ArticleProceedings of the National Academy of Sciences of the United States of America1993
Caldesmon and a 20-kDa actin-binding fragment of caldesmon inhibit tension development in skinned gizzard muscle fiber bundles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 55 citations in OpenAlex.
- Regulation of Vascular Tone of Preglomerular Renal Vasculature by Caldesmon.Journal of the American Heart Association · 2026Article
- Dual thick and thin filament linked regulation of stretch- and L-NAME-induced tone in young and senescent murine basilar artery.Frontiers in physiology · 2023Article
- Caldesmon ablation in mice causes umbilical herniation and alters contractility of fetal urinary bladder smooth muscle.The Journal of general physiology · 2021Article
- New insights into myosin phosphorylation during cyclic nucleotide-mediated smooth muscle relaxation.Journal of muscle research and cell motility · 2012Article
- Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1.The Journal of physiology · 2003Article
- Thiophosphorylation-induced Ca(2+) sensitization of guinea-pig ileum contractility is not mediated by Rho-associated kinase.The Journal of physiology · 2001Article
- Caldesmon exhibits a clustered distribution along individual chicken gizzard native thin filaments.Journal of muscle research and cell motility · 2001Article
- Mutant Caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis.Molecular biology of the cell · 2001Article
- A role for p21-activated kinase in endothelial cell migration.The Journal of cell biology · 1999Article
- Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.Molecular biology of the cell · 1999Article
- Clostridium difficile toxin B inhibits carbachol-induced force and myosin light chain phosphorylation in guinea-pig smooth muscle: role of Rho proteins.The Journal of physiology · 1998Article
- Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.Biophysical journal · 1997Article
- Affinity and structure of complexes of tropomyosin and caldesmon domains.Biophysical journal · 1996Article
- The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations.Pflugers Archiv : European journal of physiology · 1996Article
- Phosphorylation of caldesmon by mitogen-activated protein kinase with no effect on Ca2+ sensitivity in rabbit smooth muscle.The Journal of physiology · 1995Article
- Kinetics of binding of caldesmon to actin.The Journal of biological chemistry · 1995Article
- The variable coupling between force and myosin light chain phosphorylation in Triton-skinned chicken gizzard fibre bundles: role of myosin light chain phosphatase.Pflugers Archiv : European journal of physiology · 1995Article
- Augmented agonist-induced Ca(2+)-sensitization of coronary artery contraction in genetically hypertensive rats. Evidence for altered signal transduction in the coronary smooth muscle cells.The Journal of clinical investigation · 1994Article
- Calmodulin and the regulation of smooth muscle contraction.Molecular and cellular biochemistry · 1994Review
- Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin.Biophysical journal · 1993Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Caldesmon is known to inhibit actin-activated myosin ATPase activity in solution, to inhibit force production when added to skeletal muscle fibers, and to alter actin movement in the in vitro cell motility assay. It is less clear that caldesmon can inhibit contraction in smooth muscle cells in which caldesmon is abundant. We now show that caldesmon and its 20-kDa actin-binding fragment are able to inhibit force in chemically skinned gizzard fiber bundles, which are activated by a constitutively active myosin light-chain kinase in the presence and absence of okadaic acid. This inhibitory effect is reversed by high concentrations of Ca2+ and calmodulin. Therefore, caldesmon may act by increasing the level of myosin phosphorylation required to obtain full activation. Our results also suggest that caldesmon does not act to maintain force in smooth muscle by cross-linking myosin with actin since competition of binding of caldesmon with myosin does not cause a reduction in tension.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.