Characterization of microwell cultures of dissociated brain tissue for studies of cell-cell interactions

Maar, Thomas E.; Rønn, Lars Christian B.; Bock, Elisabeth; Berezin, Vladimir; Morán, Julio; Pasantes‐Morales, Herminia; Schousboe, Arne

doi:10.1002/(sici)1097-4547(19970115)47:2<163::aid-jnr5>3.0.co;2-d

Cited by 38 publications

(33 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…26,2006 S100A4 INCREASES Ca 2ϩ VIA PLC AND HEPARAN SULFATE 3629 S100A12 and S100A4 interacted with the same or significantly overlapping regions of RAGE and that "saturation" of immobilized RAGE by S100A12 decreased the number of binding sites available for subsequent interaction with S100A4. Oligomeric but not dimeric S100A4 induces a rise of [Ca 2؉ ] i involving voltage-dependent Ca 2؉ channels (VDCC) and affects intracellular Ca 2؉ stores.…”

Section: Resultssupporting

confidence: 93%

See 1 more Smart Citation

Molecular Mechanisms of Ca²⁺ Signaling in Neurons Induced by the S100A4 Protein

Kiryushko¹,

Novitskaya²,

Soroka³

et al. 2006

Molecular and Cellular Biology

Self Cite

126

123

View full text Add to dashboard Cite

The S100A4 protein belongs to the S100 family of vertebrate-specific proteins possessing both intra-and extracellular functions. In the nervous system, high levels of S100A4 expression are observed at sites of neurogenesis and lesions, suggesting a role of the protein in neuronal plasticity. Extracellular oligomeric S100A4 is a potent promoter of neurite outgrowth and survival from cultured primary neurons; however, the molecular mechanism of this effect has not been established. Here we demonstrate that oligomeric S100A4 increases the intracellular calcium concentration in primary neurons. We present evidence that both S100A4-induced Ca 2؉ signaling and neurite extension require activation of a cascade including a heterotrimeric G protein(s), phosphoinositide-specific phospholipase C, and diacylglycerol-lipase, resulting in Ca 2؉ entry via nonselective cation channels and via T-and L-type voltage-gated Ca 2؉ channels. We demonstrate that S100A4-induced neurite outgrowth is not mediated by the receptor for advanced glycation end products, a known target for other extracellular S100 proteins. However, S100A4-induced signaling depends on interactions with heparan sulfate proteoglycans at the cell surface. Thus, glycosaminoglycans may act as coreceptors of S100 proteins in neurons. This may provide a mechanism by which S100 proteins could locally regulate neuronal plasticity in connection with brain lesions and neurological disorders.The S100 family is a group of vertebrate-specific Ca 2ϩ -binding proteins with a highly conserved primary structure possessing both intra-and extracellular functions. Most S100 family members, including S100A4, are antiparallelly packed homodimers stabilized by disulfide bridges (reviewed in references 8 and 9). Intracellularly, S100 proteins are involved in a variety of processes, including the regulation of cytoskeletal dynamics, Ca 2ϩ homeostasis, and cell proliferation and differentiation. Importantly, some S100 proteins can also be secreted, form oligomers owing to the nonreducing conditions of the environment, and exert their effects acting at the cell surface (10; 43; reviewed in reference 20). A plasma membrane target for S100B and S100A12, the receptor for advanced glycation end products (RAGE), has been identified on inflammatory and neural cells (14). However, RAGE is probably not the sole receptor for members of the S100 family, since the effects of extracellular S100A12 and S100B proteins can be observed in cells lacking RAGE (32), and some of these effects are RAGE independent in cells expressing the receptor (37).The S100A4 (also termed Mts1) gene was isolated from tumor cells (11,40), where its expression increased the ability of the tumor to metastasize. S100A4 has also been detected in healthy tissues, particularly in the nervous system. In both the brain and spinal cord, S100A4 expression appears in astrocytes shortly after the start of myelination, with the highest level observed in the areas in which neurogenesis takes place and in regions possessing high plasticit...

show abstract

Section: Resultssupporting

confidence: 93%

“…Hippocampal and cerebellar neurons were prepared from E19 rat embryos and P3 rat pups as previously described (26,29,38). Cultures were seeded at a density of 10,000 cells/cm 2 in eight-well LabTek tissue culture chambers with a growth surface of Permanox plastic (Nunc, Roskilde, Denmark) and maintained in Neurobasal medium.…”

Section: Methodsmentioning

confidence: 99%

Molecular Mechanisms of Ca²⁺ Signaling in Neurons Induced by the S100A4 Protein

Kiryushko¹,

Novitskaya²,

Soroka³

et al. 2006

Molecular and Cellular Biology

Self Cite

126

123

View full text Add to dashboard Cite

show abstract

“…Hippocampal neurons were prepared from embryonic day 19 rat embryos as described previously (Maar et al, 1997). Neurons were plated at a density of 50,000 cells/cm 2 in eight-well LabTek tissue culture chambers (Nunc, Roskilde, Denmark) coated with poly-L-lysine.…”

Section: Methodsmentioning

confidence: 99%

A Synthetic Neural Cell Adhesion Molecule Mimetic Peptide Promotes Synaptogenesis, Enhances Presynaptic Function, and Facilitates Memory Consolidation

Cambon¹,

Hansen²,

Venero³

et al. 2004

J. Neurosci.

157

129

View full text Add to dashboard Cite

The neural cell adhesion molecule (NCAM) plays a critical role in development and plasticity of the nervous system and is involved in the mechanisms of learning and memory. Here, we show that intracerebroventricular administration of the FG loop (FGL), a synthetic 15 amino acid peptide corresponding to the binding site of NCAM for the fibroblast growth factor receptor 1 (FGFR1), immediately after training rats in fear conditioning or water maze learning, induced a long-lasting improvement of memory. In primary cultures of hippocampal neurons, FGL enhanced the presynaptic function through activation of FGFR1 and promoted synapse formation. These results provide the first evidence for a memory-facilitating effect resulting from a treatment that mimics NCAM function. They suggest that increased efficacy of synaptic transmission and formation of new synapses probably mediate the cognition-enhancing properties displayed by the peptide.

show abstract

“…This observation is consistent with earlier reports (Maar et al, 1997;Segev et al, 2003) that cells dissociated from rat cortices would form clusterized networks, consisting of large cell aggregates interconnected to each other by thick neurite bundles, when plated at high cell densities on the SiN surface of glass or in microwells.…”

Section: 2mentioning

confidence: 99%