ArticleThe Journal of cell biology1986
Identification by monoclonal antibodies and characterization of human platelet caldesmon.
Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 69 citations in OpenAlex.
- Ablation of smooth muscle caldesmon affects the relaxation kinetics of arterial muscle.Pflugers Archiv : European journal of physiology · 2013Article
- The actin-binding protein caldesmon is in spleen and lymph nodes predominately expressed by smooth-muscle cells, reticular cells, and follicular dendritic cells.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
- New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010Review
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- Mutant Caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis.Molecular biology of the cell · 2001Article
- A 32-nucleotide exon-splicing enhancer regulates usage of competing 5' splice sites in a differential internal exon.Molecular and cellular biology · 1995Article
- Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.Biophysical journal · 1995Article
- Overexpression of human fibroblast caldesmon fragment containing actin-, Ca++/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments.The Journal of cell biology · 1994Article
- Localization of caldesmon and its dephosphorylation during cell division.The Journal of cell biology · 1993Article
- Interaction of caldesmon with phospholipids.The Biochemical journal · 1993Article
- Genomic structure of the human caldesmon gene.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Regulation by Ca(2+)-calmodulin of the actin-bundling activity of Physarum 210-kDa protein.Journal of muscle research and cell motility · 1992Article
- The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes.The Journal of cell biology · 1992Article
- The molecular anatomy of caldesmon.The Biochemical journal · 1991Review
- Sequence of an avian non-muscle caldesmon.Journal of muscle research and cell motility · 1991Article
- Microinjection of nonmuscle and smooth muscle caldesmon into fibroblasts and muscle cells.The Journal of cell biology · 1990Article
- Characterization of 83-kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin.The Journal of cell biology · 1988Article
- Autophosphorylation of smooth-muscle caldesmon.The Biochemical journal · 1988Article
- Expression of high and low molecular weight caldesmons during phenotypic modulation of smooth muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 1987Article
- Calcium-independent contraction in lysed cell models of teleost retinal cones: activation by unregulated myosin light chain kinase or high magnesium and loss of cAMP inhibition.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin-based gels were prepared from clarified high-salt extracts of human platelets by dialysis against physiological salt buffers. The gel was partially solubilized with 0.3 M KCl. Mice were immunized with the 0.3 M KCl extract of the actin gel, and hybridomas were produced by fusion of spleen cells with myeloma cells. Three hybridomas were generated that secrete antibodies against an 80-kD protein. These monoclonal antibodies stained stress fibers in cultured cells and cross-reacted with proteins in several tissue types, including smooth muscle. The cross-reacting protein in chicken gizzard smooth muscle had an apparent molecular weight of 140,000 and was demonstrated to be caldesmon, a calmodulin and actin-binding protein (Sobue, K., Y. Muramoto, M. Fujita, and S. Kakiuchi, Proc. Natl. Acad. Sci. USA, 78:5652-5655). No proteins of molecular weight greater than 80 kD were detectable in platelets by immunoblotting using the monoclonal antibodies. The 80-kD protein is heat stable and was purified using modifications of the procedure reported by Bretscher for the rapid purification of smooth muscle caldesmon (Bretscher, A., 1985, J. Biol. Chem., 259:12873-12880). The 80-kD protein bound to calmodulin-Sepharose in a Ca++-dependent manner and sedimented with actin filaments, but did not greatly increase the viscosity of F-actin solutions. The actin-binding activity was inhibited by calmodulin in the presence of calcium. Except for the molecular weight difference, the 80-kD platelet protein appears functionally similar to 140-kD smooth muscle caldesmon. We propose that the 80-kD protein is platelet caldesmon.
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