title: Changes in rapidly transported proteins associated with development of abnormal projections in the diencephalon.
abstract: The development of the hamster visual system is accompanied by striking changes in the pattern of proteins that are synthesized in retinal ganglion cells and rapidly transported to their nerve terminals. To determine whether any of these protein changes are regulated by interactions between the developing nerve endings and the cells with which they form synapses, we induced retinofugal axons to form abnormal projections in the lateral posterior (LP) nucleus of the thalamus and dense patches of hyperinnervation in the lateral geniculate nucleus (LGN) by removing their principal target, the superior colliculus (SC), the day after birth. Under these experimental conditions, two rapidly transported proteins, including the neural cell adhesion molecule, NCAM, showed significant changes in their time course of expression. NCAM, identified here using a monospecific antibody, is normally synthesized and transported at high levels at early stages of development and then declines during the second and third postnatal weeks. However, this decline was delayed when optic fibers were re-routed. A second rapidly transported protein, M(r) = 67 kDa, pI = 4.7, normally shows a rise in its synthesis and transport during terminal arbor formation and a subsequent decline, but it also remained elevated for a prolonged period when the SC was absent. These findings cannot be accounted for by a simple delay in the retinal ganglion cells' program of axonal growth, since other rapidly transported proteins, including the growth-associated protein GAP-43, showed a normal developmental time-course when the SC was removed. Target interactions therefore appear to influence the retinal ganglion cells' expression of different proteins in a specific fashion.
authors.affiliation: Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge.
authors.forename: K L
authors.initials: KL
authors.lastname: Moya
authors.forename: L I
authors.initials: LI
authors.lastname: Benowitz
authors.forename: B A
authors.initials: BA
authors.lastname: Sabel
authors.forename: G E
authors.initials: GE
authors.lastname: Schneider
mesh_terms: D000375:Aging / Q000502:physiology*; D000818:Animals; D001345:Autoradiography; D001370:Axonal Transport; D001369:Axons / Q000502:physiology; D015153:Blotting, Western; D001930:Brain Injuries / Q000503:physiopathology; D015816:Cell Adhesion Molecules, Neuronal / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D006224:Cricetinae; D004027:Diencephalon / Q000033:anatomy & histology* / Q000254:growth & development; D019922:GAP-43 Protein; D005829:Geniculate Bodies / Q000502:physiology; D006735:Horseradish Peroxidase; D008562:Membrane Glycoproteins / Q000302:isolation & purification / Q000378:metabolism; D008647:Mesocricetus; D008715:Methionine / Q000378:metabolism; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D012160:Retina / Q000254:growth & development*; D012165:Retinal Ganglion Cells / Q000502:physiology*; D013462:Sulfur Radioisotopes; D013477:Superior Colliculi / Q000502:physiology*; D013788:Thalamus / Q000502:physiology
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D019922:GAP-43 Protein; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D013462:Sulfur Radioisotopes; D008715:Methionine; D006735:Horseradish Peroxidase