Caldesmon, a calmodulin‐binding, F actin‐interacting protein, is present in aorta, uterus and platelets

Kakiuchi, Ritsu; Inui, Makoto; Morimoto, Kouichi; Kanda, Keiko; Sobue, Kenji; Kakiuchi, Shiro

doi:10.1016/0014-5793(83)80181-1

Cited by 57 publications

(36 citation statements)

References 21 publications

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“…In addition, Kakiuchi and co-workers have reported the detection of 150,000-mol-wt caldesmon- like proteins in platelets (12). These results suggest the 80-kD protein may be a proteolytic fragment.…”

Section: -Kd Caldesmon Was Purified According To the Published Promentioning

confidence: 90%

Identification by monoclonal antibodies and characterization of human platelet caldesmon.

Dingus¹,

Hwo²,

Bryan³

1986

The Journal of Cell Biology

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Abstract. Actin-based gels were prepared from clarified high-salt extracts of human platdets by dialysis against physiological salt buffers. The gel was partially solubilized with 0.3 M KC1. Mice were immunized with the 0.3 M KC1 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 Factin 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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Section: -Kd Caldesmon Was Purified According To the Published Promentioning

confidence: 90%

Identification by monoclonal antibodies and characterization of human platelet caldesmon.

Dingus¹,

Hwo²,

Bryan³

1986

The Journal of Cell Biology

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“…The specific rabbit IgG-fraction to chicken gizzard caldesmon was prepared from the serum by ammonium sulfate precipitation (48% saturation) followed by affinity chromatography on caldesmonSepharose 4B (16) . The anti-caldesmon serum was specific for caldesmon as determined by an Ouchterlony immuno-diffusion test (12) . The anti-chicken gizzard actin antibody was produced in rabbits by the method of Lazarides and Weber (13).…”

Section: Methodsmentioning

confidence: 99%

“…Since this protein could bind to F-actin and calmodulin alternatively depending upon the concentration of Ca2+ (flip-flop binding), it has been thought to play an important role in the control of actin-myosin interaction of smooth muscle cells (16). Caldesmon was subsequently found in bovine aorta and uterus, and human platelets biochemically (12). Morphologically, this calmodulin-binding, F-actin-interacting protein was demonstrated in smooth muscle cells and absorptive epithelial cells of the rat small intestine (11), and in the apical part of follicle epithelial cells of the rat thyroid (7).…”

mentioning

confidence: 99%

Immunocytochemical demonstration for caldesmon and actin in the striated and smooth muscle cells and non-muscular cells of various organs of rats.

Ban

Ishimura

Fujita

et al. 1984

Acta Histochem. Cytochem

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“…l-Caldesmon has a role in the organization and stabilization of the microfilament network, thus regulating proliferation and migration (Kordowska et al 2006;Yokouchi et al 2006;Morita et al 2007). High-molecular-mass isoforms (h-caldesmon, 120 to 150 kDa) are predominantly expressed in differentiated smooth-muscle cells (SMCs), with only a few reported exceptions; platelets, colorectal pericryptal fibroblasts, and myoepithelial cells of galactophorous sinuses of human breast tissue contain h-caldesmon as well (Kakiuchi et al 1983;Frid et al 1992;Lazard et al 1993;Nakayama et al 1999). In vitro studies suggest that h-caldesmon modulates the contraction of smooth muscle by inhibiting actomyosin ATPase.…”

Section: Introductionmentioning

confidence: 99%

The Actin-binding Protein Caldesmon Is in Spleen and Lymph Nodes Predominately Expressed by Smooth-muscle Cells, Reticular Cells, and Follicular Dendritic Cells

Köhler

2009

J Histochem Cytochem.

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Reticular cells and follicular dendritic cells (FDCs) build up a framework that underlies the compartmentalization of spleens and lymph nodes. Subpopulations of reticular cells express the smooth-muscle isoform of actin, indicative of a specialized contractile apparatus. We have investigated the distribution of the actin-binding protein caldesmon in spleen and lymph nodes of mice and rats. Caldesmon modulates contraction and regulates cell motility. Alternative splicing of transcripts from a single gene results in high-molecular-mass isoforms ( h-caldesmon) that are predominately expressed by smooth-muscle cells (SMCs), and low-molecular-mass isoforms ( I-caldesmon) that are thought to be widely distributed in non-muscle tissues, but the distribution of caldesmon in spleen and lymph nodes has not been reported. We have performed Western blot analysis and immunohistochemistry using four different antibodies against caldesmon, among these a newly developed polyclonal antibody directed against recombinant mouse caldesmon. Western blot analysis showed the preponderance of I-caldesmon in spleen and lymph nodes. Our results from immunohistochemistry demonstrate caldesmon in SMCs, as expected, but also in reticular cells and FDCs, and suggest that the isoform highly expressed by reticular cells is I-caldesmon. In spleen of SCID mice, caldesmon was expressed by reticular cells in the absence of lymphocytes.

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Caldesmon, a calmodulin‐binding, F actin‐interacting protein, is present in aorta, uterus and platelets

Cited by 57 publications

References 21 publications

Identification by monoclonal antibodies and characterization of human platelet caldesmon.

Identification by monoclonal antibodies and characterization of human platelet caldesmon.

Immunocytochemical demonstration for caldesmon and actin in the striated and smooth muscle cells and non-muscular cells of various organs of rats.

The Actin-binding Protein Caldesmon Is in Spleen and Lymph Nodes Predominately Expressed by Smooth-muscle Cells, Reticular Cells, and Follicular Dendritic Cells

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