title: Subcellular localization of phosphoprotein B-50 in regenerating muscle. An immuno-electron microscopic study.
abstract: Phosphoprotein B-50, also termed growth-associated protein GAP43, is a membrane-bound phosphoprotein expressed in neurons. It is particularly abundant during periods of axonal outgrowth in development and regeneration of the central and peripheral nervous systems. Recently the expression of phosphoprotein B-50 in regenerating muscle fibers was reported and it was assumed that phosphoprotein B-50, in muscles, plays a role in the determination of the growth morphology of regenerating muscle fibers. Thus, phosphoprotein B-50 no longer can be regarded as a neuron-specific molecule. In this paper we study the subcellular localization of phosphoprotein B-50 in regenerating human skeletal muscle fibers by electron immunohistochemistry. Phosphoprotein B-50 immunoreactivity is randomly distributed over the nuclear and perinuclear area of regenerating muscle fibers. Previously, by light-microscopy phosphoprotein B-50 immunoreactivity was demonstrated on the inner face of the sarcolemma in hypotrophic type 1 fibers in congenital fiber type disproportion. It is this distribution of phosphoprotein B-50 in developmentally disordered myocytes in particular which allows an analogy to the corresponding results found for growing axons. But we did not find subsarcolemmal expression of B-50 in regenerating muscle fibers. Probably this indicates that there is a difference in B-50 expression between regeneration of muscle fibers and developmentally retarded/immature myofibers. The presented data suggest that phosphoprotein B-50 is inserted only stage-dependent in the extending sarcolemma of the growing muscle fiber. Analogously to the nervous system, phosphoprotein B-50 may serve a local function involving transmembrane signalling by means of calmodulin binding of phosphoprotein B-50 and/or phosphoprotein B-50 phosphorylation and dephosphorylation.
authors.affiliation: Department of Neurology, Friedrich Alexander University of Erlangen-Nuremberg, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Heuss
authors.forename: U
authors.initials: U
authors.lastname: Schlötzer-Schrehardt
mesh_terms: D019922:GAP-43 Protein / Q000378:metabolism*; D006801:Humans; D016253:Microscopy, Immunoelectron; D018482:Muscle, Skeletal / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D012038:Regeneration / Q000502:physiology*; D013347:Subcellular Fractions / Q000378:metabolism*; D014018:Tissue Distribution
chemical_list: D019922:GAP-43 Protein