ArticleThe Biochemical journal1986
Proteins of the human placental microvillar cytoskeleton. alpha-Actinin.
Article in The Biochemical journal, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- The Molecular Biology of Placental Transport of Calcium to the Human Foetus.International journal of molecular sciences · 2025Review
- Human placental proteomics and exon variant studies link AAT/SERPINA1 with spontaneous preterm birth.BMC medicine · 2022Article
- Article
- Polycystin-2 cation channel function in the human syncytiotrophoblast is regulated by microtubular structures.The Journal of physiology · 2007Article
- Cytoskeletal regulation of calcium-permeable cation channels in the human syncytiotrophoblast: role of gelsolin.The Journal of physiology · 2005Article
- Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis.The Journal of cell biology · 1995Article
- A vitronectin-receptor-related molecule in human placental brush border membranes.The Biochemical journal · 1991Article
- Calcium-sensitive, lipid-binding cytoskeletal proteins of the human placental microvillar region.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human placental syncytiotrophoblast microvilli are supported by an underlying cytoskeleton consisting mainly of actin microfilaments. The major proteins associated with the actin have Mr values of 105 000, 80 000 and 68 000. The 105 000-Mr protein is recognized by an antibody preparation raised to purified chicken gizzard alpha-actinin. Electron microscopy has shown that the human placental protein has dimensions similar to those reported for muscle alpha-actinin. About half of the placental microvillar alpha-actinin is released from the cytoskeleton in the presence of Ca2+. This effect occurs at concentrations of Ca2+ greater than 0.3 muM and has been used as the basis of a method for the purification of the placental alpha-actinin. This sensitivity to Ca2+ is not affected by trifluoperazine and is therefore likely to be a property of the alpha-actinin as such rather than being mediated via calmodulin.
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Registered trials
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