Acidic Calponin Cloned from Neural Cells is Differentially Expressed During Rat Brain Development

Ferhat, Lotfi; Charton, Gérard; Represa, Alfonso; Ben‐Ari, Y.; Terrossian, E. Der; Khrestchatisky, Michel

doi:10.1111/j.1460-9568.1996.tb01612.x

Cited by 40 publications

(38 citation statements)

References 28 publications

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“…Since acidic calponin is also expressed in glial cells (Ferhat et al, 1996;Plantier et al, 1999; present findings), we first investigated whether the increased labeling intensity for acidic calponin observed in the inner one-third of the molecular layer in pilocarpinetreated animals occurred in glial processes. For this purpose, double labeling for acidic calponin (red) and GFAP (green) was performed in pilocarpine-treated rats at 1 and 2 weeks.…”

Section: Immunolabeling For Acidic Calponin Was Absent From Presynaptmentioning

confidence: 96%

Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine‐induced seizures

et al. 2003

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We have previously shown that, in HEK 293 cells, overexpression of acidic calponin, an actin-binding protein, induces remodeling of actin filaments, leading to a change in cell morphology. In addition, this protein is found in dendritic spines of adult hippocampal neurons. We hypothesized that this protein plays a role in regulating actin-based filaments during dendritic spine plasticity. To assess this hypothesis, the pilocarpine model of temporal lobe epilepsy was selected because an important reorganization of the glutamatergic network, which includes an aberrant sprouting of granule cell axons, neo-synaptogenesis, and dendritic spine remodeling, is well established in the dentate gyrus. This reorganization begins after the initial period of status epilepticus after pilocarpine injection, during the silent period when animals display a normal behavior, and reaches a plateau at the chronic stage when the animals have developed spontaneous recurrent seizures. Our data show that the intensity of immunolabeling for acidic calponin was clearly increased in the inner one-third of the molecular layer of the dentate gyrus, the site of mossy fiber sprouting, and neo-synaptogenesis, at 1 and 2 weeks after pilocarpine injection (silent period) when the reorganization was taking place. In contrast, in chronic pilocarpine-treated animals, when the reorganization was established, the levels of labeling for acidic calponin in the inner molecular layer were similar to those observed in control rats. In addition, double immunostaining studies suggested that the increase in acidic calponin levels occurred within the dendritic spines. Altogether, these results are consistent with an involvement of acidic calponin in dendritic spine plasticity.

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Section: Immunolabeling For Acidic Calponin Was Absent From Presynaptmentioning

confidence: 96%

Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine‐induced seizures

et al. 2003

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“…Acidic (h3) calponin is found in the brain, mainly expressed by neurons [79], astrocytes [80], and glial cells [81] in the actin cytoskeleton with a proposed role in the plasticity of neural tissues [82,83]. Acidic calponin was also found in the post-synaptic side of symmetric synapses and accumulated in the post-synaptic densities of asymmetric synapses [80].…”

Section: Physiological and Pathological Significance Of Calponin In Nmentioning

confidence: 97%

Calponin in Non-Muscle Cells

Jin

2008

Cell Biochem Biophys

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Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and non-muscle cells. Calponin is an inhibitor of the actin-activated myosin ATPase. Three isoforms of calponin have been found in the vertebrates. Whereas the role of calponin in regulating smooth muscle contractility has been extensively investigated, the function and regulation of calponin in non-muscle cells is much less understood. Based on recent progresses in the field, this review focuses on the studies of calponin in non-muscle cells, especially its regulation by cytoskeleton tension and function in cell motility. The ongoing research has demonstrated that calponin plays a regulatory role in non-muscle cell motility. Therefore, non-muscle calponin is an attractive target for the control of cell proliferation, migration and phagocytosis, and the treatment of cancer metastasis.

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“…3 The expression of CaP isoforms is not restricted to muscle tissue, and different members of the CaP family have been identified in a wide range of vertebrate cells. CaP variants have thus been implicated in the regulation of a variety of actomyosin-based processes, including neurite outgrowth (33) and the organization of the nonmuscle cell cytoskeleton (34). The CLIK-23 module may have acquired a specialized function in the course of evolution from invertebrates to vertebrates and the concomitant specialization of different muscle types (see also Ref.…”

Section: Unc-87 Is An Actin-bundling Proteinmentioning

confidence: 99%

UNC-87 Is an Actin-bundling Protein

Kranewitter

Ylänne

Gimona

2001

Journal of Biological Chemistry

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The Caenorhabditis elegans unc-87 gene product is essential for the maintenance of the nematode body wall muscle where it is found colocalized with actin in the I band. The molecular domain structure of the protein reveals similarity to the C-terminal repeat region of the smooth muscle actin-binding protein calponin. In this study we investigated the in vitro function of UNC-87 using both the full-length recombinant molecule and several truncated mutants. According to analytical ultracentrifugation UNC-87 occurs as a monomer in solution. UNC-87 cosedimented with both smooth and skeletal muscle F-actin, but not with monomeric G-actin, and exhibited potent actin filament bundling activity. Actin binding was independent of the presence of tropomyosin and the actin cross-linking proteins filamin and ␣-actinin. Consistent with its actin bundling activity in vitro, UNC-87 tagged with green fluorescent protein associated with and promoted the formation of actin stress fiber bundles in living cells. These data identify UNC-87 as an actin-bundling protein and highlight the calponin-like repeats as a novel actin-binding module.The interaction of actin and myosin to produce force is an essential prerequisite for a variety of cellular processes including muscle contraction (1), cell motility, and anchorage (2). The organization of contractile and motile systems based on actin relies on a large family of actin-associated proteins that regulate and define the assembly of actin into filaments and then into filament arrays (3, 4). To date, more than 60 different proteins directly interacting with actin have been identified, but the majority of F-actin-binding proteins populate partially overlapping regions on the filament (5, 6). Despite the large number of actin-binding proteins, functional diversity is reflected by a limited number of basic structural modules (7). Most actin cross-linking proteins exhibit two independent actin-binding domains, each individual actin-binding domain commonly composed of a tandem arrangement of the calponin homology domain module (8) and other modular elements defining the distance between and the relative orientation of the two actin-binding domains, often involving parallel or antiparallel dimerization (7).We have shown recently that a unique sequence motif found in the C-terminal third of the calponin (CaP) 1 molecule and other members of the CaP family of actin-associated proteins (9), namely a 23-amino acid residue repeat, which we will refer to from now on as the CLIK-23 repeat, forms an independent actin-binding site (10). This finding was corroborated by Mino et al. (11) who demonstrated the direct interaction of a peptide corresponding to the first CaP repeat with actin in vitro. A survey of the available data bases identified other proteins with CLIK-23 repeats, in particular the Caenorhabditis elegans body wall muscle protein UNC-87 that exhibits seven tandem CLIK-23 repeats (12). A protein with a similar molecular structure has also been described by Irvine et al. (13) in the filar...

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Acidic Calponin Cloned from Neural Cells is Differentially Expressed During Rat Brain Development

Cited by 40 publications

References 28 publications

Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine‐induced seizures

Increased levels of acidic calponin during dendritic spine plasticity after pilocarpine‐induced seizures

Calponin in Non-Muscle Cells

UNC-87 Is an Actin-bundling Protein

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