By Phillip R. Gordon-Weeks
In Neuronal progress Cones, Phillip Gordon-Weeks explores the molecular biology of the habit of progress cones, conical-like endings of the turning out to be axon. He covers the fundamental morphology and behaviour of progress cones, motility and neurite extension through the expansion cone cytoskeleton, pathfinding, intracellular signaling, and synaptogenesis. a close, serious research of all elements of progress cone biology, this incisive reference is a necessary paintings for complicated graduate scholars, postgraduates, and researchers in mobile and molecular neuroscience, developmental biology, and anatomy.
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1985; see also Fig. 6 in Bunge, 1973), and in growth cones of the rat pyramidal tract (Gorgels, 1991). The sheet-like nature of this form of smooth endoplasmic reticulum has been confirmed by serial section analysis of growth cones isolated as a subcellular fraction from postnatal rat forebrain (Gordon-Weeks & Lockerbie, 1984) and, in freeze-substituted growth cones in chick tectum (Cheng & Reese, 1985, 1987). Unlike the branching form of smooth endoplasmic reticulum, the sheet-like form has a translucent lumen which appears to be partially lost after freeze-substitution by artefactual apposition of the adjacent membrane; only at the rim of the cisternae, does the lumen remain patent, possibly because of the greater curvature of the membrane here (Gordon-Weeks, 1988a).
They showed that newly synthesised tubulin remains soluble for up to 10 minutes following a pulse-chase with unlabelled methionine, whereas by 120 minutes it is mainly associated with the detergent-insoluble fraction (presumably microtubules). This result might be taken to imply that tubulin is assembled into microtubules near its site of synthesis, the cell body, since, if tubulin was moving along the axon solely by slow axoplasmic transport, it would only have travelled a maximum distance of about 80 /xm.
These post-translational modifications are unique to tubulin. Most, if not all, of the soluble a-tubulin in cells is C-terminally tyrosinated whereas polymerised tubulin contains both forms of of-tubulin. , 1987). This phenomenon produces microtubules with variations in a-tubulin isoforms along their length. There is a correlation between microtubule populations that are relatively stable to depolymerisation by cold shock and microtubule depolymerising agents, such as nocodazole, and acetylation and detyrosination on the one hand, and labile microtubules and tyrosination on the other (Kreis, 1986; Khawaja, Gundersen & Bulinski, 1988).
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