The effect of neonatal nerve injury on the expression of heat shock proteins in developing rat motoneurones.
The expression of the heat shock proteins hsp27 and hsp70 was examined in the spinal cord and sciatic nerves of developing rats. Using immunohistochemistry, we found that hsp27 is present in many motoneurones at birth. With development, the intensity of staining increases, reaching adult levels by 21 days, when all sciatic motoneurones express hsp27. In the sciatic nerve, hsp27 is strongly expressed throughout postnatal development. In contrast, hsp70 immunoreactivity in motoneurones and the sciatic nerve is weak at birth and does not change with development. The expression of heat shock proteins has been shown to increase in cells under conditions of stress, where they have beneficial effects on cell survival. The effect of neonatal nerve injury on hsp27 and hsp70 expression was also examined in this study. Four days after injury, staining for hsp27 increases in motoneurones, whereas hsp70 does not change. However, there is a significant increase in hsp70 staining in glial cells surrounding the injured motor pool, predominantly in astrocytes. Since neonatal nerve injury induces apoptotic motoneurone death, we also studied the co-expression of hsp27 with markers of apoptosis. No hsp27-positive motoneurones were found to be apoptotic, as assessed by both TUNEL and caspase-3 immunoreactivity. Therefore, it is possible that the upregulation of hsp27 observed in injured motoneurones may play a role in protecting motoneurones from apoptotic cell death following nerve injury.
Kalmár
Bernadett
B
Sobell Department of Neurophysiology, Institute of Neurology, London, United Kingdom.
Burnstock
Geoffrey
G
Vrbová
Gerta
G
Greensmith
Linda
L
D000818:Animals; D000831:Animals, Newborn; D000906:Antibodies; D017209:Apoptosis / Q000502:physiology; D015153:Blotting, Western; D053148:Caspase 3; D020169:Caspases / Q000032:analysis; D005260:Female; D005904:Glial Fibrillary Acidic Protein / Q000032:analysis; D005911:Gliosis / Q000503:physiopathology; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis / Q000276:immunology / Q000502:physiology*; D006360:Heat-Shock Proteins; D007150:Immunohistochemistry; D020287:In Situ Nick-End Labeling; D008297:Male; D009046:Motor Neurons / Q000737:chemistry / Q000166:cytology / Q000502:physiology*; D009363:Neoplasm Proteins / Q000032:analysis / Q000276:immunology / Q000502:physiology; D009409:Nerve Crush; D051381:Rats; D017207:Rats, Sprague-Dawley; D012584:Sciatic Nerve / Q000166:cytology* / Q000254:growth & development / Q000502:physiology; D013116:Spinal Cord / Q000166:cytology* / Q000254:growth & development / Q000502:physiology
D000906:Antibodies; D005904:Glial Fibrillary Acidic Protein; D055551:HSP27 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C486114:Hspb1 protein, rat; D009363:Neoplasm Proteins; C505410:Casp3 protein, rat; D053148:Caspase 3; D020169:Caspases