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We are analyzing https://link.springer.com/article/10.1186/1471-2202-6-24.

Title:
Hsp27 and axonal growth in adult sensory neurons in vitro | BMC Neuroscience
Description:
Background Neurite growth can be elicited by growth factors and interactions with extracellular matrix molecules like laminin. Among the targets of the signalling pathways activated by these stimuli are cytoskeletal elements, such as actin, tubulin and neurofilaments. The cytoskeleton can also be modulated by other proteins, such as the small heat shock protein Hsp27. Hsp27 interacts with actin and tubulin in non-neuronal cells and while it has been suggested to play a role in the response of some neurons to injury, there have been no direct studies of its contribution to axonal regeneration. Results We have investigated neurite initiation and process extension using cultures of adult dorsal root ganglion (DRG) sensory neurons and a laminin stimulation paradigm. Employing confocal microscopy and biochemical analyses we have examined localization of Hsp27 at early and later stages of neurite growth. Our results show that Hsp27 is colocalized with actin and tubulin in lamellopodia, filopodia, focal contacts and mature neurites and growth cones. Disruption of the actin cytoskeleton with cytochalasin D results in aberrant neurite initiation and extension, effects which may be attributable to alterations in actin polymerization states. Inhibition of Hsp27 phosphorylation in our cultures results in an atypical growth pattern that may be attributable to an effect of pHsp27 on the stability of the actin cytoskeleton. Conclusion We observed colocalization of the phosphorylated and non-phosphorylated forms of Hsp27 with actin and tubulin in both very early and later stages of neurite growth from cultured adult DRG neurons. The colocalization of Hsp27 and pHsp27 with actin in lamellopodia and focal contacts at early stages of neurite growth, and in processes, branch points and growth cones at later stages, suggests that Hsp27 may play a role in neuritogenesis and subsequent neurite extension, and potentially in the patterning of this growth. Hsp27 has been reported to play a key role in modulating actin cytoskeletal dynamics as an actin-capping protein in non-neuronal cells. Our results suggest that this may also be the case in neurons and support a role for Hsp27 in neurite outgrowth via its phosphorylation state-dependent interactions with actin.
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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {πŸ”}

hsp, growth, actin, neurons, neurite, google, scholar, cas, article, tubulin, pubmed, protein, phsp, cells, phosphorylation, cell, figure, role, heat, hrs, shock, cones, laminin, cytoskeleton, stages, initiation, small, cytoskeletal, processes, colocalization, kinase, results, mapk, images, arrowheads, process, extension, early, show, neurites, observed, plated, arrows, phosphorylated, reported, arrow, red, drg, lamellopodia, formation,

Topics {βœ’οΈ}

axonal charcot-marie-tooth disease map-kinase-activated protein-kinase 2/3 article download pdf cgmp-dependent protein kinase heat-shock protein-25/27 phosphorylation cy5-tagged secondary antibodies phosphorylation state-dependent interactions actin polymerization-inhibiting activity cell-free assay systems 45-kda/54-kda hsp27 kinase serum-free neurobasal medium growth cone induced modified serum-free nb phosphorylation-sensitive intermolecular interactions mitogen-activated kinases heat shock proteins p38 map kinase heat-shock protein 27 heat-shock protein growth cone dynamics inhibiting p38 mapk hsp27 phosphorylation-mediated resistance cgmp-dependent kinase authors’ original file stress-mediated signaling phosphorylation-dependent protective function privacy choices/manage cookies camp-dependent kinase signalling pathways activated full size image prog brain res stimulates mapkap kinase-2 bca protein assay stress-sensitive kinase p38 mapk activity distal motor neuropathy plasma membrane proteins kinase cascade triggered stimulate axon growth smooth muscle contraction phosphorylation-dependent manner [41 serum-induced phosphorylation full access p38 mapk activation da silva js human fetal brain cell free assays s6 kinase ii aberrant neurite growth author information authors

Questions {❓}

  • Dehmelt L, Halpain S: Actin and microtubules in neurite initiation: are MAPs the missing link?
  • Mounier N, Arrigo AP: Actin cytoskeleton and small heat shock proteins: how do they interact?

Schema {πŸ—ΊοΈ}

WebPage:
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         description:Neurite growth can be elicited by growth factors and interactions with extracellular matrix molecules like laminin. Among the targets of the signalling pathways activated by these stimuli are cytoskeletal elements, such as actin, tubulin and neurofilaments. The cytoskeleton can also be modulated by other proteins, such as the small heat shock protein Hsp27. Hsp27 interacts with actin and tubulin in non-neuronal cells and while it has been suggested to play a role in the response of some neurons to injury, there have been no direct studies of its contribution to axonal regeneration. We have investigated neurite initiation and process extension using cultures of adult dorsal root ganglion (DRG) sensory neurons and a laminin stimulation paradigm. Employing confocal microscopy and biochemical analyses we have examined localization of Hsp27 at early and later stages of neurite growth. Our results show that Hsp27 is colocalized with actin and tubulin in lamellopodia, filopodia, focal contacts and mature neurites and growth cones. Disruption of the actin cytoskeleton with cytochalasin D results in aberrant neurite initiation and extension, effects which may be attributable to alterations in actin polymerization states. Inhibition of Hsp27 phosphorylation in our cultures results in an atypical growth pattern that may be attributable to an effect of pHsp27 on the stability of the actin cytoskeleton. We observed colocalization of the phosphorylated and non-phosphorylated forms of Hsp27 with actin and tubulin in both very early and later stages of neurite growth from cultured adult DRG neurons. The colocalization of Hsp27 and pHsp27 with actin in lamellopodia and focal contacts at early stages of neurite growth, and in processes, branch points and growth cones at later stages, suggests that Hsp27 may play a role in neuritogenesis and subsequent neurite extension, and potentially in the patterning of this growth. Hsp27 has been reported to play a key role in modulating actin cytoskeletal dynamics as an actin-capping protein in non-neuronal cells. Our results suggest that this may also be the case in neurons and support a role for Hsp27 in neurite outgrowth via its phosphorylation state-dependent interactions with actin.
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      headline:Hsp27 and axonal growth in adult sensory neurons in vitro
      description:Neurite growth can be elicited by growth factors and interactions with extracellular matrix molecules like laminin. Among the targets of the signalling pathways activated by these stimuli are cytoskeletal elements, such as actin, tubulin and neurofilaments. The cytoskeleton can also be modulated by other proteins, such as the small heat shock protein Hsp27. Hsp27 interacts with actin and tubulin in non-neuronal cells and while it has been suggested to play a role in the response of some neurons to injury, there have been no direct studies of its contribution to axonal regeneration. We have investigated neurite initiation and process extension using cultures of adult dorsal root ganglion (DRG) sensory neurons and a laminin stimulation paradigm. Employing confocal microscopy and biochemical analyses we have examined localization of Hsp27 at early and later stages of neurite growth. Our results show that Hsp27 is colocalized with actin and tubulin in lamellopodia, filopodia, focal contacts and mature neurites and growth cones. Disruption of the actin cytoskeleton with cytochalasin D results in aberrant neurite initiation and extension, effects which may be attributable to alterations in actin polymerization states. Inhibition of Hsp27 phosphorylation in our cultures results in an atypical growth pattern that may be attributable to an effect of pHsp27 on the stability of the actin cytoskeleton. We observed colocalization of the phosphorylated and non-phosphorylated forms of Hsp27 with actin and tubulin in both very early and later stages of neurite growth from cultured adult DRG neurons. The colocalization of Hsp27 and pHsp27 with actin in lamellopodia and focal contacts at early stages of neurite growth, and in processes, branch points and growth cones at later stages, suggests that Hsp27 may play a role in neuritogenesis and subsequent neurite extension, and potentially in the patterning of this growth. Hsp27 has been reported to play a key role in modulating actin cytoskeletal dynamics as an actin-capping protein in non-neuronal cells. Our results suggest that this may also be the case in neurons and support a role for Hsp27 in neurite outgrowth via its phosphorylation state-dependent interactions with actin.
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         Animal Models
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      name:Division of Basic Medical Sciences, Memorial University of Newfoundland, St. John's, Canada
      name:Division of Basic Medical Sciences, Memorial University of Newfoundland, St. John's, Canada

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