ArticleThe Journal of cell biology1987
Calcium-sensitive, lipid-binding cytoskeletal proteins of the human placental microvillar region.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli.Molecular biology of the cell · 2000Article
- 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
- Expression of annexin VI (p68, 67 kDa-calelectrin) in normal human tissues: evidence for developmental regulation in B- and T-lymphocytes.Histochemistry · 1991Article
- Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor.The Journal of cell biology · 1989Article
- Functional and genetic analysis of annexin VI.Molecular and cellular biochemistryReview
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we describe a group of Ca2+-sensitive proteins located in the microvillar region of the human placental syncytiotrophoblast. By following the distribution of proteins between the particulate and supernatant phases of detergent-solubilized microvilli in the presence of defined concentrations of free Ca2+, we demonstrate a class of proteins of subunit molecular weights 72,000, 69,000, 38,000, 36,000, and 32,000 that associate with both the cytoskeleton and lipid at high concentrations of free Ca2+. These proteins can be released from microvilli using EGTA-containing buffers. Although they do not bind to phenyl-Sepharose, they will bind to phospholipids immobilized on phenyl-Sepharose columns in a Ca2+-dependent manner and show a marked preference for phospholipids with negatively charged headgroups. The results provide evidence for a sequence of events which may occur within the microvillus as the localized concentration of intracellular free Ca2+ rises.
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Registered trials
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