A light and electron microscopical study of B-50 (GAP-43) in human intramuscular nerve and neuromuscular junctions during development

Hesselmans, L.F.G.M.; Jennekens, F.G.I.; Oord, C.J.M. van den; Oestreicher, A.B.; Veldman, H.; Gispen, Willem Hendrik

doi:10.1016/0022-510x(89)90031-2

Cited by 19 publications

(11 citation statements)

References 31 publications

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“…These authors reported that a decrease in the number of B-50-positive end plates is observed with the age of the individuals, indicating that also in human peripheral nervous system the B-50 expression is developmentally regulated. In corroboration of the findings of Hesselmans et al (1989), we show that the NM4 Mabs detect very well outgrowing axons in developing peripheral human nervous tissue.…”

Section: Discussionsupporting

confidence: 89%

“…This suggestion is supported by recent observations of Masliah et al ( 199 1 ) . Hesselmans et al (1989), using a polyclonal rabbit antibody to B-50, showed by light and electron immunomicroscopy that B-50 is present in intramuscular nerve fibers and at motor end plates of human muscle biopsies. These authors reported that a decrease in the number of B-50-positive end plates is observed with the age of the individuals, indicating that also in human peripheral nervous system the B-50 expression is developmentally regulated.…”

Section: Discussionmentioning

confidence: 99%

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Immunocytochemical detection of the growth‐associated protein B‐50 by newly characterized monoclonal antibodies in human brain and muscle

et al. 1992

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The growth-associated protein B-50 also termed GAP-43, F1, pp46, P-57 and neuromodulin is a nervous tissue-specific protein kinase C (PKC) substrate that is considered to play a major role in neurite formation, regeneration, and neuroplasticity. We describe the isolation of seven mouse monoclonal antibodies (Mabs) directed against B-50. The Mabs are produced against the bovine B-50, selected by ELISA for cross-reactivity with its human counterpart, and evaluated on Western blots in comparison with the well-characterized affinity-purified rabbit polyclonal antibodies to rat-B-50. The Western blots show that the Mabs NM1, NM4, and NM6 recognize specifically the B-50 of bovine, human, and rat brain extract and the purified PKC phosphorylated and unphosphorylated rat B-50 isoforms. The Mabs NM2 and NM3 cross-react with bovine B-50 immunoreactive c-kinase substrate (BICKS), a protein sharing a 17 amino acid sequence homology with B-50. Two Mabs are useful for the detection of B-50 immunoreactivity in formalin-fixed human and rat brain tissues. In human specimen of the hippocampus, a characteristic neuropil distribution of B-50 is detected by the Mabs. In human muscle, Mabs reveal B-50 in nerve bundles and in axons at motor end plates. Thus, these Mabs are useful in investigating the function and localization of the B-50 protein.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Immunocytochemical detection of the growth‐associated protein B‐50 by newly characterized monoclonal antibodies in human brain and muscle

et al. 1992

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“…Looking at previous literature concerning expression of B-50 in muscle tissue, it seems that our findings contrast with the results of Hesselmans et al in 1989 [13]. In developing muscle they found B-50 in human intramuscular nerves and neuromuscular junctions, but not in myocytes.…”

Section: Discussioncontrasting

confidence: 99%

Light-microscopic study of phosphoprotein B-50 in myopathies

Heuss

Engelhardt

Göbel

et al. 1995

Vichows Archiv A Pathol Anat

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The growth-associated protein B-50, also termed GAP-43, is a membrane-bound phosphoprotein that is expressed in neurons. It is particularly abundant during periods of axonal outgrowth in development and regeneration of the central and peripheral nervous system. In this paper we study the expression of B-50 in inflammatory and dystrophic myopathies. To investigate the state of regeneration, N-CAM and vimentin serial sections were performed, because N-CAM and cytoskeletal protein vimentin are excellent markers for regenerating muscle. Light-microscopic evaluation showed that muscle fiber regeneration in myopathies corresponds closely to B-50 immunoreactivity in satellite cells, myoblasts, myotubes and small regenerating myocytes in cytoplasmatic distribution. In normal muscle and in biopsies of neurogenic muscular atrophy, however, no light-microscopically demonstrable B-50 staining was found. B-50 in muscles apparently plays a role in the growth morphology of regenerating myocytes, and the phosphoprotein B-50 can no longer be regarded as a neuron-specific molecule.

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“…Spanish Phartnucwigdance Syjtem (Cantabrian Regional 2) and in regenerated nerve terminals [I, 31. Parhad and colleagues C41 recently reported that GAP-43 messenger RNA expression is increased two to four times in the anterior horn cells of the spinal cord of patients with amyotrophic lateral sclerosis (ALS).…”

Section: Clinical Pharmacology Unitmentioning

confidence: 99%

“…Although CNS adverse reactions have been reported after use of terfenadine products in adults 111, in controlled clinical studies, no significant difference between terfenadine and placebo in the incidence of these effects was found [2]. The lack of significant terfenadine penetration into the central nervous system (CNS) is probably responsible for its lack of CNS effects.…”

mentioning

confidence: 99%