ArticleThe Biochemical journal1995
Calponin induces actin polymerization at low ionic strength and inhibits depolymerization of actin filaments.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 47 citations in OpenAlex.
- Promoting effects of calponin 3 on the growth of diffuse large B‑cell lymphoma cells.Oncology reports · 2023Article
- Article
- Molecular Profiles of Cell-to-Cell Variation in the Regenerative Potential of Mesenchymal Stromal Cells.Stem cells international · 2019Review
- Article
- Review
- UNC-87 isoforms, Caenorhabditis elegans calponin-related proteins, interact with both actin and myosin and regulate actomyosin contractility.Molecular biology of the cell · 2015Article
- Functional proteomic analysis of long-term growth factor stimulation and receptor tyrosine kinase coactivation in Swiss 3T3 fibroblasts.Molecular & cellular proteomics : MCP · 2012Article
- Effects of basic calponin on the flexural mechanics and stability of F-actin.Cytoskeleton (Hoboken, N.J.) · 2012Article
- The effects of combined cyclic stretch and pressure on the aortic valve interstitial cell phenotype.Annals of biomedical engineering · 2011Article
- Calponin h1 suppresses tumor growth of Src-induced transformed 3Y1 cells in association with a decrease in angiogenesis.Japanese journal of cancer research : Gann · 2002Article
- Contractile properties and proteins of smooth muscles of a calponin knockout mouse.The Journal of physiology · 2000Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calponin from chicken gizzard induced polymerization of actin in the presence of 10 mM KCl. Only 2 min after the addition of KCl in the presence of a 0.0625-0.25:1 molar ratio of calponin to actin, a Poisson-type length distribution (with an average length of approx. 0.7 micron) was observed with formed actin filaments. This result suggests that calponin-actin complexes served as nuclei for rapid elongation. Calponin caused a rapid polymerization of actin even in G-buffer (2 mM Tris/HCl, pH 8.0) which is usually used for depolymerization of actin filaments. Binding of calponin at a level of up to 1.25 mol per mol of actin was observed in the actin filaments formed in the presence of calponin at very low ionic strengths. When actin filaments were exposed to 3.3 mM KCl, by dilution with G-buffer, a rapid depolymerization occurred. Addition of calponin greatly retarded the depolymerization process and, in the presence of an equimolar ratio of calponin to actin, depolymerization hardly occurred. In the presence of calmodulin, this inhibitory effect on depolymerization was reversed by Ca2+, releasing calponin from actin filaments.
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