title: Molecular organization of the nodal region is not altered in spontaneously diabetic BB-Wistar rats.
abstract: We examined the organization of the molecular components of the nodal region in spontaneously diabetic BB-Wistar rats. Frozen sections and teased fibers from the sciatic nerves were immunostained for nodal (voltage-gated Na(+) channels, ankyrin(G), and ezrin), paranodal (contactin, Caspr, and neurofascin 155 kDa), and juxtaparanodal (Caspr2, the Shaker-type K(+) channels Kv1.1 and Kv1.2, and their associated subunit Kvbeta2) proteins. All of these proteins were properly localized in myelinated fibers from rats that had been diabetic for 15-44 days, compared to age-matched, nondiabetic animals. These results demonstrate that the axonal membrane is not reorganized, so nodal reorganization is not likely to be the cause of nerve conduction slowing in this animal model of acute diabetes.
authors: Department of Neurology, The University of Pennsylvania Medical Center, Philadelphia 19104, USA.
authors: A A
authors: AA
authors: Brown
authors: T
authors: T
authors: Xu
authors: E J
authors: EJ
authors: Arroyo
authors: S R
authors: SR
authors: Levinson
authors: P J
authors: PJ
authors: Brophy
authors: E
authors: E
authors: Peles
authors: S S
authors: SS
authors: Scherer
mesh_terms: D000818:Animals; D017487:Ankyrins / Q000378:metabolism; D001369:Axons / Q000378:metabolism* / Q000473:pathology; D015815:Cell Adhesion Molecules / Q000378:metabolism; D015816:Cell Adhesion Molecules, Neuronal / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism* / Q000473:pathology; D058966:Contactins; D003598:Cytoskeletal Proteins; D003929:Diabetic Neuropathies / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D007150:Immunohistochemistry; D051662:Kv1.1 Potassium Channel; D051663:Kv1.2 Potassium Channel; D008565:Membrane Proteins; D009414:Nerve Growth Factors / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D015221:Potassium Channels / Q000378:metabolism; D024642:Potassium Channels, Voltage-Gated; D011901:Ranvier's Nodes / Q000378:metabolism* / Q000473:pathology / Q000648:ultrastructure; D051381:Rats; D011913:Rats, Inbred BB / Q000033:anatomy & histology / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D012584:Sciatic Nerve / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D000099149:Ezrin
chemical_list: D017487:Ankyrins; D015815:Cell Adhesion Molecules; D015816:Cell Adhesion Molecules, Neuronal; D058966:Contactins; D003598:Cytoskeletal Proteins; D051662:Kv1.1 Potassium Channel; D051663:Kv1.2 Potassium Channel; D008565:Membrane Proteins; D009414:Nerve Growth Factors; D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D011956:Receptors, Cell Surface; D000099149:Ezrin; C491323:CNTNAP1 protein, human; C403049:CNTNAP2 protein, human; C105177:Cntnap1 protein, rat; C496972:Kcna2 protein, rat; C426239:Kcnab2 protein, rat; C504594:Nfasc protein, rat