ArticleThe Journal of cell biology1985
Comparison of Ca++-regulated events in the intestinal brush border.
Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 98 citations in OpenAlex.
- The Molecular Biology of Placental Transport of Calcium to the Human Foetus.International journal of molecular sciences · 2025Review
- Role of Neural Stem Cells and Vitamin D Receptor (VDR)-Mediated Cellular Signaling in the Mitigation of Neurological Diseases.Molecular neurobiology · 2022Review
- Calcium intake and urinary stone disease.Translational andrology and urology · 2014Review
- Enterocyte loss of polarity and gut wound healing rely upon the F-actin-severing function of villin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders.The Journal of cell biology · 1999Article
- Tomato annexins p34 and p35 bind to F-actin and display nucleotide phosphodiesterase activity inhibited by phospholipid binding.The Plant cell · 1996Article
- In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium.In vitro cellular & developmental biology. Animal · 1994Article
- Article
- High-purity isolation of bullfrog hair bundles and subcellular and topological localization of constituent proteins.The Journal of cell biology · 1991Article
- Purification and partial sequence analysis of plant annexins.The Biochemical journal · 1990Article
- Evaluation of the annexins as potential mediators of membrane fusion in exocytosis.Journal of bioenergetics and biomembranes · 1990Review
- Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.The Journal of cell biology · 1989Article
- "Bundle blot" purification and initial protein characterization of hair cell stereocilia.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains.The Journal of cell biology · 1988Article
- The 28-kDa calbindin-D is a major calcium-binding protein in the basilar papilla of the chick.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
- Calmodulin in normal and cystic fibrosis human intestine at different developmental stages.Gut · 1988Article
- The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits.The Journal of cell biology · 1987Article
- Article
- Calcium-sensitive, lipid-binding cytoskeletal proteins of the human placental microvillar region.The Journal of cell biology · 1987Article
- The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intestinal epithelial cell and specifically the cytoskeleton of the brush border are thought to be controlled by micromolar levels of free calcium. Calcium-binding proteins of this system include intestinal calcium binding protein (CaBP), calmodulin (CaM), villin, and a 36,000-mol-wt protein substrate of tyrosine kinases. To assess the sequence of events as the intracellular Ca++ level rises, we determined the amount of CaM and CaBP in the intestinal epithelium by western blotting and tested the Ca++ binding of CaM and CaBP by equilibrium dialysis. The Ca++-dependent actin severing activity of villin was analyzed in the presence of physiological CaM levels and increasing calcium concentrations. In addition, we analyzed the Ca++ levels required for interaction between CaM and the microvillus 110,000-mol-wt protein as well as fodrin and the interaction between a polypeptide of 36,000 mol wt (P-36) and actin. The results suggest that CaBP serves as the predominant Ca++ buffer in the cell, but CaM can effectively buffer ionic calcium in the microvillus and thus protect actin from the severing activity of villin. CaM binds to its cytoskeletal receptors, 110,000-mol-wt protein and fodrin differently, governed by the free Ca++ and pH. The interaction between P-36 and actin, however, appears to require an unphysiologically high calcium concentration (10(-4) to 10(-3) M) to be meaningful. The results provide a coherent picture of the different Ca++ regulated events occurring when the free calcium rises into the micromolar level in this unique system. This study would suggest that as the Ca++ rises in the intestinal epithelial cell an ordered sequence of Ca++ saturation of intracellular receptors occurs with the order from the lowest to highest Ca++ requirements being CaBP less than CaM less than villin less than P-36.
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