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Changes in Organization and Axonal Transport of Cytoskeletal Proteins During Regeneration
Author(s) -
Tashiro Tomoko,
Komiya Yoshiaki
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb02051.x
Subject(s) - cytoskeleton , tubulin , neurofilament , axoplasmic transport , regeneration (biology) , actin , sciatic nerve , chemistry , microbiology and biotechnology , microtubule , biochemistry , biology , anatomy , cell , immunohistochemistry , immunology
Abstract: Changes in solubility and transport rate of cyto‐skeletal proteins during regeneration were studied in the motor fibers of the rat sciatic nerve. Nerves were injured by freezing at the midthigh level either 1–2 weeks before (experiment I) or 1 week after radioactive labeling of the spinal cord with l ‐[ 35 S]methionine (experiment II). Labeled proteins in 6‐mm consecutive segments of the nerve 2 weeks after labeling were analyzed following fractionation into soluble and insoluble populations with 1° Triton at 4°C. When ax‐onal transport of newly synthesized cytoskeleton was examined in the regenerating nerve in experiment I, a new faster component enriched in soluble tubulin and actin was observed that was not present in the control nerve. The rate of the slower main component containing most of the insoluble tubulin and actin together with neurofilament proteins was not affected. A smaller but significant peak of radioactivity enriched in soluble tubulin and actin was also detected ahead of the main peak when the response of the preexisting cytoskeleton was examined in experiment II. It is thus concluded that during regeneration changes in the organization take place in both the newly synthesized and the preexisting axonal cytoskeleton, resulting in a selective acceleration in rate of transport of soluble tubulin and actin.