytic maturation of prelamin A, the isoprenylated moiety is lost. A significant difference between prelamin A processing, and that of p21ras and the B-type lamins that undergo isoprenylation-dependent proteolytic maturation, is that the mature form of lamin A is no longer isoprenylated
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