title: The human spiral ganglion.
abstract: The adult normal human spiral ganglion (SG) was analyzed with regard to ultrastructure and immunohistochemistry. The cytoskeleton of the SG cells was found to comprise F-actin, intermediate filaments (IFs) and microtubules (MTs). The IF subgroups (cytokeratins, Cks; neurofilaments, NFs, vimentin, glial fibrillary acidic proteins, GFAP; desmin) displayed characteristic staining patterns. Ck No. 8 was found in all SG cells, whereas vimentin was lacking. GFAP stained only a small subpopulation of SG cells (type 2?). The light (68 kD) and medium-sized chains of NFs occurred in all SG cells and axons, whereas the 200-kD NF subunit was only found in the axonal hillock of (type 2?) SG cells, but in no other part of the cytoplasm, and regionally in nerve fibres. MAP-1 and MAP-2 occurred in all SG cells but only MAP-1 was found in the nerve fibres. The calcium-binding protein synaptophysin (SY) was expressed only in SG cells, in contrast to the S-100 which occurred more generally in the labyrinth. The neuropeptides VIP and substance P were identified in all SG cells, in contrast to NPY which was expressed in a small subpopulation of SG cell (type 2?). Staining for neuron-specific enolase (NSE) identified most (type 1?) but not all SG cells. The cell surface glycoprotein Thy-1 was expressed in SG cells in a way similar to that described for neurons in the CNS. The SG cells express a high degree of cytoskeletal complexity, allowing one to distinguish between type 1 and type 2 cells. The cell bodies and their adjacent nerve fibres show characteristic features of calcium-binding proteins, surface membrane glycoproteins, NSE and neuropeptides but the basic pattern is still similar to neurons in the CNS.
authors.affiliation: Department of Oto-Rhino-Laryngology and Head and Neck Surgery, Uppsala University Hospital Akademiska sjukhuset, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Anniko
authors.forename: W
authors.initials: W
authors.lastname: Arnold
authors.forename: T
authors.initials: T
authors.lastname: Stigbrand
authors.forename: A
authors.initials: A
authors.lastname: Ström
mesh_terms: D000199:Actins / Q000378:metabolism; D000328:Adult; D001369:Axons / Q000378:metabolism / Q000648:ultrastructure; D003593:Cytoplasm / Q000378:metabolism / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000648:ultrastructure; D003893:Desmin / Q000378:metabolism; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D007381:Intermediate Filament Proteins / Q000378:metabolism; D007382:Intermediate Filaments / Q000648:ultrastructure; D007633:Keratins / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000648:ultrastructure; D009412:Nerve Fibers / Q000378:metabolism / Q000648:ultrastructure; D016900:Neurofilament Proteins / Q000378:metabolism; D009478:Neuropeptide Y / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000378:metabolism; D009418:S100 Proteins / Q000378:metabolism; D013136:Spiral Ganglion / Q000378:metabolism / Q000648:ultrastructure*; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism; D014746:Vimentin / Q000378:metabolism
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D003893:Desmin; D005904:Glial Fibrillary Acidic Protein; D007381:Intermediate Filament Proteins; D008562:Membrane Glycoproteins; D008869:Microtubule-Associated Proteins; D016900:Neurofilament Proteins; D009478:Neuropeptide Y; D009418:S100 Proteins; D014746:Vimentin; D014660:Vasoactive Intestinal Peptide; D007633:Keratins; D010751:Phosphopyruvate Hydratase