title: Biochemical basis of microtubule cold stability in the peripheral and central nervous systems.
abstract: Cold-stable, cold-labile and unpolymerized tubulins extracted from thalamic nuclei (soma-enriched fraction) and various nerves (both central and peripheral: axon-enriched fractions) appear different when analyzed by high-resolution isoelectric focusing. Cold-labile tubulin appears identical to unpolymerized tubulin. The axonal fractions contain fewer tubulin isotypes than the soma-enriched fraction; the peripheral axonal fraction has fewer isotypes than the central fraction. Cold-stable tubulin exhibits a specific pattern characterized by the abundance of two isotypes of alpha-tubulin, 7 and 8, and one beta-tubulin, isotype 9, with slightly different patterns of the axon-enriched fractions from the central and peripheral nervous systems. Our results suggest that the cold stability of microtubules is based on biochemical properties of tubulin, and confirm the domain specificity of the heterogeneity of tubulin.
authors.affiliation: Laboratoire d'Anatomie, UER Biomédicales des St-Pères, Paris, France.
authors.forename: S
authors.initials: S
authors.lastname: Binet
authors.forename: V
authors.initials: V
authors.lastname: Meininger
mesh_terms: D000818:Animals; D002490:Central Nervous System / Q000378:metabolism*; D003080:Cold Temperature; D007525:Isoelectric Focusing; D051379:Mice; D008870:Microtubules / Q000378:metabolism*; D008970:Molecular Weight; D010525:Peripheral Nerves / Q000378:metabolism*; D014021:Tissue Preservation