Literature DB >> 3339416

Anatomical distribution of the growth-associated protein GAP-43/B-50 in the adult rat brain.

L I Benowitz1, P J Apostolides, N Perrone-Bizzozero, S P Finklestein, H Zwiers.   

Abstract

GAP-43 (B-50,F1,pp46) is a neuron-specific phosphoprotein that has been implicated in the development and modulation of synaptic relationships. Although most neurons cease expressing high levels of GAP-43 after the completion of synaptogenesis (Jacobson et al., 1986), certain brain regions continue to have considerable amounts of the protein throughout life (Oestreicher et al., 1986); in at least one such area, the phosphorylation of the protein has been linked with the events that underlie synaptic potentiation (Lovinger et al., 1985). In this study, we used the indirect immunoperoxidase method to map the distribution of GAP-43/B-50 in the brains of 8 adult rats with 2 different antibodies: a monospecific, polyclonal antibody prepared in sheep against the purified protein and an affinity-purified IgG prepared in rabbits. Specific immunoreactivity was found primarily in the neuropil and followed a generally increasing caudal-to-rostral gradient along the neuraxis. Densest staining occurred in layer I of the cortex, the CA1 field of the hippocampus, and in a continuum of subcortical structures that included the caudate-putamen, olfactory tubercle, nucleus accumbens, bed nucleus of the stria terminalis, amygdala, and medial preoptic area-hypothalamus. In the brain stem, staining was seen in the central gray and in ascending visceral relay nuclei, but was essentially absent in areas related to ascending somatosensory information (e.g., the cochlear nuclei or vestibular complex) and motor control (e.g., nucleus ruber or the motor nuclei of the cranial nerves). Staining in dorsal thalamus was likewise modest in most somatosensory and somatomotor relay nuclei, but dark in certain other structures (e.g., mediodorsal nucleus, lateral complex). This distributional pattern raises the question of whether synapses in all areas containing high levels of GAP-43/B-50 are capable of undergoing functional plasticity, or whether the protein may function in some of these areas in some other capacity (e.g., general signal transduction).

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Year:  1988        PMID: 3339416      PMCID: PMC6569357     

Source DB:  PubMed          Journal:  J Neurosci        ISSN: 0270-6474            Impact factor:   6.167


  57 in total

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2.  The RNA-binding protein HuD is required for GAP-43 mRNA stability, GAP-43 gene expression, and PKC-dependent neurite outgrowth in PC12 cells.

Authors:  C D Mobarak; K D Anderson; M Morin; A Beckel-Mitchener; S L Rogers; H Furneaux; P King; N I Perrone-Bizzozero
Journal:  Mol Biol Cell       Date:  2000-09       Impact factor: 4.138

3.  Intracisternal basic fibroblast growth factor enhances functional recovery and up-regulates the expression of a molecular marker of neuronal sprouting following focal cerebral infarction.

Authors:  T Kawamata; W D Dietrich; T Schallert; J E Gotts; R R Cocke; L I Benowitz; S P Finklestein
Journal:  Proc Natl Acad Sci U S A       Date:  1997-07-22       Impact factor: 11.205

4.  Expression of GAP-43 mRNA in the adult mammalian spinal cord under normal conditions and after different types of lesions, with special reference to motoneurons.

Authors:  H Lindå; F Piehl; A Dagerlind; V M Verge; U Arvidsson; S Cullheim; M Risling; B Ulfhake; T Hökfelt
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5.  Switching mature retinal ganglion cells to a robust growth state in vivo: gene expression and synergy with RhoA inactivation.

Authors:  Dietmar Fischer; Victoria Petkova; Solon Thanos; Larry I Benowitz
Journal:  J Neurosci       Date:  2004-10-06       Impact factor: 6.167

6.  Adenoviral vector-mediated expression of B-50/GAP-43 induces alterations in the membrane organization of olfactory axon terminals in vivo.

Authors:  A J Holtmaat; W T Hermens; M A Sonnemans; R J Giger; F W Van Leeuwen; M G Kaplitt; A B Oestreicher; W H Gispen; J Verhaagen
Journal:  J Neurosci       Date:  1997-09-01       Impact factor: 6.167

7.  HuD distribution changes in response to heat shock but not neurotrophic stimulation.

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Review 8.  Molecular analysis of the function of the neuronal growth-associated protein GAP-43 by genetic intervention.

Authors:  R L Neve; K J Ivins; L I Benowitz; M J During; A I Geller
Journal:  Mol Neurobiol       Date:  1991       Impact factor: 5.590

9.  Growth-associated protein 43 is down-regulated in cultured astrocytes.

Authors:  L Vitković; M Mersel
Journal:  Metab Brain Dis       Date:  1989-03       Impact factor: 3.584

Review 10.  Role of the growth-associated protein B-50/GAP-43 in neuronal plasticity.

Authors:  W H Gispen; H B Nielander; P N De Graan; A B Oestreicher; L H Schrama; P Schotman
Journal:  Mol Neurobiol       Date:  1991       Impact factor: 5.590

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