TY - JOUR
T1 - Heat shock protein 27
T2 - Developmental regulation and expression after peripheral nerve injury
AU - Costigan, Michael
AU - Mannion, Richard J.
AU - Kendall, Giles
AU - Lewis, Susan E.
AU - Campagna, Jason A.
AU - Coggeshall, Richard E.
AU - Meridith-Middleton, Jacqueta
AU - Tate, Simon
AU - Woolf, Clifford J.
PY - 1998/8/1
Y1 - 1998/8/1
N2 - The heat shock protein (HSP) 27 is constitutively expressed at low levels in medium-sized lumbar dorsal root ganglion (DRG) cells in adult rats. Transection of the sciatic nerve results in a nine/old upregulation of HSP27 mRNA and protein in axotomized neurons in the/psilateral DRG at 48 hr, without equivalent changes n the mRNAs encoding HSP56, HSP60, HSP70, and HSP90. Dorsal rhizotomy, injuring the central axon of the DRG neuron, does not upregulate HSP27 mRNA levels. After peripheral axotomy, HSP27 mRNA and protein are present in small, medium, and large DRG neurons, and HSP27 protein is transported anterogradely, accumulating in the dorsal horn and dorsal columns of the spinal cord, where it persists for several months. Axotomized motor neurons also upregulate HSP27. Only a minority of cultured adult DRG neurons are HSP27-immunoreactive soon after dissociation, but all express HSP27 after 24 hr in culture with prominent label throughout the neuron, including the growth cone. HSP27 differs from most axonal injury- regulated and growth-associated genes, which are typically present at high levels in early development and down-regulated on innerration of their targets, in that its mRNA is first detectable in the DRG late in development and only approaches adult levels by postnatal day 21. In non-neuronal cells, HSP27 has been shown to be involved both in actin filament dynamics and in protection against necrotic and apoptotic cell death. Therefore, its upregulation after adult peripheral nerve injury may both promote survival of the injured neurons and contribute to alterations in the cytoskeleton associated with axonal growth.
AB - The heat shock protein (HSP) 27 is constitutively expressed at low levels in medium-sized lumbar dorsal root ganglion (DRG) cells in adult rats. Transection of the sciatic nerve results in a nine/old upregulation of HSP27 mRNA and protein in axotomized neurons in the/psilateral DRG at 48 hr, without equivalent changes n the mRNAs encoding HSP56, HSP60, HSP70, and HSP90. Dorsal rhizotomy, injuring the central axon of the DRG neuron, does not upregulate HSP27 mRNA levels. After peripheral axotomy, HSP27 mRNA and protein are present in small, medium, and large DRG neurons, and HSP27 protein is transported anterogradely, accumulating in the dorsal horn and dorsal columns of the spinal cord, where it persists for several months. Axotomized motor neurons also upregulate HSP27. Only a minority of cultured adult DRG neurons are HSP27-immunoreactive soon after dissociation, but all express HSP27 after 24 hr in culture with prominent label throughout the neuron, including the growth cone. HSP27 differs from most axonal injury- regulated and growth-associated genes, which are typically present at high levels in early development and down-regulated on innerration of their targets, in that its mRNA is first detectable in the DRG late in development and only approaches adult levels by postnatal day 21. In non-neuronal cells, HSP27 has been shown to be involved both in actin filament dynamics and in protection against necrotic and apoptotic cell death. Therefore, its upregulation after adult peripheral nerve injury may both promote survival of the injured neurons and contribute to alterations in the cytoskeleton associated with axonal growth.
KW - Apoptosis
KW - Axotomy
KW - Differential gene expression
KW - Dorsal root ganglion
KW - Regeneration
KW - Spinal cord
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U2 - 10.1523/jneurosci.18-15-05891.1998
DO - 10.1523/jneurosci.18-15-05891.1998
M3 - Article
C2 - 9671676
AN - SCOPUS:0032146734
SN - 0270-6474
VL - 18
SP - 5891
EP - 5900
JO - Journal of Neuroscience
JF - Journal of Neuroscience
IS - 15
ER -