Publications by authors named "G Filliatreau"

The product of the RET proto-oncogene is a protein belonging to the receptor-like tyrosine kinase superfamily. RET is expressed in several neural crest-derived cell lineages and has been implicated in the correct development of the peripheral nervous system. To gain further insight into RET function, we investigated the presence of active RET in adult rat tissues.

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Changes in the axonal transport of acetylcholinesterase (AChE) were studied in the painful mononeuropathy induced by setting 4 loose ligatures around the right sciatic nerve of the rat. Since changes in the axonal transport of AChE can be used to assess axonal degeneration/regeneration, we used this marker to investigate whether the time course of pain-related behavioral disorders observed following chronic constriction injury (CCI) to the sciatic nerve are related to the time course of the regeneration of the injured axons. In addition, a comparison was made between changes in AChE observed in this model of nerve injury and those observed after sciatic nerve crush.

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This study evaluated the pain-related behaviours induced by 2 models of peripheral sciatic nerve injuries in the rat: transient nerve crush and chronic constriction injury (CCI). Various lesions of the saphenous nerve were performed in order to investigate the role of saphenous innervation in behavioural disorders induced by these nerve injuries. Behavioural testing included assessment of responses to phasic stimulation (mechanical and thermal) and observation of 'spontaneous' pain-related behaviour.

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Slow axonal transport of peripherin has been studied in the motor axons of both intact and regenerating rat sciatic nerves 7 days post-crush. The studies were done by two-dimensional gel electrophoresis after intraspinal injection of 35S-methionine. In the first experiment, the sciatic nerves were removed 3 weeks after the radiolabeling pulse and cut into 6 mm segments.

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Western blotting of rat dorsal root ganglion (DRG) and sciatic nerve under nonreducing conditions revealed that a peripherin-specific antibody recognized a protein species of 116/130 kDa, pI 5.6, in addition to peripherin (56 kDa, pI 5.6).

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