1982
DOI: 10.1016/s0022-5320(82)90049-1
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Stability at low temperatures of neuronal microtubules in spinal ganglia and dorsal roots of the lizard (Lacerta muralis)

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Cited by 16 publications
(5 citation statements)
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“…There is wealth of information for many other contemporary lines of investigation, such as detailed descriptions of MT behaviors during axon branching , of the ultrastructure of growth cones, dendrites, and synapses (Peters et al, 1991), or of curious phenomena such as impressive packages of ER-derived tubular structures found in certain axons (Andres, 1965b;Peters et al, 1991). Axonal MTs of species as diverse as cockroach, lamprey, frog, toad, chick, mouse, and rats were reported to contain luminal material in form of a ∼4-nm-thick central dot or filament (Andres, 1965a;Burton, 1984Burton, , 1987Gonatas and Robbins, 1965;Lane and Treherne, 1970;Nixon et al, 1994;Rodríguez Echandía et al, 1968;Smith et al, 1970Smith et al, , 1975Wuerker and Palay, 1969), matching recent reports of MTs with incorporated actin filaments or MAP6/stable tubule-only peptide (Cuveillier et al, 2020;Paul et al, 2019 Preprint), of which the latter could help to explain long-term cold resistance of axonal MTs observed in vivo (Delphin et al, 2012;Pannese et al, 1982; but see also Song et al, 2013). Furthermore, classical studies revealed the presence of post-translationally modified subdomains in MT lattices (Baas and Ahmad, 1992;Baas and Black, 1990;Baas and Joshi, 1992), which start finding their explanations in current models of MT stability (Baas et al, 2016).…”
Section: Conclusion and Final Remarkssupporting
confidence: 66%
“…There is wealth of information for many other contemporary lines of investigation, such as detailed descriptions of MT behaviors during axon branching , of the ultrastructure of growth cones, dendrites, and synapses (Peters et al, 1991), or of curious phenomena such as impressive packages of ER-derived tubular structures found in certain axons (Andres, 1965b;Peters et al, 1991). Axonal MTs of species as diverse as cockroach, lamprey, frog, toad, chick, mouse, and rats were reported to contain luminal material in form of a ∼4-nm-thick central dot or filament (Andres, 1965a;Burton, 1984Burton, , 1987Gonatas and Robbins, 1965;Lane and Treherne, 1970;Nixon et al, 1994;Rodríguez Echandía et al, 1968;Smith et al, 1970Smith et al, , 1975Wuerker and Palay, 1969), matching recent reports of MTs with incorporated actin filaments or MAP6/stable tubule-only peptide (Cuveillier et al, 2020;Paul et al, 2019 Preprint), of which the latter could help to explain long-term cold resistance of axonal MTs observed in vivo (Delphin et al, 2012;Pannese et al, 1982; but see also Song et al, 2013). Furthermore, classical studies revealed the presence of post-translationally modified subdomains in MT lattices (Baas and Ahmad, 1992;Baas and Black, 1990;Baas and Joshi, 1992), which start finding their explanations in current models of MT stability (Baas et al, 2016).…”
Section: Conclusion and Final Remarkssupporting
confidence: 66%
“…At this point it must be noted that, in contrast t o the results presented here, other studies have claimed that axonal MT appear to be stable to cold (Pannese et al, 1982;Lewis and Burton, 1977). On the other hand, there are reports in agreement with the present report indicating that MT in peripheral nerves are affected by cold (Rodriguez-Echandia and Piezzi, 1968;Banks et al, 1975;Brimijoin et al, 1979).…”
Section: Discussioncontrasting
confidence: 88%
“…On the other hand, frog bladder microtubules are resistant to cold: frogs maintained at 4°C for 15 d exhibit, in their bladder granular cells, the same extended network as at 20°C; however, if an isolated bladder, from room temperature-adapted frogs, is refrigerated at 4°C for 4 h, only a few fluorescent fragments of microtubules can be observed, an aspect highly reminiscent of the action of the depolymerizing drugs (unpublished observations). This cold adaptation has also been observed in fish and lizards [21]. It appears in relation to a biochemical modification of the microtubular structure by a proteic or peptidic stabilizing factor [13] or by a special alphatubulin [7].…”
Section: Microtubular Networkmentioning
confidence: 60%