Alteration of Free Calcium Levels and Acylphosphatase Muscular Isoenzyme in Cultured Dystrophic Skin Fibroblasts
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 230, Issue: 2, Page: 327-330
1997
- 3Citations
- 2Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations3
- Citation Indexes3
- Captures2
- Readers2
Article Description
Levels of free intracellular calcium have been measured on two cell lines of cultured human fibroblasts carrying the genetic lesions occurring in Duchenne and Becker dystrophies. Both cell lines elicited a markedly higher content of the cation (98 nM and 57 nM, respectively) than control fibroblasts (35 nM). Differences toward controls were statistically significant (p<0.01). Dystrophic fibroblasts were also found to possess a significantly reduced amount by about 50% of muscular acylphosphatase isoenzyme as compared to normal cells. As acylphosphatase was demonstrated to be involved in the regulation of Ca 2+ -ATPase activity from different sources, a hypothesis was formulated that could explain the disruption of calcium homeostasis as an effect of the altered acylphosphatase activity.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0006291X96959549; http://dx.doi.org/10.1006/bbrc.1996.5954; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0030614862&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9016776; https://linkinghub.elsevier.com/retrieve/pii/S0006291X96959549; https://dx.doi.org/10.1006/bbrc.1996.5954
Elsevier BV
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